Information on EC 4.2.1.84 - nitrile hydratase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea

EC NUMBER
COMMENTARY
4.2.1.84
-
RECOMMENDED NAME
GeneOntology No.
nitrile hydratase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
an aliphatic amide = a nitrile + H2O
show the reaction diagram
light
-
-
-
an aliphatic amide = a nitrile + H2O
show the reaction diagram
N-771 and N-774 strains can be inactivated in the dark and reactivated by light
-
an aliphatic amide = a nitrile + H2O
show the reaction diagram
the activity of the enzyme in intact cells increases on light irradiation and gradually decreases in the dark. For purified enzyme no differences are detected when kept in dark or light-irradiated
-
an aliphatic amide = a nitrile + H2O
show the reaction diagram
the iron-type enzyme is photoreactive, it loses the catalytic activity through aerobic incubation in the dark and recovers it by light irradiation
-
an aliphatic amide = a nitrile + H2O
show the reaction diagram
substrate binding occurs via breathing and flip-flop mechanisms
-
an aliphatic amide = a nitrile + H2O
show the reaction diagram
monitoring of binding of substrates and their analogues to the active pocket via the NO bands
-
an aliphatic amide = a nitrile + H2O
show the reaction diagram
possible role of water and active center residues in reaction mechanism is shown
-
an aliphatic amide = a nitrile + H2O
show the reaction diagram
water dynamics and catalytic mechanism, a water molecule bound to the metal ion directly attacks the nitrile carbon, overview. Dynamics of the active site channel, NO diffusion paths, and water molecules positions are key components in the functioning of this important industrial enzyme
-
an aliphatic amide = a nitrile + H2O
show the reaction diagram
reaction mechanism, overview
-
an aliphatic amide = a nitrile + H2O
show the reaction diagram
reaction mechanism, first-shell mechanism of CoIII-NHase involving Tyr68 as catalytic base, deprotonated Tyr68 is proposed to abstract a proton from the nucleophilic water molecule, thus activating it for attack on the metal-bound substrate, modelling, detailed overview
-
an aliphatic amide = a nitrile + H2O
show the reaction diagram
first- and second-shell reaction mechanism, a tyrosine residue acts as catalytic base, modelling, detailed overview
-
an aliphatic amide = a nitrile + H2O
show the reaction diagram
modeling of the catalytic mechanism of nitrile hydratase by semi-empirical quantum mechanical calculation using the enzyme crystal structure, PDB code 1IRE, overview. Active site activation is the first step of NHase catalysis, in which the Co2+ coordinated to a water molecule forms a Co-OH complex mediated by the oxidized alpha-CEA113. Then the oxygen atom in the Co-OH attacks the C atom in the -CN triple bond of acrylonitrile, forming a precursor of acrylamide, proton rearrangement happens transforming the precursor into the final product of acrylamide, under the assistance of the hydrogen atom in the -OH group of alpha-Ser112
Q7SID2
an aliphatic amide = a nitrile + H2O
show the reaction diagram
thermal-stable mechanism of thermophilic nitrile hydratases, molecular dynamic simulation, overview
-
an aliphatic amide = a nitrile + H2O
show the reaction diagram
thermal-stable mechanism of thermophilic nitrile hydratases, molecular dynamic simulation, overview
Q7SID2
an aliphatic amide = a nitrile + H2O
show the reaction diagram
role of residues in the active site and enzymatic reaction mechanism. Cys146 acts as the nucleophile, Glu42 as the general base, Lys113/Glu42 as the general acid, WatA as the hydrolytic water and Nf_Lys113 and N_Phe147 form the oxyanion hole, hydrogen bonding network in the active site of Nit structure, overview
-
an aliphatic amide = a nitrile + H2O
show the reaction diagram
thermal-stable mechanism of thermophilic nitrile hydratases, molecular dynamic simulation, overview
Bacillus sp. SC-105-1
-
-
an aliphatic amide = a nitrile + H2O
show the reaction diagram
modeling of the catalytic mechanism of nitrile hydratase by semi-empirical quantum mechanical calculation using the enzyme crystal structure, PDB code 1IRE, overview. Active site activation is the first step of NHase catalysis, in which the Co2+ coordinated to a water molecule forms a Co-OH complex mediated by the oxidized alpha-CEA113. Then the oxygen atom in the Co-OH attacks the C atom in the -CN triple bond of acrylonitrile, forming a precursor of acrylamide, proton rearrangement happens transforming the precursor into the final product of acrylamide, under the assistance of the hydrogen atom in the -OH group of alpha-Ser112; possible role of water and active center residues in reaction mechanism is shown; reaction mechanism, first-shell mechanism of CoIII-NHase involving Tyr68 as catalytic base, deprotonated Tyr68 is proposed to abstract a proton from the nucleophilic water molecule, thus activating it for attack on the metal-bound substrate, modelling, detailed overview; reaction mechanism, overview
Pseudonocardia thermophila JCM 3095
-
-
an aliphatic amide = a nitrile + H2O
show the reaction diagram
thermal-stable mechanism of thermophilic nitrile hydratases, molecular dynamic simulation, overview
Pseudonocardia thermophila JCM3095
-
-
an aliphatic amide = a nitrile + H2O
show the reaction diagram
first- and second-shell reaction mechanism, a tyrosine residue acts as catalytic base, modelling, detailed overview
Rhodococcus erythropolis N-771
-
-
an aliphatic amide = a nitrile + H2O
show the reaction diagram
N-771 and N-774 strains can be inactivated in the dark and reactivated by light; the activity of the enzyme in intact cells increases on light irradiation and gradually decreases in the dark. For purified enzyme no differences are detected when kept in dark or light-irradiated
Rhodococcus sp. N-774
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
C-O bond cleavage by elimination of water
-
-
-
-
C-O bond cleavage by elimination of water
-
-
C-O bond cleavage by elimination of water
-
-
C-O bond cleavage by elimination of water
Pseudomonas chlororaphis B23
-
-
-
C-O bond cleavage by elimination of water
Rhodococcus rhodochrous J1
-
;
-
additional information
-
a new biocatalytic mechanism is proposed, that is based on crystallographic data of the active center
additional information
Rhodococcus erythropolis AJ270
-
a new biocatalytic mechanism is proposed, that is based on crystallographic data of the active center
-
PATHWAY
KEGG Link
MetaCyc Link
acrylonitrile degradation I
-
aldoxime degradation
-
Aminobenzoate degradation
-
Fluorobenzoate degradation
-
indole-3-acetate biosynthesis II
-
indole-3-acetate biosynthesis IV (bacteria)
-
Microbial metabolism in diverse environments
-
Styrene degradation
-
Tryptophan metabolism
-
SYSTEMATIC NAME
IUBMB Comments
aliphatic-amide hydro-lyase (nitrile-forming)
Acts on short-chain aliphatic nitriles, converting them into the corresponding amides. Does not act on these amides or on aromatic nitriles. cf. EC 3.5.5.1 nitrilase.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3-cyanopyridine hydratase
-
-
-
-
acrylonitrile hydratase
-
-
-
-
aliphatic nitrile hydratase
-
-
-
-
ANHase
-
acetonitrile hydratase
ANHase
Rhodococcus sp. RHA1
-
acetonitrile hydratase
-
Co-type NHase
Q7SID2
-
Co-type NHase
Pseudonocardia thermophila JCM 3095
Q7SID2
-
-
Co-type nitrile hydratase
-
-
Co-type nitrile hydratase
Pseudomonas putida NRRL-18668
-
-
-
CoIII-NHase
Pseudonocardia thermophila JCM 3095
-
-
-
CoIII-NHase
Rhodococcus erythropolis N-771
-
-
-
Fe-NHase
-
-
H-NHase
-
-
-
-
H-NHase
Rhodococcus rhodochrous J1
-
-
-
H-nitrilase
-
-
-
-
high-molecular mass nitrile hydratase
-
-
high-molecular mass nitrile hydratase
Rhodococcus rhodochrous J1
-
-
-
hydratase, nitrile
-
-
-
-
L-Nhase
-
-
-
-
L-Nhase
Rhodococcus fascians DSM43985
-
-
-
L-Nhase
Rhodococcus rhodochrous J1
-
-
-
L-nitrilase
-
-
-
-
low-molecular mass nitrile hydratase
-
-
low-molecular mass nitrile hydratase
Rhodococcus rhodochrous J1
-
-
-
NHase
-
-
-
-
NHase
Aeribacillus pallidus RAPc8
-
-
-
NHase
Alcaligenes faecalis CCTCC M 208168
-
-
-
NHase
-
-
NHase
Bacillus sp. SC-105-1
-
-
-
NHase
Bacillus subtilis CCTCC M 206038
-
-
-
NHase
Mesorhizobium sp.
-
-
NHase
Mesorhizobium sp. BNC1
-
-
-
NHase
Q8GJG6
-
NHase
Q8GJG6
-
-
NHase
Pseudonocardia thermophila JCM 3095
-, Q7SID2
-
-
NHase
Pseudonocardia thermophila JCM3095
Q7SID2
-
-
NHase
Rhodococcus boritolerans CCTCC M 208108
-
-
-
NHase
Rhodococcus equi TG328-2
-
-
-
NHase
Rhodococcus erythropolis AJ270
-
;
-
NHase
Rhodococcus erythropolis MTCC 1526, Rhodococcus erythropolis N4, Rhodococcus erythropolis N771
-
-
-
NHase
Rhodococcus qingshengii ZA0707
-
-
-
NHase
Rhodococcus rhodochrous PA-34
-
-
-
NHase
Rhodococcus ruber CCTCC M 206040, Rhodococcus ruber CGMCC3090
-
-
-
NHase
Rhodococcus sp. AJ270, Rhodococcus sp. N595
-
-
-
NHase
Rhodococcus sp. N771
-
;
-
NHase
Rhodococcus sp. RHA1, Rhodococcus sp. SHZ-1
-
-
-
NHase
Serratia marcescens CCTCC M 208231, Serratia marcescens ZJB-09104
-
-
-
NI1 NHase
-
-
-
-
nitrilase
-
-
-
-
nitrilase
-
-
nitrile hydratase
Comamonas oleophilus
-
-
nitrile hydratase
-
-
nitrile hydratase
no activity in Arabidopsis thaliana
-
-
nitrile hydratase
-
-
nitrile hydratase
Q8GJG6
-
nitrile hydratase
Nocardia sp. 108
-
-
-
nitrile hydratase
Q8GJG6
-
-
nitrile hydratase
-
-
nitrile hydratase
-
-
nitrile hydratase
Pseudonocardia thermophila JCM 3095
-
-
-
nitrile hydratase
Rhodococcus erythropolis AJ270
-
;
-
nitrile hydratase
-
-
nitrile hydratase
-
-
nitrile hydratase
Rhodococcus sp. AJ270, Rhodococcus sp. N771, Rhodococcus sp. RHA1, Rhodococcus sp. SHZ-1
-
-
-
nitrile hydratase
-
-
ppNHase
Pseudomonas putida NRRL-18668
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
82391-37-5
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
strain RAPc8
-
-
Manually annotated by BRENDA team
Aeribacillus pallidus RAPc8
strain RAPc8
-
-
Manually annotated by BRENDA team
Agrobacterium tumefaciens B-261
strain B-261
-
-
Manually annotated by BRENDA team
Agrobacterium tumefaciens IAM B-261
-
-
-
Manually annotated by BRENDA team
Alcaligenes faecalis CCTCC M 208168
-
-
-
Manually annotated by BRENDA team
strain J-1
-
-
Manually annotated by BRENDA team
Arthrobacter sp. J-1
strain J-1
-
-
Manually annotated by BRENDA team
alpha-subunit; strain SC-J05-1
E13931
EMBL
Manually annotated by BRENDA team
beta-subunit; strain SC-J05-1
E13932
EMBL
Manually annotated by BRENDA team
Bacillus smithii SC-J05-1
alpha-subunit; strain SC-J05-1
E13931
EMBL
Manually annotated by BRENDA team
Bacillus smithii SC-J05-1
beta-subunit; strain SC-J05-1
E13932
EMBL
Manually annotated by BRENDA team
strain DSM 2349
-
-
Manually annotated by BRENDA team
strain RAPc8, expression in Escherichia coli
-
-
Manually annotated by BRENDA team
strain SC-105-1
-
-
Manually annotated by BRENDA team
strain RAPc8, expression in Escherichia coli
-
-
Manually annotated by BRENDA team
Bacillus sp. SC-105-1
strain SC-105-1
-
-
Manually annotated by BRENDA team
Bacillus subtilis CCTCC M 206038
-
-
-
Manually annotated by BRENDA team
mutant strain ACV2; strain R312
-
-
Manually annotated by BRENDA team
Brevibacterium sp. R312
strain R312
-
-
Manually annotated by BRENDA team
Comamonas oleophilus
strain ATCC 15963
-
-
Manually annotated by BRENDA team
beta-subunit; strain 5-MGAM-4D, expression in Escherichia coli
Swissprot
Manually annotated by BRENDA team
Fe-dependent, wild-type nitrile hydratase is compared with artificial, Co-dependent nitrile hydratase
-
-
Manually annotated by BRENDA team
Comamonas testosteroni 5-MGAM-4D
beta-subunit; strain 5-MGAM-4D, expression in Escherichia coli
Swissprot
Manually annotated by BRENDA team
Corynebacterium nitrilophilus
-
-
-
Manually annotated by BRENDA team
Corynebacterium pseudodiphtheriticum ZBB-41
strain ZBB-41
-
-
Manually annotated by BRENDA team
strain N-774
-
-
Manually annotated by BRENDA team
Corynebacterium sp. C5
C5
-
-
Manually annotated by BRENDA team
Corynebacterium sp. N-774
strain N-774
-
-
Manually annotated by BRENDA team
Klebsiella oxytoca 38.1.2
-
-
-
Manually annotated by BRENDA team
Mesorhizobium loti 02-10055
-
-
-
Manually annotated by BRENDA team
Mesorhizobium loti 02-10056
-
-
-
Manually annotated by BRENDA team
Mesorhizobium loti 02-10101
-
-
-
Manually annotated by BRENDA team
Mesorhizobium sp.
strain F28, isolated from a wastewater treatment system in a polyacrylonitrile fibre factory
-
-
Manually annotated by BRENDA team
Mesorhizobium sp. BNC1
strain F28, isolated from a wastewater treatment system in a polyacrylonitrile fibre factory
-
-
Manually annotated by BRENDA team
strain CBS 498-74
-
-
Manually annotated by BRENDA team
Microbacterium imperiale CBS 498-74
-
-
-
Manually annotated by BRENDA team
Microbacterium imperiale CBS 498-74
strain CBS 498-74
-
-
Manually annotated by BRENDA team
no activity in Arabidopsis thaliana
strain CYP79A1, genetic modification
-
-
Manually annotated by BRENDA team
alpha-subunit; strain YS-2002
Swissprot
Manually annotated by BRENDA team
beta-subunit; strain YS-2002
Swissprot
Manually annotated by BRENDA team
strain 108
-
-
Manually annotated by BRENDA team
Nocardia sp. 108
strain 108
-
-
Manually annotated by BRENDA team
alpha-subunit; strain YS-2002
Swissprot
Manually annotated by BRENDA team
beta-subunit; strain YS-2002
Swissprot
Manually annotated by BRENDA team
strain ATCC 12485
-
-
Manually annotated by BRENDA team
Pseudomonas chlororaphis B23
B23
-
-
Manually annotated by BRENDA team
Pseudomonas chlororaphis B23
strain B23
-
-
Manually annotated by BRENDA team
strain 5B
-
-
Manually annotated by BRENDA team
strain NRRL-18668
-
-
Manually annotated by BRENDA team
Pseudomonas putida 5B
strain 5B
-
-
Manually annotated by BRENDA team
Pseudomonas putida NRRL-18668
-
-
-
Manually annotated by BRENDA team
Pseudomonas putida NRRL-18668
strain NRRL-18668
-
-
Manually annotated by BRENDA team
cobalt-containing subunit alpha; strain JCM3095
SwissProt
Manually annotated by BRENDA team
strain JCM 3095
SwissProt
Manually annotated by BRENDA team
Pseudonocardia thermophila JCM 3095
strain JCM 3095
-
-
Manually annotated by BRENDA team
Pseudonocardia thermophila JCM 3095
strain JCM 3095
SwissProt
Manually annotated by BRENDA team
Pseudonocardia thermophila JCM3095
cobalt-containing subunit alpha; strain JCM3095
SwissProt
Manually annotated by BRENDA team
gene nit-30
-
-
Manually annotated by BRENDA team
Raoultella terrigena 77.1
-
-
-
Manually annotated by BRENDA team
Rhizobium leguminosarum 02-03119
-
-
-
Manually annotated by BRENDA team
Rhizobium leguminosarum 02-10041
-
-
-
Manually annotated by BRENDA team
Rhizobium leguminosarum 02-10230
-
-
-
Manually annotated by BRENDA team
Rhodococcus boritolerans CCTCC M 208108
-
-
-
Manually annotated by BRENDA team
strain TG328-2
-
-
Manually annotated by BRENDA team
Rhodococcus equi TG328-2
strain TG328-2
-
-
Manually annotated by BRENDA team
alpha subunit; recombinant enzyme
Q7AZY7
Swissprot
Manually annotated by BRENDA team
strain 870-AN019, expression of enzyme in Escherichia coli
-
-
Manually annotated by BRENDA team
strain AJ270
-
-
Manually annotated by BRENDA team
strain AJ270, origin of genes encoding NHase (nha1 and nha2) and P44k protein (nha3)
-
-
Manually annotated by BRENDA team
strain ATCC 25544
-
-
Manually annotated by BRENDA team
strain MTCC 1526
-
-
Manually annotated by BRENDA team
strain N-771
-
-
Manually annotated by BRENDA team
Rhodococcus erythropolis 870-AN019
strain 870-AN019, expression of enzyme in Escherichia coli
-
-
Manually annotated by BRENDA team
Rhodococcus erythropolis A4
-
-
-
Manually annotated by BRENDA team
Rhodococcus erythropolis AJ270
strain AJ270
-
-
Manually annotated by BRENDA team
Rhodococcus erythropolis AJ270
strain AJ270, origin of genes encoding NHase (nha1 and nha2) and P44k protein (nha3)
-
-
Manually annotated by BRENDA team
Rhodococcus erythropolis MTCC 1526
-
-
-
Manually annotated by BRENDA team
Rhodococcus erythropolis MTCC 1526
strain MTCC 1526
-
-
Manually annotated by BRENDA team
Rhodococcus erythropolis N-771
strain N-771
-
-
Manually annotated by BRENDA team
Rhodococcus erythropolis N4
strain N4
-
-
Manually annotated by BRENDA team
Rhodococcus erythropolis N771
strain N771
-
-
Manually annotated by BRENDA team
strain DSM43985
-
-
Manually annotated by BRENDA team
Rhodococcus fascians DSM43985
strain DSM43985
-
-
Manually annotated by BRENDA team
alpha-subunit; strain MW3
Swissprot
Manually annotated by BRENDA team
beta-subunit; strain MW3
Swissprot
Manually annotated by BRENDA team
strain S85-2, enzyme activity is induced by acetonitrile, acetamide, propionamide, urea
-
-
Manually annotated by BRENDA team
Rhodococcus pyridinivorans MW3
alpha-subunit; strain MW3
Swissprot
Manually annotated by BRENDA team
Rhodococcus pyridinivorans MW3
beta-subunit; strain MW3
Swissprot
Manually annotated by BRENDA team
Rhodococcus pyridinivorans S82-2
strain: S82-2
-
-
Manually annotated by BRENDA team
Rhodococcus pyridinivorans S85-2
strain S85-2, enzyme activity is induced by acetonitrile, acetamide, propionamide, urea
-
-
Manually annotated by BRENDA team
Rhodococcus qingshengii ZA0707
-
-
-
Manually annotated by BRENDA team
J1; strain J1
-
-
Manually annotated by BRENDA team
strain ATCC 12674; strain ATCC 33278
-
-
Manually annotated by BRENDA team
strain IFO 15564
-
-
Manually annotated by BRENDA team
strain J1, 2 kinds of enzyme, a high molecular mass: H-NHase, and a low molecular mass enzyme: L-NHase
-
-
Manually annotated by BRENDA team
strain NCIMB 11216
-
-
Manually annotated by BRENDA team
strain PA-34
-
-
Manually annotated by BRENDA team
Rhodococcus rhodochrous IFO 15564
strain IFO 15564
-
-
Manually annotated by BRENDA team
Rhodococcus rhodochrous J1
-
-
-
Manually annotated by BRENDA team
Rhodococcus rhodochrous J1
J1
-
-
Manually annotated by BRENDA team
Rhodococcus rhodochrous J1
J1; strain J1
-
-
Manually annotated by BRENDA team
Rhodococcus rhodochrous J1
strain J1
-
-
Manually annotated by BRENDA team
Rhodococcus rhodochrous J1
strain J1, 2 kinds of enzyme, a high molecular mass: H-NHase, and a low molecular mass enzyme: L-NHase
-
-
Manually annotated by BRENDA team
Rhodococcus rhodochrous NCIMB 11216
strain NCIMB 11216
-
-
Manually annotated by BRENDA team
Rhodococcus rhodochrous PA-34
strain PA-34
-
-
Manually annotated by BRENDA team
; strain TH
-
-
Manually annotated by BRENDA team
strain CGMCC3090
-
-
Manually annotated by BRENDA team
Rhodococcus ruber CCTCC M 206040
-
-
-
Manually annotated by BRENDA team
Rhodococcus ruber CGMCC3090
strain CGMCC3090
-
-
Manually annotated by BRENDA team
Rhodococcus ruber TH
; strain TH
-
-
Manually annotated by BRENDA team
strain 7
-
-
Manually annotated by BRENDA team
strain 7; strain N-774
-
-
Manually annotated by BRENDA team
strain AJ270
-
-
Manually annotated by BRENDA team
strain ATCC BAA-869; strain ATCC BAA-870; strain DSM 44519; strain Novo SP361
-
-
Manually annotated by BRENDA team
strain J1
-
-
Manually annotated by BRENDA team
strain N-771; strain N-774
-
-
Manually annotated by BRENDA team
strain N-774
-
-
Manually annotated by BRENDA team
strain N-774; strain R312
-
-
Manually annotated by BRENDA team
strain N771
-
-
Manually annotated by BRENDA team
strain RHA1
-
-
Manually annotated by BRENDA team
strain SHZ-1
-
-
Manually annotated by BRENDA team
strains R312 and N771
-
-
Manually annotated by BRENDA team
Rhodococcus sp. 7
strain 7
-
-
Manually annotated by BRENDA team
strain AJ270
-
-
Manually annotated by BRENDA team
Rhodococcus sp. J1
strain J1
-
-
Manually annotated by BRENDA team
Rhodococcus sp. N-774
strain N-774
-
-
Manually annotated by BRENDA team
Rhodococcus sp. N595
-
-
-
Manually annotated by BRENDA team
Rhodococcus sp. N771
strain N771
-
-
Manually annotated by BRENDA team
Rhodococcus sp. Novo SP361
strain Novo SP361
-
-
Manually annotated by BRENDA team
strain R312
-
-
Manually annotated by BRENDA team
Rhodococcus sp. RHA1
strain RHA1
-
-
Manually annotated by BRENDA team
Rhodococcus sp. SHZ-1
strain SHZ-1
-
-
Manually annotated by BRENDA team
; strain CGA009
-
-
Manually annotated by BRENDA team
strain ZJB-09104
-
-
Manually annotated by BRENDA team
Serratia marcescens CCTCC M 208231
-
-
-
Manually annotated by BRENDA team
Serratia marcescens ZJB-09104
strain ZJB-09104
-
-
Manually annotated by BRENDA team
Sinorhizobium meliloti 03-03046
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
incorporation of cobalt into L-NHase in a mode of post-translational maturation, i.e. self-subunit swapping. NhlE is recognized as a self-subunit swapping chaperone, mechanism, detailed overview
additional information
Rhodococcus rhodochrous J1
-
incorporation of cobalt into L-NHase in a mode of post-translational maturation, i.e. self-subunit swapping. NhlE is recognized as a self-subunit swapping chaperone, mechanism, detailed overview
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(1R,3R)-2,2-dibromo-3-phenylcyclopropanecarbonitrile + H2O
(1R,3R)-2,2-dibromo-3-phenylcyclopropanecarbamide
show the reaction diagram
-
substrate conversion: 11.6%, enantiomeric excess: 83.8, 88.9 (methanol), 81.0 (n-hexane)
-
-
r
(1R,3R)-3-phenylcyclopropanecarbonitrile + H2O
(1R,3R)-3-phenylcyclopropanecarbamide
show the reaction diagram
-
substrate conversion: 49.1%, enantiomeric excess: 22.7, 31.1 (methanol), 21.6 (n-hexane)
-
-
r
(1R,3S)-3-phenylcyclopropanecarbonitrile + H2O
(1R,3S)-3-phenylcyclopropanecarbamide
show the reaction diagram
-
substrate conversion: 25.8%, enantiomeric excess: 95.4, 95.4 (methanol), 95.5 (n-hexane)
-
-
r
(1S,3S)-2,2-dimethyl-3-phenylcyclopropanecarbonitrile + H2O
(1S,3S)-2,2-dimethyl-3-phenylcyclopropanecarbamide
show the reaction diagram
-
substrate conversion: 40.3%, enantiomeric excess: 84.7, substrate conversion: 7.9%, enantiomeric excess: 3.2, 5.9 (methanol), 0.7 (n-hexane)
-
-
r
(2R)-2-hydroxy-3-methylbutanenitrile + H2O
(2R)-2-hydroxy-3-methylbutanamide
show the reaction diagram
-
-
-
-
?
(2R)-2-hydroxybut-3-enenitrile + H2O
(2R)-2-hydroxybut-3-enamide
show the reaction diagram
-
-
-
-
?
(2R)-2-hydroxybutanenitrile + H2O
(2R)-2-hydroxybutanamide
show the reaction diagram
-
-
-
-
?
(2R)-2-hydroxyhexanenitrile + H2O
(2R)-2-hydroxyhexanamide
show the reaction diagram
-
-
-
-
?
(2R)-2-hydroxypentanenitrile + H2O
(2R)-2-hydroxypentanamide
show the reaction diagram
-
-
-
-
?
(R)-2-chloromandelonitrile + H2O
(R)-2-chloromandelamide
show the reaction diagram
Q7AZY7
at 100% the rate of 2-hydroxy-4-phenylbutyronitrile
-
-
?
(R,S)-2-(4-nitrophenyl)-propionitrile + H2O
?
show the reaction diagram
-
39% conversion
-
-
?
(R,S)-2-bromopropionitrile + H2O
?
show the reaction diagram
-
47% conversion
-
-
?
(R,S)-2-chloropropionitrile + H2O
?
show the reaction diagram
-
48% conversion
-
-
?
(R,S)-2-phenylbutyronitrile + H2O
?
show the reaction diagram
-
51% conversion
-
-
?
(R,S)-2-phenylpropionitrile + H2O
?
show the reaction diagram
-
43% conversion
-
-
?
(R,S)-3-oxo-2-phenylbutyronitrile + H2O
?
show the reaction diagram
-
43% conversion
-
-
?
(S)-3-benzoyloxypentanedinitrile + H2O
3-amino-1-(2-amino-2-oxoethyl)-3-oxopropyl benzoate
show the reaction diagram
-
substrate conversion: 38.5%, enantiomeric excess: 68.2
-
-
r
1,1,3,3,-tetramethylbutylisonitrile + H2O
1,1,3,3,-tetramethylisobutylamide
show the reaction diagram
Rhodococcus sp., Rhodococcus sp. N771
-
-
-
-
?
1-(4-bromo-phenyl)-aziridine-2-carbonitrile + H2O
1-(4-bromophenyl)aziridine-2-carboxamide
show the reaction diagram
-
-
-
-
r
1-(4-methoxy-phenyl)-aziridine-2-carbonitrile + H2O
1-(4-methoxyphenyl)aziridine-2-carboxamide
show the reaction diagram
-
-
-
-
r
1-naphthylnitrile + H2O
1-naphthylamide
show the reaction diagram
Rhodococcus rhodochrous, Rhodococcus rhodochrous IFO 15564
-
-
-
-
?
17alpha-cyanomethyl-17beta-hydroxy-estra-4,9-dien-3-one + H2O
17alpha-acetamido-estra-1,3,5(10),9(11)-tetraene-3,17beta-diol
show the reaction diagram
-
the steroidal group is metabolized very slowly
-
?
2(R)-(4-chlorophenyl)-3-methylbutyronitrile + H2O
2(R)-(4-chloro-phenyl)-3-methyl-butyramide
show the reaction diagram
Pseudomonas putida, Pseudomonas putida 5B
-
enantioselective hydration
-
?
2(S)-(4-chlorophenyl)-3-methylbutyronitrile + H2O
2(S)-(4-chloro-phenyl)-3-methyl-butyramide
show the reaction diagram
-
-
-
?
2(S)-(4-chlorophenyl)-3-methylbutyronitrile + H2O
2(S)-(4-chloro-phenyl)-3-methyl-butyramide
show the reaction diagram
-
-
-
?
2(S)-(4-chlorophenyl)-3-methylbutyronitrile + H2O
2(S)-(4-chloro-phenyl)-3-methyl-butyramide
show the reaction diagram
Pseudomonas putida, Pseudomonas putida NRRL-18668
-
enantioselective hydration
-
?
2(S)-(4-chlorophenyl)-3-methylbutyronitrile + H2O
2(S)-(4-chloro-phenyl)-3-methyl-butyramide
show the reaction diagram
Pseudomonas putida 5B
-
-
-
?
2,2-dimethylcyclopropanecarbonitrile + H2O
2,2-dimethylcyclopropanecarboxamide
show the reaction diagram
-
-
-
-
?
2,2-dimethylcyclopropanecarbonitrile + H2O
2,2-dimethylcyclopropanecarbamide
show the reaction diagram
Rhodococcus qingshengii, Rhodococcus qingshengii ZA0707
-
-
-
-
?
2,3,4,5,6-pentafluorobenzonitrile + H2O
2,3,4,5,6-pentafluorobenzamide
show the reaction diagram
-
-
-
-
?
2,3-dihydro-benzo(1,4)dioxine-2-carbonitrile + H2O
2,3-dihydro-1,4-benzodioxine-2-carboxamide
show the reaction diagram
-
substrate conversion: 45.1%, enantiomeric excess: 0
-
-
r
2,6-difluorobenzonitrile + H2O
2,6-difluorobenzamide
show the reaction diagram
-
-
-
-
?
2-amino-2,3-dimethylbutyronitrile + H2O
2-amino-2,3-dimethylbutyramide
show the reaction diagram
-
-
-
-
?
2-amino-2,3-dimethylbutyronitrile + H2O
2-amino-2,3-dimethylbutyramide
show the reaction diagram
-
-
-
-
?
2-amino-2,3-dimethylbutyronitrile + H2O
2-amino-2,3-dimethylbutyramide
show the reaction diagram
Rhodococcus boritolerans, Rhodococcus boritolerans CCTCC M 208108, Bacillus subtilis CCTCC M 206038, Alcaligenes faecalis CCTCC M 208168, Rhodococcus ruber CCTCC M 206040, Serratia marcescens CCTCC M 208231, Rhodococcus sp. N595
-
-
-
-
?
2-aminopropionitrile + H2O
2-aminopropionic acid amide
show the reaction diagram
-
90% of the activity with propionitrile
-
-
?
2-bromobenzonitrile + H2O
2-bromobenzamide
show the reaction diagram
-
-
-
-
ir
2-chlorobenzaldehyde + HCN + H2O
(R)-2-chloromandelonitrile
show the reaction diagram
-
-
90% conversion to alpha-hydroxy nitrile
-
?
2-chlorobenzonitrile + H2O
2-chlorobenzamide
show the reaction diagram
-
-
-
-
ir
2-cyanopyridine + H2O
pyridine-2-carbamide
show the reaction diagram
-
-
-
-
?
2-cyanopyridine + H2O
pyridine-2-carbamide
show the reaction diagram
-
-
-
-
?
2-cyanopyridine + H2O
pyridine-2-carbamide
show the reaction diagram
Aeribacillus pallidus, Aeribacillus pallidus RAPc8
-
-
-
-
?
2-cyanopyridine + H2O
pyridine-2-carbamide
show the reaction diagram
Serratia marcescens ZJB-09104
-
-
-
-
?
2-fluorobenzaldehyde + HCN + H2O
? + H2O
show the reaction diagram
-
-
100% conversion to alpha-hydroxy nitrile
-
?
2-fluorobenzonitrile + H2O
2-fluorobenzamide
show the reaction diagram
-
-
-
-
ir
2-furonitrile + H2O
2-furoamide
show the reaction diagram
Rhodococcus rhodochrous, Rhodococcus rhodochrous IFO 15564
-
-
-
-
?
2-hydroxy-4-phenylbutyronitrile + H2O
2-hydroxy-4-phenylbutyramide
show the reaction diagram
Q7AZY7
-
-
-
?
2-hydroxymethyl-3-phenyl-propionitrile + H2O
2-benzyl-3-hydroxypropanamide
show the reaction diagram
-
-
-
-
r
2-hydroxypropionitrile + H2O
2-hydroxypropionic acid amide
show the reaction diagram
-
i.e. DL-lactonitrile, 116% of the activity with propionitrile
-
-
?
2-methoxybenzonitrile + H2O
2-methoxybenzamide
show the reaction diagram
-
-
-
-
ir
2-methoxymethyl-3-phenyl-propionitrile + H2O
2-benzyl-3-methoxypropanamide
show the reaction diagram
-
-
-
-
r
2-methyl-3-butenenitrile + H2O
?
show the reaction diagram
-
-
-
-
?
2-methylbenzonitrile + H2O
2-methylbenzamide
show the reaction diagram
-
-
-
-
ir
2-naphthylacetonitrile + H2O
2-naphthylacetamide
show the reaction diagram
Rhodococcus rhodochrous, Rhodococcus rhodochrous IFO 15564
-
-
-
-
?
2-nitro-5-thiocyanato-benzoic acid + H2O
?
show the reaction diagram
-
-
-
-
?
2-nitrobenzaldehyde + HCN + H2O
? + H2O
show the reaction diagram
-
-
20% conversion to alpha-hydroxy nitrile
-
?
2-phenylacetonitrile + H2O
2-phenylpropionamide
show the reaction diagram
-
-
-
-
?
2-phenylbutyronitrile + H2O
2-phenylbutyramide
show the reaction diagram
-
used as well as phenylacetonitrile
-
-
?
2-phenylglycinonitrile + H2O
aminoacetamide
show the reaction diagram
-
used as well as phenylacetonitrile
-
-
?
2-phenylpropionitrile + H2O
2-phenylpropionamide
show the reaction diagram
-
-
-
-
?
2-phenylpropionitrile + H2O
2-phenylpropionamide
show the reaction diagram
-
used as well as phenylacetonitrile
-
-
?
2-phenylpropionitrile + H2O
2-phenylpropionamide
show the reaction diagram
Rhodococcus sp. Novo SP361
-
-
-
-
?
3,4,5-trimethoxybenzonitrile + H2O
3,4,5-trimethoxybenzamide
show the reaction diagram
Nocardia sp., Nocardia sp. 108
-
conversion rate: 21.71%
-
-
?
3,4-dimethoxybenzonitrile + H2O
3,4-dimethoxybenzaldehyde
show the reaction diagram
Rhodococcus sp., Rhodococcus sp. Novo SP361
-
-
-
-
?
3,4-dimethoxybenzonitrile + H2O
3,4-dimethoxybenzaldehyde + HCN
show the reaction diagram
Rhodococcus sp., Rhodococcus sp. Novo SP361
-
-
-
-
?
3-(trifluoromethyl)benzonitrile + H2O
3-(trifluoromethyl)benzamide
show the reaction diagram
-
5% conversion, in phosphate buffer pH 7.0, at 30C
-
-
?
3-(trifluoromethyl)pyridine-4-carbonitrile + H2O
3-(trifluoromethyl)pyridine-4-carboxamide
show the reaction diagram
-
-
-
-
ir
3-allyloxy-4-phenyl-butyronitrile + H2O
4-phenyl-3-(prop-2-en-1-yloxy)butanamide
show the reaction diagram
-
-
-
-
r
3-aminopropionitrile + H2O
3-aminopropionic acid amide
show the reaction diagram
-
2.7% of the activity with propionitrile
-
-
?
3-benzoyloxyglutaronitrile + H2O
(S)-3-benzoyloxy-4-cyanobutyramide
show the reaction diagram
Rhodococcus erythropolis, Rhodococcus erythropolis AJ270
-
enantiomeric excess: 95%, 5 h
-
-
?
3-benzyloxy-3-vinyl-propionitrile + H2O
3-(benzyloxy)pent-4-enamide
show the reaction diagram
-
-
-
-
r
3-benzyloxy-pentanonitrile + H2O
3-(benzyloxy)pentanamide
show the reaction diagram
-
-
-
-
r
3-benzyloxyglutaronitrile + H2O
3-benzyloxy-4-cyanobutyramide
show the reaction diagram
Rhodococcus erythropolis, Rhodococcus erythropolis AJ270
-
enantiomeric excess: 69%, 30 min
-
-
?
3-bromobenzonitrile + H2O
3-bromobenzamide
show the reaction diagram
-
5% conversion, in phosphate buffer pH 7.0, at 30C
-
-
?
3-chlorobenzaldehyde + HCN + H2O
? + H2O
show the reaction diagram
-
-
100% conversion to alpha-hydroxy nitrile
-
?
3-chlorobenzonitrile + H2O
3-chlorobenzamide
show the reaction diagram
-
-
-
-
?
3-chlorobenzonitrile + H2O
3-chlorobenzamide
show the reaction diagram
-
95% conversion, in phosphate buffer pH 7.0, at 30C
-
-
?
3-cyanopyridine + H2O
pyridine-3-carbamide
show the reaction diagram
-
-
-
-
?
3-cyanopyridine + H2O
pyridine-3-carbamide
show the reaction diagram
-
-
-
-
3-cyanopyridine + H2O
pyridine-3-carbamide
show the reaction diagram
-
-
-
-
3-cyanopyridine + H2O
pyridine-3-carbamide
show the reaction diagram
-
-
-
-
?
3-cyanopyridine + H2O
pyridine-3-carbamide
show the reaction diagram
-
-
-
-
?
3-cyanopyridine + H2O
pyridine-3-carbamide
show the reaction diagram
-
-
-
-
?
3-cyanopyridine + H2O
pyridine-3-carbamide
show the reaction diagram
-
-
-
-
?
3-cyanopyridine + H2O
pyridine-3-carbamide
show the reaction diagram
-
-
i.e. nicotinamide
?
3-cyanopyridine + H2O
pyridine-3-carbamide
show the reaction diagram
-
-
i.e. nicotinamide
?
3-cyanopyridine + H2O
pyridine-3-carbamide
show the reaction diagram
-
-
i.e. nicotinamide
?
3-cyanopyridine + H2O
pyridine-3-carbamide
show the reaction diagram
-
-
i.e. nicotinamide
?
3-cyanopyridine + H2O
pyridine-3-carbamide
show the reaction diagram
-
-
i.e. nicotinamide
-
3-cyanopyridine + H2O
pyridine-3-carbamide
show the reaction diagram
Aeribacillus pallidus RAPc8
-
-
-
-
?
3-cyanopyridine + H2O
pyridine-3-carbamide
show the reaction diagram
Rhodococcus sp. N-774
-
-
-
-
3-cyanopyridine + H2O
pyridine-3-carbamide
show the reaction diagram
Rhodococcus ruber CGMCC3090
-
-
-
-
?
3-cyanopyridine + H2O
pyridine-3-carbamide
show the reaction diagram
Rhodococcus fascians DSM43985
-
-
-
-
?
3-cyanopyridine + H2O
pyridine-3-carbamide
show the reaction diagram
-
-
-
-
3-cyanopyridine + H2O
pyridine-3-carbamide
show the reaction diagram
Rhodococcus rhodochrous PA-34
-
-
-
-
?
3-cyanopyridine + H2O
pyridine-3-carbamide
show the reaction diagram
Rhodococcus rhodochrous J1
-
-
i.e. nicotinamide
?
3-cyanopyridine + H2O
nicotinamide
show the reaction diagram
-
-
-
-
-
3-cyanopyridine + H2O
nicotinamide
show the reaction diagram
-
-
-
-
?
3-cyanopyridine + H2O
nicotinamide
show the reaction diagram
-
-
-
-
?
3-cyanopyridine + H2O
nicotinamide
show the reaction diagram
-
a step in the biosynthesis of nicotinamide, one of the important forms of vitamin B3
-
-
?
3-cyanopyridine + H2O
nicotinamide
show the reaction diagram
-
NHase-AMase cascade system exploited in a continuous reactor configuration, including nitrile hydratase and amidase, EC 3.5.1.4, activity. Bioconversion to intermediate nicotinamide and further to nicotinic acid
-
-
?
3-cyanopyridine + H2O
nicotinamide
show the reaction diagram
-
H-NHase activity
-
-
?
3-cyanopyridine + H2O
nicotinamide
show the reaction diagram
Rhodococcus erythropolis MTCC 1526
-
-
-
-
?
3-cyanopyridine + H2O
nicotinamide
show the reaction diagram
Rhodococcus erythropolis MTCC 1526
-
a step in the biosynthesis of nicotinamide, one of the important forms of vitamin B3
-
-
?
3-cyanopyridine + H2O
nicotinamide
show the reaction diagram
Microbacterium imperiale CBS 498-74
-
-, NHase-AMase cascade system exploited in a continuous reactor configuration, including nitrile hydratase and amidase, EC 3.5.1.4, activity. Bioconversion to intermediate nicotinamide and further to nicotinic acid
-
-
?
3-cyanopyridine + H2O
nicotinamide
show the reaction diagram
Microbacterium imperiale CBS 498-74
-
-, NHase-AMase cascade system exploited in a continuous reactor configuration, including nitrile hydratase and amidase, EC 3.5.1.4, activity. Bioconversion to intermediate nicotinamide and further to nicotinic acid
-
-
?
3-cyanopyridine + H2O
nicotinamide
show the reaction diagram
Rhodococcus rhodochrous J1
-
H-NHase activity
-
-
?
3-cyanopyridine + H2O
nicotinamide
show the reaction diagram
Rhodococcus rhodochrous J1
-
-
-
-
-
3-cyanopyridine + H2O
pyridine-3-carboxamide
show the reaction diagram
Nocardia sp., Nocardia sp. 108
-
-
-
-
?
3-fluorobenzonitrile + H2O
3-fluorobenzamide
show the reaction diagram
-
above 99.9% conversion, in phosphate buffer pH 7.0, at 30C
-
-
?
3-hydroxy-3-phenylpropionitrile + H2O
3-hydroxy-3-phenylpropionamide
show the reaction diagram
-
-
-
-
?
3-hydroxybenzonitrile + H2O
3-hydroxybenzamide
show the reaction diagram
-
-
-
-
?
3-hydroxybutryronitrile + H2O
3-hydroxybutyramide
show the reaction diagram
Comamonas testosteroni, Comamonas testosteroni 5-MGAM-4D
Q5XPL4
-
yield 99%
-
?
3-hydroxypropionitrile + H2O
3-hydroxypropionic acid amide
show the reaction diagram
-
35% of the activity with propionitrile
-
-
?
3-hydroxypropionitrile + H2O
3-hydroxypropionamide
show the reaction diagram
Comamonas testosteroni, Comamonas testosteroni 5-MGAM-4D
Q5XPL4
-
yield 100%
-
?
3-hydroxyvaleronitrile + H2O
3-hydroxyvaleramide
show the reaction diagram
Comamonas testosteroni, Comamonas testosteroni 5-MGAM-4D
Q5XPL4
-
yield 99%
-
?
3-methoxybenzonitrile + H2O
3-methoxybenzamide
show the reaction diagram
-
3% conversion, in phosphate buffer pH 7.0, at 30C
-
-
?
3-methylbenzonitrile + H2O
3-methylbenzamide
show the reaction diagram
-
17% conversion, in phosphate buffer pH 7.0, at 30C
-
-
?
3-phenoxymandelonitrile + H2O
3-phenoxymandelamine
show the reaction diagram
Q7AZY7
at 10% the rate of 2-hydroxy-4-phenylbutyronitrile
-
-
?
3-phenylpropanenitrile + H2O
3-phenylpropanamide
show the reaction diagram
-
-
-
-
ir
3-phenylpropanenitrile + H2O
3-phenylpropanamide
show the reaction diagram
-
99.9% conversion, in phosphate buffer pH 7.0, at 30C
-
-
?
3-phenylpropionitrile + H2O
3-phenylpropionamide
show the reaction diagram
-
used as well as phenylacetonitrile
-
-
?
3-tolunitrile + H2O
?
show the reaction diagram
-
-
-
-
?
4-(trifluoromethyl)benzonitrile + H2O
4-(trifluoromethyl)benzamide
show the reaction diagram
-
-
-
-
ir
4-(trifluoromethyl)benzonitrile + H2O
4-(trifluoromethyl)benzamide
show the reaction diagram
-
above 99.9% conversion, in phosphate buffer pH 7.0, at 30C
-
-
?
4-acetylbenzonitrile + H2O
4-acetylbenzamide
show the reaction diagram
-
-
-
-
ir
4-acetylbenzonitrile + H2O
4-acetylbenzamide
show the reaction diagram
-
above 99% conversion, in phosphate buffer pH 7.0, at 30C
-
-
?
4-aminobenzonitrile + H2O
4-aminobenzamide
show the reaction diagram
-
-
-
-
?
4-bromobenzonitrile + H2O
4-bromobenzonitrile
show the reaction diagram
-
above 99% conversion, in phosphate buffer pH 7.0, at 30C
-
-
?
4-bromobenzonitrile + H2O
4-bromobenzamide
show the reaction diagram
-
-
-
-
ir
4-chloro-3-hydroxybutyronitrile + H2O
4-chloro-3-hydroxybutyramide
show the reaction diagram
-
the following reaction by an amidase leads to the correspondend carboxylic acid
-
-
?
4-chlorobenzaldehyde + HCN + H2O
? + H2O
show the reaction diagram
-
-
100% conversion to alpha-hydroxy nitrile
-
?
4-chlorobenzonitrile + H2O
4-chlorobenzamide
show the reaction diagram
-
-
-
-
?
4-chlorobenzonitrile + H2O
4-chlorobenzamide
show the reaction diagram
-
above 99.9% conversion, in phosphate buffer pH 7.0, at 30C
-
-
?
4-chlorobenzonitrile + H2O
4-chlorbenzamide
show the reaction diagram
-
-
-
-
ir
4-cyanobenzaldehyde + HCN + H2O
? + H2O
show the reaction diagram
-
-
100% conversion to alpha-hydroxy nitrile
-
?
4-cyanobenzoic acid + H2O
4-(aminocarbonyl)benzoic acid
show the reaction diagram
-
-
-
-
?
4-cyanopyridine + H2O
pyridine-4-carbamide
show the reaction diagram
-
-
-
-
?
4-cyanopyridine + H2O
pyridine-4-carbamide
show the reaction diagram
Aeribacillus pallidus, Aeribacillus pallidus RAPc8
-
-
-
-
?
4-fluorobenzonitrile + H2O
4-fluorobenzamide
show the reaction diagram
-
above 99.9% conversion, in phosphate buffer pH 7.0, at 30C
-
-
?
4-fluorobenzonitrile + H2O
4-fluorbenzamide
show the reaction diagram
-
-
-
-
ir
4-hydroxybenzaldehyde + HCN + H2O
? + H2O
show the reaction diagram
-
-
55% conversion to alpha-hydroxy nitrile
-
?
4-hydroxybenzonitrile + H2O
4-hydroxybenzoic acid amide
show the reaction diagram
-
-
-
-
?
4-hydroxybenzonitrile + H2O
4-hydroxybenzoic acid amide
show the reaction diagram
-
-
-
-
?
4-hydroxybenzonitrile + H2O
4-hydroxybenzoic acid amide
show the reaction diagram
-
-
-
-
?
4-hydroxybenzonitrile + H2O
4-hydroxybenzamide
show the reaction diagram
-
-
-
-
?
4-hydroxyphenylacetonitrile + H2O
4-hydroxyphenylacetamide
show the reaction diagram
-
-
-
-
?
4-hydroxyphenylacetonitrile + H2O
4-hydroxyphenylacetamide
show the reaction diagram
-
-
-
-
?
4-methoxybenzonitrile + H2O
4-methoxybenzamide
show the reaction diagram
-
-
-
-
ir
4-methoxybenzonitrile + H2O
4-methoxybenzamide
show the reaction diagram
-
above 99% conversion, in phosphate buffer pH 7.0, at 30C
-
-
?
4-methylbenzaldehyde + HCN + H2O
? + H2O
show the reaction diagram
-
-
51% conversion to alpha-hydroxy nitrile
-
?
4-methylbenzonitrile + H2O
4-methylbenzamide
show the reaction diagram
-
-
-
-
ir
4-methylbenzonitrile + H2O
4-methylbenzamide
show the reaction diagram
-
above 99.9% conversion, in phosphate buffer pH 7.0, at 30C
-
-
?
4-methylmandelonitrile + H2O
4-methylmandelamine
show the reaction diagram
Q7AZY7
at 60% the rate of 2-hydroxy-4-phenylbutyronitrile
-
-
?
4-nitrobenzaldehyde + HCN + H2O
? + H2O
show the reaction diagram
-
-
100% conversion to alpha-hydroxy nitrile
-
?
5-cyanovaleric acid + H2O
6-amino-6-oxohexanoic acid
show the reaction diagram
-
NilFe and NilCo
-
-
r
5-hydroxymethyl-2-furonitrile + H2O
5-hydroxymethyl-2-furamide
show the reaction diagram
Rhodococcus rhodochrous, Rhodococcus rhodochrous IFO 15564
-
-
-
-
?
acetonitrile + H2O
acetamide
show the reaction diagram
-
-
-
-
?
acetonitrile + H2O
acetamide
show the reaction diagram
-
-
-
-
?
acetonitrile + H2O
acetamide
show the reaction diagram
-
-
-
-
-
acetonitrile + H2O
acetamide
show the reaction diagram
-
-
-
ir
acetonitrile + H2O
acetamide
show the reaction diagram
-
-
-
-
?
acetonitrile + H2O
acetamide
show the reaction diagram
-
-
-
-
r
acetonitrile + H2O
acetamide
show the reaction diagram
-
-
-
-
?
acetonitrile + H2O
acetamide
show the reaction diagram
-
very low activity
-
-
?
acetonitrile + H2O
acetamide
show the reaction diagram
-
best substrate
-
-
?
acetonitrile + H2O
acetamide
show the reaction diagram
-
79% of the activity with acrylonitrile
-
-
?
acetonitrile + H2O
acetamide
show the reaction diagram
-
10% of the activity with propionitrile
-
-
?
acetonitrile + H2O
acetamide
show the reaction diagram
-
substrate specificity: acetonitrile ~ propionitrile > acrylonitrile >> butyronitrile
-
-
r
acetonitrile + H2O
acetamide
show the reaction diagram
Corynebacterium sp. C5
-
-
-
-
?
acetonitrile + H2O
acetamide
show the reaction diagram
Rhodococcus erythropolis N4
-
very low activity
-
-
?
acetonitrile + H2O
acetamide
show the reaction diagram
Arthrobacter sp. J-1
-
-
-
ir
acetonitrile + H2O
acetamide
show the reaction diagram
Rhodococcus pyridinivorans S82-2
-
-
-
-
r
acetonitrile + H2O
acetamide
show the reaction diagram
Brevibacterium sp. R312
-
10% of the activity with propionitrile
-
-
?
acetonitrile + H2O
acetamide
show the reaction diagram
Rhodococcus sp. RHA1
-
substrate specificity: acetonitrile ~ propionitrile > acrylonitrile >> butyronitrile
-
-
r
acetonitrile + H2O
acetamide
show the reaction diagram
Rhodococcus sp. 7
-
79% of the activity with acrylonitrile
-
-
?
acetonitrile + H2O
acetamide
show the reaction diagram
Rhodococcus qingshengii ZA0707
-
-
-
-
?
acetonitrile + H2O
acetamide
show the reaction diagram
Rhodococcus rhodochrous J1
-
-
-
-
?
acetonitrile + H2O
acetamide
show the reaction diagram
Rhodococcus rhodochrous J1
-
best substrate
-
-
?
acrylamide + H2O
acrylonitrile
show the reaction diagram
-
-
-
-
?
acrylamide + H2O
acrylonitrile
show the reaction diagram
Rhodococcus sp., Rhodococcus sp. N-774
-
-
-
?
acrylamide + H2O
acrylonitrile
show the reaction diagram
Rhodococcus rhodochrous NCIMB 11216
-
-
-
-
?
acrylamide + H2O
acrylonitrile
show the reaction diagram
-
-
-
?
acrylamide + H2O
acrylonitrile
show the reaction diagram
Rhodococcus rhodochrous J1
-
-
-
-
?
acrylonitrile + H2O
2-propenoic acid amide
show the reaction diagram
-
-
-
-
?
acrylonitrile + H2O
2-propenoic acid amide
show the reaction diagram
-
-
-
-
-
acrylonitrile + H2O
2-propenoic acid amide
show the reaction diagram
-
-
-
-
?
acrylonitrile + H2O
2-propenoic acid amide
show the reaction diagram
-
-
-
-
-
acrylonitrile + H2O
2-propenoic acid amide
show the reaction diagram
-
-
-
-
?
acrylonitrile + H2O
2-propenoic acid amide
show the reaction diagram
-
-
i.e. acrylic acid amide
?
acrylonitrile + H2O
2-propenoic acid amide
show the reaction diagram
-
-
i.e. acrylic acid amide
?
acrylonitrile + H2O
2-propenoic acid amide
show the reaction diagram
-
-
i.e. acrylic acid amide
r
acrylonitrile + H2O
2-propenoic acid amide
show the reaction diagram
-
-
i.e. acrylic acid amide
?
acrylonitrile + H2O
2-propenoic acid amide
show the reaction diagram
-
-
i.e. acrylic acid amide
?
acrylonitrile + H2O
2-propenoic acid amide
show the reaction diagram
-
-
i.e. acrylic acid amide
?
acrylonitrile + H2O
2-propenoic acid amide
show the reaction diagram
-
-
i.e. acrylic acid amide
?
acrylonitrile + H2O
2-propenoic acid amide
show the reaction diagram
-
-
i.e. acrylic acid amide
?
acrylonitrile + H2O
2-propenoic acid amide
show the reaction diagram
-
-
i.e. acrylamide
-
?
acrylonitrile + H2O
2-propenoic acid amide
show the reaction diagram
-
78% of the activity with propionitrile
i.e. acrylic acid amide
?
acrylonitrile + H2O
2-propenoic acid amide
show the reaction diagram
Rhodococcus erythropolis N4
-
-
i.e. acrylamide
-
?
acrylonitrile + H2O
2-propenoic acid amide
show the reaction diagram
Corynebacterium pseudodiphtheriticum ZBB-41
-
-
i.e. acrylic acid amide
?
acrylonitrile + H2O
2-propenoic acid amide
show the reaction diagram
Brevibacterium sp. R312
-
-
-
-
-
acrylonitrile + H2O
2-propenoic acid amide
show the reaction diagram
Rhodococcus rhodochrous NCIMB 11216
-
-
-
-
?
acrylonitrile + H2O
2-propenoic acid amide
show the reaction diagram
Rhodococcus sp. 7
-
-
i.e. acrylic acid amide
?
acrylonitrile + H2O
2-propenoic acid amide
show the reaction diagram
Pseudomonas chlororaphis B23, Rhodococcus rhodochrous J1
-
-
-
-
?
acrylonitrile + H2O
2-propenoic acid amide
show the reaction diagram
Rhodococcus rhodochrous J1
-
-
-
-
?
acrylonitrile + H2O
acrylamide
show the reaction diagram
-
-
-
-
-
acrylonitrile + H2O
acrylamide
show the reaction diagram
-
-
-
-
?
acrylonitrile + H2O
acrylamide
show the reaction diagram
-
-
-
-
?
acrylonitrile + H2O
acrylamide
show the reaction diagram
-
-
-
-
r
acrylonitrile + H2O
acrylamide
show the reaction diagram
-
-
-
-
?
acrylonitrile + H2O
acrylamide
show the reaction diagram
-
-
-
-
?
acrylonitrile + H2O
acrylamide
show the reaction diagram
Q2UZQ5, Q2UZQ6
-
-
-
?
acrylonitrile + H2O
acrylamide
show the reaction diagram
Q8GJG6, Q8GJG7
-
-
-
?
acrylonitrile + H2O
acrylamide
show the reaction diagram
Mesorhizobium sp.
-
-
-
-
?
acrylonitrile + H2O
acrylamide
show the reaction diagram
-
-
-
-
?
acrylonitrile + H2O
acrylamide
show the reaction diagram
Q5XPL4
-
yield 100%
-
?
acrylonitrile + H2O
acrylamide
show the reaction diagram
-
highest activity
-
-
?
acrylonitrile + H2O
acrylamide
show the reaction diagram
Mesorhizobium sp.
-
best substrate
-
-
?
acrylonitrile + H2O
acrylamide
show the reaction diagram
-
stereoselective reaction
-
-
?
acrylonitrile + H2O
acrylamide
show the reaction diagram
-
substrate specificity: acetonitrile ~ propionitrile > acrylonitrile >> butyronitrile
-
-
r
acrylonitrile + H2O
acrylamide
show the reaction diagram
Q7SID2
analysis of the structure model of the enzyme-substrate complex and catalytic mechanism, overview
-
-
?
acrylonitrile + H2O
acrylamide
show the reaction diagram
Comamonas testosteroni 5-MGAM-4D
Q5XPL4
-
yield 100%
-
?
acrylonitrile + H2O
acrylamide
show the reaction diagram
Rhodococcus ruber TH
-
-
-
-
?
acrylonitrile + H2O
acrylamide
show the reaction diagram
Q8GJG6, Q8GJG7
-
-
-
?
acrylonitrile + H2O
acrylamide
show the reaction diagram
Rhodococcus ruber CGMCC3090
-
highest activity
-
-
?
acrylonitrile + H2O
acrylamide
show the reaction diagram
Pseudonocardia thermophila JCM 3095
-
-
-
-
?
acrylonitrile + H2O
acrylamide
show the reaction diagram
Pseudonocardia thermophila JCM 3095
-
stereoselective reaction
-
-
?
acrylonitrile + H2O
acrylamide
show the reaction diagram
Pseudonocardia thermophila JCM 3095
Q7SID2
analysis of the structure model of the enzyme-substrate complex and catalytic mechanism, overview
-
-
?
acrylonitrile + H2O
acrylamide
show the reaction diagram
Rhodococcus sp. RHA1
-
substrate specificity: acetonitrile ~ propionitrile > acrylonitrile >> butyronitrile
-
-
r
acrylonitrile + H2O
acrylamide
show the reaction diagram
-
-
-
-
r
acrylonitrile + H2O
acrylamide
show the reaction diagram
Rhodococcus sp. SHZ-1
-
-
-
-
?
acrylonitrile + H2O
acrylamide
show the reaction diagram
Rhodococcus pyridinivorans MW3
Q2UZQ5, Q2UZQ6
-
-
-
?
acrylonitrile + H2O
acrylamide
show the reaction diagram
Rhodococcus qingshengii ZA0707
-
-
-
-
?
acrylonitrile + H2O
acrylamide
show the reaction diagram
Rhodococcus sp. J1
-
-
-
-
?
acrylonitrile + H2O
acrylamide
show the reaction diagram
Nocardia sp. 108
-
-
-
-
?
adiponitrile + H2O
adipic acid amide
show the reaction diagram
-
-
-
-
?
adiponitrile + H2O
adipic acid amide
show the reaction diagram
-
-
-
-
?
adiponitrile + H2O
adipic acid amide
show the reaction diagram
-
108% of the activity with propionitrile
-
-
?
adiponitrile + H2O
adipic acid amide
show the reaction diagram
Rhodococcus ruber CGMCC3090
-
-
-
-
?
adiponitrile + H2O
adipic acid amide
show the reaction diagram
Brevibacterium sp. R312
-
-
-
-
?
adiponitrile + H2O
5-cyanovaleramide
show the reaction diagram
Pseudomonas chlororaphis, Pseudomonas chlororaphis B23
-
-
-
-
-
adiponitrile + H2O
adipamide
show the reaction diagram
Comamonas testosteroni, Comamonas testosteroni 5-MGAM-4D
Q5XPL4
-
yield 100%
-
?
alpha-methylbenzyl cyanide + H2O
2-phenylpropanamide
show the reaction diagram
-
-
-
-
r
an aliphatic amide
a nitrile + H2O
show the reaction diagram
-
-
-
-
?
an aliphatic amide
a nitrile + H2O
show the reaction diagram
-
ligand exchange reactions, overview
-
-
?
an aliphatic amide
a nitrile + H2O
show the reaction diagram
Rhodococcus erythropolis N-771
-
-, ligand exchange reactions, overview
-
-
?
an aliphatic amide
a nitrile + H2O
show the reaction diagram
Pseudonocardia thermophila JCM 3095
-
-, ligand exchange reactions, overview
-
-
?
benzaldehyde + HCN
? + H2O
show the reaction diagram
-
-
95% conversion to alpha-hydroxy nitrile
-
?
benzonitrile + H2O
benzoic acid amide
show the reaction diagram
-
-
-
-
?
benzonitrile + H2O
benzoic acid amide
show the reaction diagram
-
-
-
-
?
benzonitrile + H2O
benzoic acid amide
show the reaction diagram
-
-
-
-
?
benzonitrile + H2O
benzoic acid amide
show the reaction diagram
-
-
-
-
?
benzonitrile + H2O
benzoic acid amide
show the reaction diagram
Mesorhizobium sp.
-
-
-
-
?
benzonitrile + H2O
benzoic acid amide
show the reaction diagram
-
low activity
-
-
?
benzonitrile + H2O
benzoic acid amide
show the reaction diagram
-
19.4% of the activity with acrylonitrile
-
-
?
benzonitrile + H2O
benzoic acid amide
show the reaction diagram
-
1.3% of the activity with propionitrile
-
-
?
benzonitrile + H2O
benzoic acid amide
show the reaction diagram
Mesorhizobium sp.
-
15% of the activity with acrylonitrile
-
-
?
benzonitrile + H2O
benzoic acid amide
show the reaction diagram
Rhodococcus equi TG328-2
-
-
-
-
?
benzonitrile + H2O
benzoic acid amide
show the reaction diagram
Rhodococcus erythropolis N4
-
low activity
-
-
?
benzonitrile + H2O
benzamide
show the reaction diagram
-
-
-
-
?
benzonitrile + H2O
benzamide
show the reaction diagram
-
-
-
-
?, ir
benzonitrile + H2O
benzamide
show the reaction diagram
-
-
-
-
?
benzonitrile + H2O
benzamide
show the reaction diagram
-
-
-
-
?
benzonitrile + H2O
benzamide
show the reaction diagram
-
99.9% conversion, in phosphate buffer pH 7.0, at 30C
-
-
?
benzonitrile + H2O
benzamide
show the reaction diagram
-
performed by a cascade bienzymatic reaction involving nitrile hydration and acyl transfer of the intermediate benzamide onto hydroxylamine. The first step is catalyzed by a cell-free extract from recombinant Escherichia coli strain expressing nitrile hydratase from Klebsiella oxytoca strain 38.1.2, the second step is cell-free extract from Rhodococcus erythropolis A4 amidase, EC 3.5.1.4
-
-
?
benzonitrile + H2O
benzamide
show the reaction diagram
-
performed by a cascade bienzymatic reaction involving nitrile hydration and acyl transfer of the intermediate benzamide onto hydroxylamine. The first step is catalyzed by a cell-free extract from recombinant Escherichia coli strain expressing nitrile hydratase from Raoultella terrigena srain 77.1, the second step is a cell-free extract from Rhodococcus erythropolis A4 amidase, EC 3.5.1.4
-
-
?
benzonitrile + H2O
benzamide
show the reaction diagram
Klebsiella oxytoca 38.1.2
-
-, performed by a cascade bienzymatic reaction involving nitrile hydration and acyl transfer of the intermediate benzamide onto hydroxylamine. The first step is catalyzed by a cell-free extract from recombinant Escherichia coli strain expressing nitrile hydratase from Klebsiella oxytoca strain 38.1.2, the second step is cell-free extract from Rhodococcus erythropolis A4 amidase, EC 3.5.1.4
-
-
?
benzonitrile + H2O
benzamide
show the reaction diagram
-
-
-
-
?, ir
benzonitrile + H2O
benzamide
show the reaction diagram
-
99.9% conversion, in phosphate buffer pH 7.0, at 30C
-
-
?
benzonitrile + H2O
benzamide
show the reaction diagram
Raoultella terrigena 77.1
-
-, performed by a cascade bienzymatic reaction involving nitrile hydration and acyl transfer of the intermediate benzamide onto hydroxylamine. The first step is catalyzed by a cell-free extract from recombinant Escherichia coli strain expressing nitrile hydratase from Raoultella terrigena srain 77.1, the second step is a cell-free extract from Rhodococcus erythropolis A4 amidase, EC 3.5.1.4
-
-
?
benzonitrile + H2O
benzamide
show the reaction diagram
Rhodococcus rhodochrous IFO 15564
-
-
-
-
?
benzonitrile + H2O
benzamide
show the reaction diagram
Pseudonocardia thermophila JCM 3095
-
-
-
-
?
benzonitrile + hydroxylamine + H2O
benzohydroxamic acid + NH3
show the reaction diagram
-
-, performed by a cascade bienzymatic reaction involving nitrile hydration and acyl transfer of the intermediate benzamide onto hydroxylamine. The first step is catalyzed by a cell-free extract from Rhodococcus erythropolis A4 containing nitrile hydratase, the second step is a cell-free extract from Rhodococcus erythropolis A4 amidase, EC 3.5.1.4
-
-
?
benzonitrile + hydroxylamine + H2O
benzohydroxamic acid + NH3
show the reaction diagram
Rhodococcus erythropolis A4
-
-, performed by a cascade bienzymatic reaction involving nitrile hydration and acyl transfer of the intermediate benzamide onto hydroxylamine. The first step is catalyzed by a cell-free extract from Rhodococcus erythropolis A4 containing nitrile hydratase, the second step is a cell-free extract from Rhodococcus erythropolis A4 amidase, EC 3.5.1.4
-
-
?
benzylcyanide + H2O
2-phenylacetamide
show the reaction diagram
-
-
-
-
r
butyronitrile + H2O
butyramide
show the reaction diagram
-
-
-
-
?
butyronitrile + H2O
butyramide
show the reaction diagram
-
-
-
-
?
butyronitrile + H2O
butyramide
show the reaction diagram
Q5XPL4
-
yield 100%
-
?
butyronitrile + H2O
butyramide
show the reaction diagram
-
substrate specificity: acetonitrile ~ propionitrile > acrylonitrile >> butyronitrile
-
-
r
butyronitrile + H2O
butyramide
show the reaction diagram
Klebsiella oxytoca 38.1.2, Raoultella terrigena 77.1
-
-
-
-
?
butyronitrile + H2O
butyramide
show the reaction diagram
Rhodococcus sp. RHA1
-
substrate specificity: acetonitrile ~ propionitrile > acrylonitrile >> butyronitrile
-
-
r
butyronitrile + H2O
butyramide
show the reaction diagram
Rhodococcus qingshengii ZA0707
-
-
-
-
?
butyronitrile + H2O
butyric acid amide
show the reaction diagram
-
best substrate
-
-
?
chloroacetonitrile + H2O
chloroacetamide
show the reaction diagram
-
-
-
-
?
chloroacetonitrile + H2O
chloroacetamide
show the reaction diagram
-
-
-
-
?
chloroacetonitrile + H2O
chloroacetamide
show the reaction diagram
-
-
-
ir
chloroacetonitrile + H2O
chloroacetamide
show the reaction diagram
-
-
-
-
?
chloroacetonitrile + H2O
chloroacetamide
show the reaction diagram
-
42% of the activity with propionitrile
-
-
?
chloroacetonitrile + H2O
chloroacetamide
show the reaction diagram
Corynebacterium sp. C5
-
-
-
-
?
chloroacetonitrile + H2O
chloroacetamide
show the reaction diagram
Arthrobacter sp. J-1
-
-
-
ir
chloroacetonitrile + H2O
chloroacetamide
show the reaction diagram
Brevibacterium sp. R312
-
42% of the activity with propionitrile
-
-
?
chloroacetonitrile + H2O
chloroacetamide
show the reaction diagram
Pseudomonas chlororaphis B23
-
-
-
-
?
chloroacetonitrile + H2O
chloroacetamide
show the reaction diagram
Rhodococcus rhodochrous J1
-
-
-
-
?
crotononitrile + H2O
(E)-2-butenoic acid amide
show the reaction diagram
-
-
-
-
?
crotononitrile + H2O
(E)-2-butenoic acid amide
show the reaction diagram
-
19% of the activity with propionitrile
-
-
?
crotononitrile + H2O
(E)-2-butenoic acid amide
show the reaction diagram
-
19% of the activity with propionitrile
-
-
?
crotononitrile + H2O
(E)-2-butenoic acid amide
show the reaction diagram
-
19% of the activity with propionitrile
-
-
?
crotononitrile + H2O
(E)-2-butenoic acid amide
show the reaction diagram
Rhodococcus rhodochrous J1
-
-
-
-
?
cyanamide + H2O
urea
show the reaction diagram
-
-
-
?
cyanide + H2O
formamide
show the reaction diagram
-
-
-
-
?
cyanide + H2O
formamide
show the reaction diagram
-
2% of the activity with propionitrile
-
-
?
cyanopyrazine + H2O
pyrazincarbamide
show the reaction diagram
-
-
-
-
?
cyanovaleramide
valerodinitrile + H2O
show the reaction diagram
Brevibacterium sp., Brevibacterium sp. R312
-
-
-
-
?
cyanovaleric acid + H2O
?
show the reaction diagram
-
-
-
-
?
cyanovaleric acid + H2O
?
show the reaction diagram
Brevibacterium sp., Brevibacterium sp. R312
-
-
-
-
?
cyclopropylcyanide + H2O
?
show the reaction diagram
-
-
-
-
?
ethyl 2-cyanobenzoate + H2O
ethyl 2-carbamoylbenzoate
show the reaction diagram
-
-
-
-
ir
ethyl 3-cyanobenzoate + H2O
ethyl 3-carbamoylbenzoate
show the reaction diagram
-
no conversion, in phosphate buffer pH 7.0, at 30C
-
-
?
ethyl 4-cyanobenzoate + H2O
ethyl 4-carbamoylbenzoate
show the reaction diagram
-
-
-
-
ir
ethyl 4-cyanobenzoate + H2O
ethyl 4-carbamoylbenzoate
show the reaction diagram
-
95% conversion, in phosphate buffer pH 7.0, at 30C
-
-
?
ethylene cyanhydrine + H2O
?
show the reaction diagram
-
-
-
-
?
ethylene cyanhydrine + H2O
?
show the reaction diagram
-
-
-
-
?
furan-2-carbonitrile + H2O
furan-2-carboxamide
show the reaction diagram
-
-
-
-
ir
furan-2-carbonitrile + H2O
furan-2-carboxamide
show the reaction diagram
-
99.9% conversion, in phosphate buffer pH 7.0, at 30C
-
-
?
glutaronitrile + H2O
?
show the reaction diagram
-
38% of the activity with propionitrile
-
-
?
glycolonitrile + H2O
glycolamide
show the reaction diagram
Q5XPL4
-
yield 63%
-
?
hydroxyacetonitrile + H2O
hydroxyacetamide
show the reaction diagram
-
-
-
-
hydroxyacetonitrile + H2O
hydroxyacetamide
show the reaction diagram
-
-
-
r
hydroxyacetonitrile + H2O
hydroxyacetamide
show the reaction diagram
-
50% of the activity with propionitrile
-
?
indole-3-acetonitrile + H2O
(indole-3-yl)acetamide
show the reaction diagram
-
-
-
-
?
indole-3-acetonitrile + H2O
(indole-3-yl)acetamide
show the reaction diagram
-
-
-
?
indole-3-acetonitrile + H2O
(indole-3-yl)acetamide
show the reaction diagram
Rhodococcus ruber CGMCC3090
-
-
-
-
?
indole-3-acetonitrile + H2O
indole-3-acetamide
show the reaction diagram
Nocardia sp., Nocardia sp. 108
-
conversion rate: 34.44%
-
-
?
indole-3-acetonitrile + H2O
(indol-3-yl)acetamide
show the reaction diagram
Sinorhizobium meliloti, Agrobacterium tumefaciens, Rhizobium leguminosarum, Mesorhizobium loti, Mesorhizobium loti 02-10055, Mesorhizobium loti 02-10056, Agrobacterium tumefaciens IAM B-261, Rhizobium leguminosarum 02-03119, Sinorhizobium meliloti 03-03046, Mesorhizobium loti 02-10101, Rhizobium leguminosarum 02-10230, Rhizobium leguminosarum 02-10041
-
-
-
-
?
isobutyronitrile + H2O
isobutyric acid amide
show the reaction diagram
-
-
-
-
?
isobutyronitrile + H2O
isobutyric acid amide
show the reaction diagram
-
-
-
-
?
isobutyronitrile + H2O
isobutyric acid amide
show the reaction diagram
-
-
-
-
?
isobutyronitrile + H2O
isobutyric acid amide
show the reaction diagram
-
-
-
-
?
isobutyronitrile + H2O
isobutyric acid amide
show the reaction diagram
Mesorhizobium sp.
-
-
-
-
?
isobutyronitrile + H2O
isobutyric acid amide
show the reaction diagram
-
113% of the activity with propionitrile
-
-
?
isobutyronitrile + H2O
isobutyric acid amide
show the reaction diagram
-
62.5% of the activity with acrylonitrile
-
-
?
isobutyronitrile + H2O
isobutyric acid amide
show the reaction diagram
Mesorhizobium sp.
-
71% of the activity with acrylonitrile
-
-
?
isobutyronitrile + H2O
isobutyric acid amide
show the reaction diagram
Rhodococcus equi TG328-2
-
-
-
-
?
isobutyronitrile + H2O
isobutyric acid amide
show the reaction diagram
Mesorhizobium sp. BNC1
-
-, 71% of the activity with acrylonitrile
-
-
?
isobutyronitrile + H2O
isobutyric acid amide
show the reaction diagram
Rhodococcus erythropolis N4
-
-
-
-
?
isobutyronitrile + H2O
isobutyric acid amide
show the reaction diagram
Brevibacterium sp. R312
-
113% of the activity with propionitrile
-
-
?
isobutyronitrile + H2O
isobutyric acid amide
show the reaction diagram
Rhodococcus sp. 7
-
62.5% of the activity with acrylonitrile
-
-
?
isobutyronitrile + H2O
isobutyramide
show the reaction diagram
-
-
-
-
?
isovaleronitrile + H2O
isovaleric acid amide
show the reaction diagram
-
-
product identification by liquid chromatography tandem mass spectrometry
-
?
isovaleronitrile + H2O
isovaleric acid amide
show the reaction diagram
-
more active than trans-4-cyanocyclohexane-1-carboxylic acid as substrate
-
-
?
isovaleronitrile + H2O
isovaleric acid amide
show the reaction diagram
Rhodococcus sp. N771
-
-
product identification by liquid chromatography tandem mass spectrometry
-
?
malonitrile + H2O
?
show the reaction diagram
-
44% of the activity with propionitrile
-
-
?
mandelonitrile + H2O
?
show the reaction diagram
-
-
-
-
?
mandelonitrile + H2O
?
show the reaction diagram
-
used as well as phenylacetonitrile
-
-
?
methacrylamide + H2O
?
show the reaction diagram
Pseudomonas chlororaphis, Pseudomonas chlororaphis B23
-
causes the greatest induction of activity
-
-
?
methacrylonitrile + H2O
methylacrylic acid amide
show the reaction diagram
-
-
-
-
?
methacrylonitrile + H2O
methylacrylic acid amide
show the reaction diagram
-
-
-
-
?
methacrylonitrile + H2O
methylacrylic acid amide
show the reaction diagram
-
-
-
r
methacrylonitrile + H2O
methylacrylic acid amide
show the reaction diagram
-
-
-
-
?
methacrylonitrile + H2O
methylacrylic acid amide
show the reaction diagram
-
more active than trans-4-cyanocyclohexane-1-carboxylic acid as substrate
-
-
?
methacrylonitrile + H2O
methylacrylic acid amide
show the reaction diagram
-
53% of the activity with propionitrile
-
-
?
methacrylonitrile + H2O
methylacrylic acid amide
show the reaction diagram
Pseudomonas putida NRRL-18668
-
-
-
-
?
methacrylonitrile + H2O
methacrylamide
show the reaction diagram
-
-
-
-
?
methacrylonitrile + H2O
methacrylamide
show the reaction diagram
-
-
-
-
?
methacrylonitrile + H2O
methacrylamide
show the reaction diagram
-
-
-
-
?
methacrylonitrile + H2O
methacrylamide
show the reaction diagram
Q5XPL4
-
yield 100%
-
?
methacrylonitrile + H2O
methacrylamide
show the reaction diagram
-
low activity
-
-
?
methacrylonitrile + H2O
methacrylamide
show the reaction diagram
Rhodococcus sp. N771
-
-
-
-
?
methacrylonitrile + H2O
methacrylamide
show the reaction diagram
Rhodococcus sp. N771
-
low activity
-
-
?
methacrylonitrile + H2O
methacrylamide
show the reaction diagram
Rhodococcus erythropolis N771
-
-
-
-
?
methacrylonitrile + H2O
methylacrylamide
show the reaction diagram
Pseudonocardia thermophila, Pseudonocardia thermophila JCM 3095
-
-
-
-
?
methacrylonitrile + H2O
methacrylic acid amide
show the reaction diagram
-
-
-
-
?
methoxyacetonitrile + H2O
?
show the reaction diagram
-
-
-
-
?
methyl 4-cyanobenzoate + H2O
methyl 4-carbamoylbenzoate
show the reaction diagram
-
-
-
-
ir
n-butyronitrile + H2O
n-butyric acid amide
show the reaction diagram
-
-
-
-
-
n-butyronitrile + H2O
n-butyric acid amide
show the reaction diagram
-
-
-
-
?
n-butyronitrile + H2O
n-butyric acid amide
show the reaction diagram
-
-
-
-
?
n-butyronitrile + H2O
n-butyric acid amide
show the reaction diagram
-
-
-
-
-
n-butyronitrile + H2O
n-butyric acid amide
show the reaction diagram
-
-
-
r
n-butyronitrile + H2O
n-butyric acid amide
show the reaction diagram
-
-
-
-
-
n-butyronitrile + H2O
n-butyric acid amide
show the reaction diagram
-
-
-
-
?
n-butyronitrile + H2O
n-butyric acid amide
show the reaction diagram
-
-
-
-
-
n-butyronitrile + H2O
n-butyric acid amide
show the reaction diagram
-
-
-
-
?
n-butyronitrile + H2O
n-butyric acid amide
show the reaction diagram
-
33% of the activity with propionitrile
-
-
?
n-butyronitrile + H2O
n-butyric acid amide
show the reaction diagram
-
140% of the activity with propionitrile
-
-
?
n-butyronitrile + H2O
n-butyric acid amide
show the reaction diagram
Corynebacterium sp. C5
-
-
-
-
?
n-butyronitrile + H2O
n-butyric acid amide
show the reaction diagram
Arthrobacter sp. J-1
-
-
-
r
n-butyronitrile + H2O
n-butyric acid amide
show the reaction diagram
Brevibacterium sp. R312
-
33% of the activity with propionitrile
-
-
?
n-butyronitrile + H2O
n-butyric acid amide
show the reaction diagram
Brevibacterium sp. R312
-
140% of the activity with propionitrile
-
-
?
n-butyronitrile + H2O
n-butyric acid amide
show the reaction diagram
Pseudomonas chlororaphis B23, Rhodococcus rhodochrous J1
-
-
-
-
-
n-butyronitrile + H2O
n-butyric acid amide
show the reaction diagram
Rhodococcus rhodochrous J1
-
-
-
-
?
n-butyronitrile + H2O
n-butyramide
show the reaction diagram
-
-
-
-
r
n-capronitrile + H2O
n-hexanoic acid amide
show the reaction diagram
-
-
-
-
?
n-capronitrile + H2O
n-hexanoic acid amide
show the reaction diagram
-
-
-
-
?
n-capronitrile + H2O
n-hexanoic acid amide
show the reaction diagram
Brevibacterium sp., Brevibacterium sp. R312
-
46% of the activity with propionitrile
-
-
?
N-phenylglycinenitrile + H2O
?
show the reaction diagram
-
-
-
-
?
n-valeronitrile + H2O
n-valeramide
show the reaction diagram
Pseudomonas putida, Pseudomonas putida NRRL-18668
-
-
-
-
?
nicotinonitrile + H2O
nicotinamide
show the reaction diagram
Pseudonocardia thermophila, Pseudonocardia thermophila JCM 3095
-
-
-
-
?
o-chlorobenzonitrile + H2O
o-chlorobenzamide
show the reaction diagram
Nocardia sp., Nocardia sp. 108
-
-
-
-
?
p-aminobenzonitrile + H2O
p-aminobenzamide
show the reaction diagram
-
conversion rate: 8.98%
-
-
?
p-chlorobenzonitrile + H2O
p-chlorobenzamide
show the reaction diagram
-
conversion rate: 93.1%
-
-
?
p-hydroxybenzylcyanide + H2O
2-(4-hydroxyphenyl)acetamide
show the reaction diagram
-
-
-
-
?
phenylacetonitrile + 2 H2O
phenylacetic acid + NH3
show the reaction diagram
-
-
-
?
phenylacetonitrile + H2O
phenylacetamide
show the reaction diagram
-
-
-
-
?
phenylacetonitrile + H2O
phenylacetamide
show the reaction diagram
Sinorhizobium meliloti, Agrobacterium tumefaciens, Agrobacterium tumefaciens IAM B-261, Sinorhizobium meliloti 03-03046
-
337% activity compared to indole-3-acetonitrile
-
-
?
phenylacetonitrile + H2O
2-phenylacetamide
show the reaction diagram
-
-
-
-
ir
phenylacetonitrile + H2O
2-phenylacetamide
show the reaction diagram
-
28% conversion, in phosphate buffer pH 7.0, at 30C
-
-
?
phthalonitrile + H2O
?
show the reaction diagram
-
-
-
-
?
phthalonitrile + H2O
2-cyanobenzamide
show the reaction diagram
-
lowest activity
-
-
?
pivalonitrile + H2O
2,2-dimethylpropionic acid amide
show the reaction diagram
-
-
-
-
?
pivalonitrile + H2O
2,2-dimethylpropionic acid amide
show the reaction diagram
-
5.3% of the activity with propionitrile
-
-
?
pivalonitrile + H2O
2,2-dimethylpropionic acid amide
show the reaction diagram
-
62% of the activity with acrylonitrile
-
-
?
pivalonitrile + H2O
2,2-dimethylpropionic acid amide
show the reaction diagram
-
5% of the activity with propionitrile
-
-
?
pivalonitrile + H2O
2,2-dimethylpropionic acid amide
show the reaction diagram
Rhodococcus sp. 7
-
62% of the activity with acrylonitrile
-
-
?
propionitrile + H2O
propionic acid amide
show the reaction diagram
-
-
-
-
?
propionitrile + H2O
propionic acid amide
show the reaction diagram
-
-
-
-
?
propionitrile + H2O
propionic acid amide
show the reaction diagram
-
-
-
-
-
propionitrile + H2O
propionic acid amide
show the reaction diagram
-
-
-
-
?
propionitrile + H2O
propionic acid amide
show the reaction diagram
-
-
-
-
?
propionitrile + H2O
propionic acid amide
show the reaction diagram
-
-
-
-
?
propionitrile + H2O
propionic acid amide
show the reaction diagram
-
-
-
?
propionitrile + H2O
propionic acid amide
show the reaction diagram
-
-
-
-
?
propionitrile + H2O
propionic acid amide
show the reaction diagram
Mesorhizobium sp.
-
-
-
-
?
propionitrile + H2O
propionic acid amide
show the reaction diagram
-
-
i.e. propionamide
r
propionitrile + H2O
propionic acid amide
show the reaction diagram
-
-
i.e. propionamide
?
propionitrile + H2O
propionic acid amide
show the reaction diagram
-
10% of conversion in 24 h
i.e. propionamide
?
propionitrile + H2O
propionic acid amide
show the reaction diagram
-
64% of the activity with acrylonitrile
-
-
?
propionitrile + H2O
propionic acid amide
show the reaction diagram
Mesorhizobium sp.
-
17% of the activity with acrylonitrile
-
-
?
propionitrile + H2O
propionic acid amide
show the reaction diagram
Corynebacterium sp. C5
-
-
-
-
?
propionitrile + H2O
propionic acid amide
show the reaction diagram
Mesorhizobium sp. BNC1
-
-, 17% of the activity with acrylonitrile
-
-
?
propionitrile + H2O
propionic acid amide
show the reaction diagram
Rhodococcus erythropolis N4
-
-
-
-
?
propionitrile + H2O
propionic acid amide
show the reaction diagram
Arthrobacter sp. J-1
-
-
i.e. propionamide
r
propionitrile + H2O
propionic acid amide
show the reaction diagram
Rhodococcus sp. N-774
-
-
-
-
?
propionitrile + H2O
propionic acid amide
show the reaction diagram
Brevibacterium sp. R312
-
-
-
-
?
propionitrile + H2O
propionic acid amide
show the reaction diagram
Brevibacterium sp. R312
-
-
i.e. propionamide
?
propionitrile + H2O
propionic acid amide
show the reaction diagram
Brevibacterium sp. R312
-
-
-
?
propionitrile + H2O
propionic acid amide
show the reaction diagram
Rhodococcus rhodochrous NCIMB 11216
-
10% of conversion in 24 h
i.e. propionamide
?
propionitrile + H2O
propionic acid amide
show the reaction diagram
Rhodococcus sp. 7
-
64% of the activity with acrylonitrile
-
-
?
propionitrile + H2O
propionic acid amide
show the reaction diagram
Pseudomonas chlororaphis B23
-
-
-
-
?
propionitrile + H2O
propionic acid amide
show the reaction diagram
Rhodococcus rhodochrous J1
-
-
-
-
?
propionitrile + H2O
propionamide
show the reaction diagram
-
-
-
-
r
propionitrile + H2O
propionamide
show the reaction diagram
-
-
-
-
?
propionitrile + H2O
propionamide
show the reaction diagram
-
-
-
-
?
propionitrile + H2O
propionamide
show the reaction diagram
-
-
-
-
?
propionitrile + H2O
propionamide
show the reaction diagram
-
-
-
-
?
propionitrile + H2O
propionamide
show the reaction diagram
-
-
-
-
?
propionitrile + H2O
propionamide
show the reaction diagram
-
substrate specificity: acetonitrile ~ propionitrile > acrylonitrile >> butyronitrile
-
-
r
propionitrile + H2O
propionamide
show the reaction diagram
Klebsiella oxytoca 38.1.2, Raoultella terrigena 77.1
-
-
-
-
?
propionitrile + H2O
propionamide
show the reaction diagram
Rhodococcus sp. RHA1
-
substrate specificity: acetonitrile ~ propionitrile > acrylonitrile >> butyronitrile
-
-
r
propionitrile + H2O
propionamide
show the reaction diagram
-
-
-
-
r
propionitrile + H2O
propionamide
show the reaction diagram
Microbacterium imperiale CBS 498-74
-
-
-
-
?
propionitrile + H2O
propionamide
show the reaction diagram
Pseudomonas chlororaphis B23
-
-
-
-
?
propionitrile + H2O
propionamide
show the reaction diagram
Rhodococcus qingshengii ZA0707
-
-
-
-
?
pyridine-2-carbonitrile + H2O
pyridine-2-carboxamide
show the reaction diagram
-
-
-
-
ir
pyridine-2-carbonitrile + H2O
pyridine-2-carboxamide
show the reaction diagram
-
99.9% conversion, in phosphate buffer pH 7.0, at 30C
-
-
?
pyridine-4-carbonitrile + H2O
pyridine-4-carboxamide
show the reaction diagram
-
-
-
-
ir
pyridine-4-carbonitrile + H2O
pyridine-4-carboxamide
show the reaction diagram
-
99.9% conversion, in phosphate buffer pH 7.0, at 30C
-
-
?
succinonitrile + H2O
?
show the reaction diagram
-
135% of the activity with propionitrile
-
-
?
tert-butylisonitrile + H2O
tert-butyl amide
show the reaction diagram
-
-
-
-
?
tert-butylisonitrile + H2O
tert-butyl amide
show the reaction diagram
-
-
-
-
?
tert-butylisonitrile + H2O
tert-butyl amide
show the reaction diagram
Rhodococcus sp. N771
-
-
-
-
?
tert-butylisonitrile + H2O
tert-butyl amide
show the reaction diagram
Pseudonocardia thermophila JCM 3095
-
-
-
-
?
thiophen-2-ylacetonitrile + H2O
2-(thiophen-2-yl)acetamide
show the reaction diagram
-
-
-
-
ir
thiophen-2-ylacetonitrile + H2O
2-(thiophen-2-yl)acetamide
show the reaction diagram
-
89% conversion, in phosphate buffer pH 7.0, at 30C
-
-
?
thiophene-2-carbonitrile + H2O
thiophene-2-carboxamide
show the reaction diagram
-
99.9% conversion, in phosphate buffer pH 7.0, at 30C
-
-
?
thiophene-2-carbonitrile + H2O
thiophen-2-carboxamide
show the reaction diagram
-
-
-
-
ir
trans-4-cyanocyclohexane-1-carboxylic acid + H2O
4-(aminocarbonyl)cyclohexanecarboxylic acid
show the reaction diagram
Corynebacterium sp., Corynebacterium sp. C5
-
-
-
?
trans-cinnamonitrile + H2O
trans-cinnamide
show the reaction diagram
-
-
-
-
?
valeronitrile + H2O
n-pentanoic acid amide
show the reaction diagram
-
-
-
-
?
valeronitrile + H2O
n-pentanoic acid amide
show the reaction diagram
-
-
-
-
-
valeronitrile + H2O
n-pentanoic acid amide
show the reaction diagram
-
-
-
-
?
valeronitrile + H2O
n-pentanoic acid amide
show the reaction diagram
-
more than 3 times more active than trans-4-cyanocyclohexane-1-carboxylic acid as substrate
-
-
?
valeronitrile + H2O
n-pentanoic acid amide
show the reaction diagram
-
2.7% of the activity with propionitrile
-
-
?
valeronitrile + H2O
n-pentanoic acid amide
show the reaction diagram
Rhodococcus equi, Rhodococcus equi TG328-2
-
almost 9000fold higher activity towards valeronitrile compared to (R,S)-2-phenylpropionitrile
-
-
?
valeronitrile + H2O
n-pentanoic acid amide
show the reaction diagram
Rhodococcus ruber CGMCC3090
-
-
-
-
?
valeronitrile + H2O
n-pentanoic acid amide
show the reaction diagram
Brevibacterium sp. R312
-
2.7% of the activity with propionitrile
-
-
?
valeronitrile + H2O
n-pentanoic acid amide
show the reaction diagram
Brevibacterium sp. R312
-
-
-
-
-
valeronitrile + H2O
valeramide
show the reaction diagram
-
-
-
-
?
methyl 4-cyanobenzoate + H2O
methyl 4-carbamoylbenzoate
show the reaction diagram
-
98% conversion, in phosphate buffer pH 7.0, at 30C
-
-
?
additional information
?
-
-
-
-
-
-
additional information
?
-
-
specificity overview
-
-
-
additional information
?
-
-
specificity overview
-
-
-
additional information
?
-
-
wide substrate spectrum
-
-
-
additional information
?
-
-
the enzyme acts on low-molecular aliphatic nitriles with 2-5 carbons but not on aliphatic nitriles with more than 6 carbons
-
-
-
additional information
?
-
-
H-NHase acts preferentially on aliphatic nitriles, while L-NHase has a higher affinity for aromatic nitriles
-
-
-
additional information
?
-
-
an unusual preference for branched and cyclic aliphatic nitriles is noted
-
-
-
additional information
?
-
-
aromatic nitriles are barely hydrated by the enzyme, formamide, acetamide, acrylamide, propionamide, n-butyramide, isobutyramide, n-valeramide, succinamide, benzamide, phenylacetamide and lactamide are no substrates
-
-
-
additional information
?
-
-
aliphatic nitriles with more than 5 carbons and aromatic nitriles cannot act as substrate
-
-
-
additional information
?
-
Corynebacterium nitrilophilus
-
highest rate of reaction with short chain aliphatic nitriles
-
-
-
additional information
?
-
-
S enantiomer conversion is 14 times greater than the rate of R enantiomer conversion
-
-
-
additional information
?
-
-
no detectably transformation with 2-methyl-2-butenenitrile, benzonitrile and phenylacetonitrile
-
-
-
additional information
?
-
-
methacrylamide-induced enzyme activity, no activity in absence of methacrylamide, no or reduced activity in NhpR transcriptional regulator defective mutants
-
-
-
additional information
?
-
-
NHase is a non-heme iron enzyme catalyzing the hydration of various nitriles to the corresponding amides
-
-
-
additional information
?
-
-
computational molecular dynamics modelling of ligand docking and substrate transport and binding, overview
-
-
-
additional information
?
-
-
hydrogen bonds between betaArg56 and alphaCys114 sulfenic acid are important to maintain the enzymatic activity, molecular dynamics simulations determining the differences in the dynamics of lightactive and dark-inactive forms of NHase, overview
-
-
-
additional information
?
-
-
NHase hydrates a nitrile to provide the corresponding amide product via an addition reaction of one water molecule, active site structure involving amidate nitrogen donors from the peptide backbone, overview
-
-
-
additional information
?
-
-
substrate binding preferences and pK(a) determinations of a nitrile hydratase model complex, catalytic mechanism, overview
-
-
-
additional information
?
-
Mesorhizobium sp.
-
the NHase active site of the strain F28 might consist of cysteine and serine
-
-
-
additional information
?
-
-
besides aromatic and heterocyclic nitriles, aliphatic ones are hydrated preferentially, no activity with (R,S)-2-(4-isobutylphenyl)propionitrile and (R,S)-3-(1-cyanoethyl)benzoic acid
-
-
-
additional information
?
-
-
NhhG forms a complex with the alpha-subunit of H-NHase. NhhAG is very similar to the mediator of L-NHase, NhlAE, which is a heterotrimer complex consisting of the cobalt-containing alpha-subunit of L-NHase and NhlE
-
-
-
additional information
?
-
-
substrate specificity of strain 38.1.2, no activity with 4-tolunitrile, overview
-
-
-
additional information
?
-
-
substrate specificity of strain 77.1, no activity with 4-tolunitrile and 3-chlorobenzonitrile, overview
-
-
-
additional information
?
-
-
the nitrile hydratase can hydrate aliphatic, aromatic and heterocyclic nitriles under very mild conditions, in mixtures of pH 7 buffer and a range of organic solvents, often with excellent chemoselectivity. Major determinant of hydration occurring is the degree of steric hindrance around the nitrile moiety and/or size of the substrates
-
-
-
additional information
?
-
-
the thermoactive nitrilase from Pyrococcus abyssi hydrolyses small aliphatic nitriles like fumaro- and malononitril, docking calculations for fumaro- and malononitriles, modelling, overview
-
-
-
additional information
?
-
-
roles of second- and third-shell residues of the active site structure in catalysis, overview. Three of the predicted second-shell residues, alpha-Asp164, beta-Glu56, and beta-His147, and one predicted third-shell residue, beta-His71, have significant effects on the catalytic efficiency of the enzyme, while one of the predicted residues, alpha-Glu168, and the three residues not predicted, alpha-Arg170, alpha-Tyr171, and beta-Tyr215, do not have any significant effects on the catalytic efficiency of the enzyme
-
-
-
additional information
?
-
-
(indol-3-yl)acetamide is no substrate, no formation of iodoacetic acid
-
-
-
additional information
?
-
Klebsiella oxytoca 38.1.2
-
substrate specificity of strain 38.1.2, no activity with 4-tolunitrile, overview
-
-
-
additional information
?
-
-
the nitrile hydratase can hydrate aliphatic, aromatic and heterocyclic nitriles under very mild conditions, in mixtures of pH 7 buffer and a range of organic solvents, often with excellent chemoselectivity. Major determinant of hydration occurring is the degree of steric hindrance around the nitrile moiety and/or size of the substrates
-
-
-
additional information
?
-
Raoultella terrigena 77.1
-
substrate specificity of strain 77.1, no activity with 4-tolunitrile and 3-chlorobenzonitrile, overview
-
-
-
additional information
?
-
Rhodococcus equi TG328-2
-
besides aromatic and heterocyclic nitriles, aliphatic ones are hydrated preferentially, no activity with (R,S)-2-(4-isobutylphenyl)propionitrile and (R,S)-3-(1-cyanoethyl)benzoic acid
-
-
-
additional information
?
-
Agrobacterium tumefaciens IAM B-261
-
(indol-3-yl)acetamide is no substrate, no formation of iodoacetic acid
-
-
-
additional information
?
-
Mesorhizobium sp. BNC1
-
the NHase active site of the strain F28 might consist of cysteine and serine
-
-
-
additional information
?
-
Arthrobacter sp. J-1
-
aliphatic nitriles with more than 5 carbons and aromatic nitriles cannot act as substrate
-
-
-
additional information
?
-
Rhodococcus sp. N771
-
NHase is a non-heme iron enzyme catalyzing the hydration of various nitriles to the corresponding amides
-
-
-
additional information
?
-
Pseudomonas putida NRRL-18668
-
roles of second- and third-shell residues of the active site structure in catalysis, overview. Three of the predicted second-shell residues, alpha-Asp164, beta-Glu56, and beta-His147, and one predicted third-shell residue, beta-His71, have significant effects on the catalytic efficiency of the enzyme, while one of the predicted residues, alpha-Glu168, and the three residues not predicted, alpha-Arg170, alpha-Tyr171, and beta-Tyr215, do not have any significant effects on the catalytic efficiency of the enzyme
-
-
-
additional information
?
-
Pseudonocardia thermophila JCM 3095
-
NHase hydrates a nitrile to provide the corresponding amide product via an addition reaction of one water molecule, active site structure involving amidate nitrogen donors from the peptide backbone, overview
-
-
-
additional information
?
-
Pseudonocardia thermophila JCM 3095
-
computational molecular dynamics modelling of ligand docking and substrate transport and binding, overview
-
-
-
additional information
?
-
Brevibacterium sp. R312
-
wide substrate spectrum
-
-
-
additional information
?
-
Rhodococcus sp. RHA1
-
no detectably transformation with 2-methyl-2-butenenitrile, benzonitrile and phenylacetonitrile
-
-
-
additional information
?
-
Pseudomonas putida 5B
-
S enantiomer conversion is 14 times greater than the rate of R enantiomer conversion
-
-
-
additional information
?
-
Pseudomonas chlororaphis B23
-
specificity overview, aromatic nitriles are barely hydrated by the enzyme, formamide, acetamide, acrylamide, propionamide, n-butyramide, isobutyramide, n-valeramide, succinamide, benzamide, phenylacetamide and lactamide are no substrates
-
-
-
additional information
?
-
Pseudomonas chlororaphis B23
-
-
-
-
-
additional information
?
-
Pseudomonas chlororaphis B23
-
methacrylamide-induced enzyme activity, no activity in absence of methacrylamide, no or reduced activity in NhpR transcriptional regulator defective mutants
-
-
-
additional information
?
-
Rhodococcus rhodochrous J1
-
NhhG forms a complex with the alpha-subunit of H-NHase. NhhAG is very similar to the mediator of L-NHase, NhlAE, which is a heterotrimer complex consisting of the cobalt-containing alpha-subunit of L-NHase and NhlE
-
-
-
additional information
?
-
Rhodococcus rhodochrous J1
-
H-NHase acts preferentially on aliphatic nitriles, while L-NHase has a higher affinity for aromatic nitriles
-
-
-
additional information
?
-
Rhodococcus rhodochrous J1
-
specificity overview
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2,2-dimethylcyclopropanecarbonitrile + H2O
2,2-dimethylcyclopropanecarbamide
show the reaction diagram
Rhodococcus qingshengii, Rhodococcus qingshengii ZA0707
-
-
-
-
?
2-amino-2,3-dimethylbutyronitrile + H2O
2-amino-2,3-dimethylbutyramide
show the reaction diagram
-
-
-
-
?
2-amino-2,3-dimethylbutyronitrile + H2O
2-amino-2,3-dimethylbutyramide
show the reaction diagram
-
-
-
-
?
2-amino-2,3-dimethylbutyronitrile + H2O
2-amino-2,3-dimethylbutyramide
show the reaction diagram
Rhodococcus boritolerans, Rhodococcus boritolerans CCTCC M 208108, Bacillus subtilis CCTCC M 206038, Alcaligenes faecalis CCTCC M 208168, Rhodococcus ruber CCTCC M 206040, Serratia marcescens CCTCC M 208231, Rhodococcus sp. N595
-
-
-
-
?
2-methyl-3-butenenitrile + H2O
?
show the reaction diagram
-
-
-
-
?
3-chlorobenzonitrile + H2O
3-chlorobenzamide
show the reaction diagram
-
-
-
-
?
3-cyanopyridine + H2O
nicotinamide
show the reaction diagram
-
-
-
-
?
3-cyanopyridine + H2O
nicotinamide
show the reaction diagram
-
a step in the biosynthesis of nicotinamide, one of the important forms of vitamin B3
-
-
?
3-cyanopyridine + H2O
nicotinamide
show the reaction diagram
-
NHase-AMase cascade system exploited in a continuous reactor configuration, including nitrile hydratase and amidase, EC 3.5.1.4, activity. Bioconversion to intermediate nicotinamide and further to nicotinic acid
-
-
?
3-cyanopyridine + H2O
nicotinamide
show the reaction diagram
Rhodococcus erythropolis MTCC 1526
-
-
-
-
?
3-cyanopyridine + H2O
nicotinamide
show the reaction diagram
Rhodococcus erythropolis MTCC 1526
-
a step in the biosynthesis of nicotinamide, one of the important forms of vitamin B3
-
-
?
3-cyanopyridine + H2O
nicotinamide
show the reaction diagram
Microbacterium imperiale CBS 498-74
-
NHase-AMase cascade system exploited in a continuous reactor configuration, including nitrile hydratase and amidase, EC 3.5.1.4, activity. Bioconversion to intermediate nicotinamide and further to nicotinic acid
-
-
?
3-hydroxybenzonitrile + H2O
3-hydroxybenzamide
show the reaction diagram
-
-
-
-
?
3-tolunitrile + H2O
?
show the reaction diagram
-
-
-
-
?
4-aminobenzonitrile + H2O
4-aminobenzamide
show the reaction diagram
-
-
-
-
?
4-chlorobenzonitrile + H2O
4-chlorobenzamide
show the reaction diagram
-
-
-
-
?
acetonitrile + H2O
acetamide
show the reaction diagram
Rhodococcus qingshengii, Rhodococcus qingshengii ZA0707
-
-
-
-
?
acrylonitrile + H2O
acrylamide
show the reaction diagram
-
-
-
-
?
acrylonitrile + H2O
acrylamide
show the reaction diagram
-
-
-
-
?
acrylonitrile + H2O
acrylamide
show the reaction diagram
-
-
-
-
?
acrylonitrile + H2O
acrylamide
show the reaction diagram
Mesorhizobium sp.
-
-
-
-
?
acrylonitrile + H2O
acrylamide
show the reaction diagram
-
-
-
-
?
acrylonitrile + H2O
acrylamide
show the reaction diagram
Rhodococcus ruber TH
-
-
-
-
?
acrylonitrile + H2O
acrylamide
show the reaction diagram
Pseudonocardia thermophila JCM 3095
-
-
-
-
?
acrylonitrile + H2O
acrylamide
show the reaction diagram
Rhodococcus qingshengii ZA0707
-
-
-
-
?
an aliphatic amide
a nitrile + H2O
show the reaction diagram
Rhodococcus erythropolis, Pseudonocardia thermophila, Rhodococcus erythropolis N-771, Pseudonocardia thermophila JCM 3095
-
-
-
-
?
benzonitrile + H2O
benzoic acid amide
show the reaction diagram
Mesorhizobium sp.
-
-
-
-
?
benzonitrile + H2O
benzamide
show the reaction diagram
-
performed by a cascade bienzymatic reaction involving nitrile hydration and acyl transfer of the intermediate benzamide onto hydroxylamine. The first step is catalyzed by a cell-free extract from recombinant Escherichia coli strain expressing nitrile hydratase from Klebsiella oxytoca strain 38.1.2, the second step is cell-free extract from Rhodococcus erythropolis A4 amidase, EC 3.5.1.4
-
-
?
benzonitrile + H2O
benzamide
show the reaction diagram
-
performed by a cascade bienzymatic reaction involving nitrile hydration and acyl transfer of the intermediate benzamide onto hydroxylamine. The first step is catalyzed by a cell-free extract from recombinant Escherichia coli strain expressing nitrile hydratase from Raoultella terrigena srain 77.1, the second step is a cell-free extract from Rhodococcus erythropolis A4 amidase, EC 3.5.1.4
-
-
?
benzonitrile + H2O
benzamide
show the reaction diagram
Klebsiella oxytoca 38.1.2
-
performed by a cascade bienzymatic reaction involving nitrile hydration and acyl transfer of the intermediate benzamide onto hydroxylamine. The first step is catalyzed by a cell-free extract from recombinant Escherichia coli strain expressing nitrile hydratase from Klebsiella oxytoca strain 38.1.2, the second step is cell-free extract from Rhodococcus erythropolis A4 amidase, EC 3.5.1.4
-
-
?
benzonitrile + H2O
benzamide
show the reaction diagram
Raoultella terrigena 77.1
-
performed by a cascade bienzymatic reaction involving nitrile hydration and acyl transfer of the intermediate benzamide onto hydroxylamine. The first step is catalyzed by a cell-free extract from recombinant Escherichia coli strain expressing nitrile hydratase from Raoultella terrigena srain 77.1, the second step is a cell-free extract from Rhodococcus erythropolis A4 amidase, EC 3.5.1.4
-
-
?
benzonitrile + hydroxylamine + H2O
benzohydroxamic acid + NH3
show the reaction diagram
Rhodococcus erythropolis, Rhodococcus erythropolis A4
-
performed by a cascade bienzymatic reaction involving nitrile hydration and acyl transfer of the intermediate benzamide onto hydroxylamine. The first step is catalyzed by a cell-free extract from Rhodococcus erythropolis A4 containing nitrile hydratase, the second step is a cell-free extract from Rhodococcus erythropolis A4 amidase, EC 3.5.1.4
-
-
?
butyronitrile + H2O
butyramide
show the reaction diagram
-
-
-
-
?
butyronitrile + H2O
butyramide
show the reaction diagram
-
-
-
-
?
butyronitrile + H2O
butyramide
show the reaction diagram
Klebsiella oxytoca 38.1.2, Raoultella terrigena 77.1
-
-
-
-
?
butyronitrile + H2O
butyramide
show the reaction diagram
Rhodococcus qingshengii ZA0707
-
-
-
-
?
indole-3-acetonitrile + H2O
(indole-3-yl)acetamide
show the reaction diagram
-
-
-
?
indole-3-acetonitrile + H2O
(indol-3-yl)acetamide
show the reaction diagram
Sinorhizobium meliloti, Agrobacterium tumefaciens, Rhizobium leguminosarum, Mesorhizobium loti, Mesorhizobium loti 02-10055, Mesorhizobium loti 02-10056, Agrobacterium tumefaciens IAM B-261, Rhizobium leguminosarum 02-03119, Sinorhizobium meliloti 03-03046, Mesorhizobium loti 02-10101, Rhizobium leguminosarum 02-10230, Rhizobium leguminosarum 02-10041
-
-
-
-
?
isobutyronitrile + H2O
isobutyric acid amide
show the reaction diagram
Mesorhizobium sp.
-
-
-
-
?
isobutyronitrile + H2O
isobutyramide
show the reaction diagram
-
-
-
-
?
phenylacetonitrile + 2 H2O
phenylacetic acid + NH3
show the reaction diagram
-
-
-
?
propionitrile + H2O
propionic acid amide
show the reaction diagram
Mesorhizobium sp.
-
-
-
-
?
propionitrile + H2O
propionamide
show the reaction diagram
-
-
-
-
?
propionitrile + H2O
propionamide
show the reaction diagram
-
-
-
-
?
propionitrile + H2O
propionamide
show the reaction diagram
Klebsiella oxytoca 38.1.2, Raoultella terrigena 77.1
-
-
-
-
?
propionitrile + H2O
propionic acid amide
show the reaction diagram
Mesorhizobium sp. BNC1
-
-
-
-
?
propionitrile + H2O
propionamide
show the reaction diagram
Rhodococcus qingshengii ZA0707
-
-
-
-
?
valeronitrile + H2O
valeramide
show the reaction diagram
-
-
-
-
?
isobutyronitrile + H2O
isobutyric acid amide
show the reaction diagram
Mesorhizobium sp. BNC1
-
-
-
-
?
additional information
?
-
-
methacrylamide-induced enzyme activity, no activity in absence of methacrylamide, no or reduced activity in NhpR transcriptional regulator defective mutants
-
-
-
additional information
?
-
-
NHase is a non-heme iron enzyme catalyzing the hydration of various nitriles to the corresponding amides
-
-
-
additional information
?
-
-
NhhG forms a complex with the alpha-subunit of H-NHase. NhhAG is very similar to the mediator of L-NHase, NhlAE, which is a heterotrimer complex consisting of the cobalt-containing alpha-subunit of L-NHase and NhlE
-
-
-
additional information
?
-
-
substrate specificity of strain 38.1.2, no activity with 4-tolunitrile, overview
-
-
-
additional information
?
-
-
substrate specificity of strain 77.1, no activity with 4-tolunitrile and 3-chlorobenzonitrile, overview
-
-
-
additional information
?
-
-
the nitrile hydratase can hydrate aliphatic, aromatic and heterocyclic nitriles under very mild conditions, in mixtures of pH 7 buffer and a range of organic solvents, often with excellent chemoselectivity. Major determinant of hydration occurring is the degree of steric hindrance around the nitrile moiety and/or size of the substrates
-
-
-
additional information
?
-
-
the thermoactive nitrilase from Pyrococcus abyssi hydrolyses small aliphatic nitriles like fumaro- and malononitril, docking calculations for fumaro- and malononitriles, modelling, overview
-
-
-
additional information
?
-
Klebsiella oxytoca 38.1.2
-
substrate specificity of strain 38.1.2, no activity with 4-tolunitrile, overview
-
-
-
additional information
?
-
-
the nitrile hydratase can hydrate aliphatic, aromatic and heterocyclic nitriles under very mild conditions, in mixtures of pH 7 buffer and a range of organic solvents, often with excellent chemoselectivity. Major determinant of hydration occurring is the degree of steric hindrance around the nitrile moiety and/or size of the substrates
-
-
-
additional information
?
-
Raoultella terrigena 77.1
-
substrate specificity of strain 77.1, no activity with 4-tolunitrile and 3-chlorobenzonitrile, overview
-
-
-
additional information
?
-
Rhodococcus sp. N771
-
NHase is a non-heme iron enzyme catalyzing the hydration of various nitriles to the corresponding amides
-
-
-
additional information
?
-
Pseudomonas chlororaphis B23
-
methacrylamide-induced enzyme activity, no activity in absence of methacrylamide, no or reduced activity in NhpR transcriptional regulator defective mutants
-
-
-
additional information
?
-
Rhodococcus rhodochrous J1
-
NhhG forms a complex with the alpha-subunit of H-NHase. NhhAG is very similar to the mediator of L-NHase, NhlAE, which is a heterotrimer complex consisting of the cobalt-containing alpha-subunit of L-NHase and NhlE
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
pyrroloquinoline quinone
-
prosthetic group, covalently bound pyrroloquinoline quinone, PQQ or a compound which closely resembles PQQ
pyrroloquinoline quinone
-
-
pyrroloquinoline quinone
-
-
pyrroloquinoline quinone
-
-
pyrroloquinoline quinone
-
-
pyrroloquinoline quinone
-
-
pyrroloquinoline quinone
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
acetate
-
the acetate ion binds close to Mg2+, and it interacts with two coordinating water molecules
BaCl2
-
1 mM, relative activity: 101.1%
CaCl2
-
1 mM, relative activity: 102.0%
Co2+
-
enzyme of J1 strain contains cobalt; plays a role in the stabilization of the polypeptide structure
Co2+
-
0.1% w/v, greatly increases the enzyme activity. Different Co2+ compounds increase the enzyme activity; 5.7 atoms cobalt/mol enzyme, tightly bound to the protein; enzyme of J1 strain contains cobalt; indispensable for high enzyme activity
Co2+
-
contains approximately 11-12 mol cobalt/mol enzyme
Co2+
-
cannot replace ferrous or ferric ions
Co2+
-
indispensable for high enzyme activity; induces the enzyme activity
Co2+
-
incorporated instead of Fe into the catalytic site with initial weak activity that increases when an oxidizing agent is added
Co2+
-
requirement, 1.7 mol cobalt/mol enzyme
Co2+
-
addition at 0.001% results in 68fold enhancement of activity
Co2+
Q2UZQ5, Q2UZQ6
;
Co2+
-
component of enzyme, one ion per holoenzyme, ICP-MS; increase of activity of EDTA-dialysed enzyme, 120% activity
Co2+
-
no enzyme activity in medium without cobalt
Co2+
-
incorporation of cobalt into L-NHase depends on the alpha-subunit exchange between cobalt-free, apo-L-NHase and its cobalt-containing mediator, NhlAE, i.e. holo-NhlAE, in a mode of post-translational maturation, i.e. self-subunit swapping. NhlE is recognized as a self-subunit swapping chaperone. Incorporation of cobalt into H-NHase also occurs via self-subunit swapping. Cobalt is inserted into cobalt-free, apo-NhhAG, but not into apo-H-NHase, suggesting that NhhG functions not only as a self-subunit swapping chaperone but also as a metallochaperone. Formation of large-sized complexes during self-subunit swapping in H-NHase. Self-subunit swapping mechanism, detailed overview
Co2+
-
enzyme-bound
Co3+
-
CD spectrum suggests low-spin Co3+ in tetragonally-distorted octahedral ligand field
Co3+
-
contains nonheme iron or noncorrin cobalt, the ion is bound buried in the protein core at the interface of two domains alpha and beta
Co3+
-
the unique active site structure of metalloenzyme nitrile hydratase includes a central metal ion, Co3+ or Fe3+, coordinated octahedrally by two amide nitrogens from the peptide backbone, one cysteine sulfur and two oxidized cysteine sulfurs, Cys-SO and Cys-SO2
Co3+
-
the enzyme belongs to the CoIII-NHase group of enzymes, octahedrally coordinated metal ion with two deprotonated backbone amides as ligands as well as three cysteine residues, two of which are posttranslationally oxidized to cysteine-sulfenic and cysteine-sulfinic acids
Co3+
Q7SID2
a Co-type NHase, Co3+ coordinated to a water molecule forms a Co-OH complex mediated by the oxidized alpha-CEA113
Co3+
Mesorhizobium sp.
-
a cobalt-containing NHase in strain F28
Co3+
-
the incorporation of cobalt into L-NHase is depend on the alpha-subunit exchange between apo-L-NHase and NhlAE, cobalt is inserted into both the cobaltfree maturation mediator NhlAE (apo-NhlAE) and the cobalt-free alpha-subunit in an NhlE-dependent manner in the presence of cobalt and dithiothreitol in vitro
Cobalt
-
belongs to the cobalt NHase family of enzymes
CoCl2
-
1 mM, relative activity: 106.4%
Cu2+
-
component of enzyme, two ions per holoenzyme, ICP-MS
Fe2+
-
non-heme iron enzyme with a typical low-spin Fe(III)-active center
Fe2+
-
enzyme of sp. N-774 contains ferric iron
Fe2+
-
a protein-bound six-coordinate mononuclear non-heme iron with a mixed sulfur and nitrogen or oxygen coordination sphere. Three of the five cysteines in the enzyme in a tentatively assigned metal binding site
Fe2+
-
contains approximately 3 g-atoms iron/mol enzyme, tightly bound to the protein
Fe2+
-
at 0.1% w/v does not enhance the enzyme activity
Fe2+
-
the enzyme contains iron
Fe2+
-
direct binding of the substrate to the Fe(III)-active site of the enzyme; non-heme iron enzyme with a typical low-spin Fe(III)-active center
Fe2+
-
contains approximately 4 mol iron/mol enzyme
Fe2+
-
0.01 mM ferric citrate increases the enzyme activity; non-heme ferric iron in the catalytic center
Fe2+
-
ferric citrate has no effect on the enzyme activity
Fe2+
-
ferrous or ferric ions greatly increase the enzyme activity; non-heme iron enzyme with a typical low-spin Fe(III)-active center
Fe2+
-
two mol iron/mol of enzyme
Fe2+
-
non-heme iron enzyme with a typical low-spin Fe(III)-active center
Fe2+
-
enzyme-bound
Fe3+
-
contains nonheme iron or noncorrin cobalt, the ion is bound buried in the protein core at the interface of two domains alpha and beta, photosensitivity of the Fe-type NHase
Fe3+
-
the unique active site structure of metalloenzyme nitrile hydratase includes a central metal ion, Co3+ or Fe3+, coordinated octahedrally by two amide nitrogens from the peptide backbone, one cysteine sulfur and two oxidized cysteine sulfurs, Cys-SO and Cys-SO2
Fe3+
-
the enzyme belongs to the FeIII-NHase group of enzymes, octahedrally coordinated metal ion with two deprotonated backbone amides as ligands as well as three cysteine residues, two of which are posttranslationally oxidized to cysteine-sulfenic and cysteine-sulfinic acids
Fe3+
-
NHase N'4 is a Fe-type enzyme with a Cys109-Ser110-Leu111-Cys112-Ser113-Cys114 sequence
Fe3+
-
a Fe-type NHase
Fe3+
-
non-heme iron enzyme
Fe3+
-
has an unusual Fe3+ center with two modified Cys ligands
Iron
-
non-heme iron center
Mg2+
-
increase of activity of EDTA-dialysed enzyme, 130% activity
Na2MoO4
-
1 mM, relative activity: 102.1%
Zn2+
-
component of enzyme, one ion per holoenzyme, ICP-MS
Mg2+
-
Mg2+ bound in chain B interacts with five water molecules and Asn49B
additional information
-
CuSO4, CaCl2, ZnSO4, MnCl2, NaMnO4, FeCl3, FeSO4, AlCl3, BaCl2, SrCl2, NaWO4, SnCl2, BeSO4, NiCl2, PbCl2, LiCl and CoCl2 at 0.1% w/v neither inhibit nor enhance the enzyme activity
additional information
-
not: Fe2+
additional information
-
metal content is unusual for NHases
additional information
-
redox potentials and structures of metal ion-enzyme complexes, overview
additional information
-
nitrile hydratase is a metalloenzyme
additional information
-
specific binding of the carboxylate group, as well as a more general electrostatic preference for negatively charged ligands revealed by binding of the Br- ions, overview
additional information
-
the Agrobacterium tunefaciens enzyme does not contain Be, B, Mg, Al, Si, P, S, Ca, Ti, V, Cr, Mn, Ni, Cu, Zn, Se, Sr, Zr, Mo, Pd, Ag, Cd, Sn, Sb, Ba, Ta, W, Pt, Au, Hg, Pb, La, or Ce
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(NH4)2S2O8
Mesorhizobium sp.
-
23% inhibition at 10 mM, 22% inhibition at 1 mM
1,10-phenanthroline
-
1 mM
1,10-phenanthroline
-
1-5 mM
1,10-phenanthroline
-
39% reduced activity at 1 mM
2,2'-dipyridyl
-
1-5 mM
2-mercaptoethanol
-
-
2-mercaptoethanol
-
9% reduced activity at 1 mM
2-Nitrophenol
-
10 microM, 40-50% residual activity of NilFe, 90% residual activity of NilCo
3-Cyanopyridine
-
the soluble enzyme shows about 15% residual activity at 500 mM 3-cyanopyridine, NHase immobilized to EupergitC and cross-linked with 1-ethyl-3-(dimethylamino-propyl) carbodiimide shows approximately 50% reduction in 3-cyanopyridine inhibition (about 65% residual activity at 500 mM 3-cyanopyridine)
3-Nitrophenol
-
10 microM, 40-50% residual activity of NilFe, fully active NilCo
4-nitrophenol
-
10 microM, 40-50% residual activity of NilFe, 80% residual activity of NilCo
5-Aminotetrazol monohydrate
-
-
7-Chloro-4-nitrobenzo-2-oxa-1,3-diazole
-
-
8-hydroxyquinoline
-
-
acetamide
-
10 mM, product inhibition, reduction of acrylonitrile degrading activity from 1.2 micromol/min/mg to 1.0 micromol/min/mg
acetate
Corynebacterium nitrilophilus
-
-
Acrylamide
Q8GJG6, Q8GJG7
mutant enzyme S122C shows higher tolerance under increasing acrylamide levels than recombinant NHase with modified start codon only
Acrylamide
-
when the concentration of acrylamide is higher than 150 g/l, the activity of the immersed-NHase in free resting cells is significantly reduced, when the concentration is higher than 250 g/l, the deactivation is more serious and the half-life of the NHase is less than 120 min
acrylonitrile
-
above > 40 g/l
Adipamic acid
-
-
Adipic acid
-
not inhibitory
Ag+
-
complete inhibition at 1 mM of AgNO3
Ag+
Corynebacterium nitrilophilus
-
-
Ag+
-
0.01-1 mM AgNO3
Ag+
-
0.01-1 mM AgNO3
Ag2SO3
Mesorhizobium sp.
-
complete inhibition at 1 mM
Ag2SO4
-
total inhibition at 1 mM, L-NHase
AgNO3
-
1 mM, complete inhibition of the enzyme
AgNO3
-
complete inhibition at 1 mM
ammonium persulfate
-
1 mM, relative activity: 0.3%
ammonium persulfate
-
52% reduced activity at 1 mM
ammonium persulfate
-
4.5% inhibition at 1 mM
BaCl2
-
weak inhibition
Ca2+
-
10% inhibition at 1 mM
Cd2+
-
8% inhibition at 1 mM
CO
-
inhibition of NilCo, reversible by photoactivation, no inhibition of NilFe
Co2+
-
2% inhibition at 1 mM
cobalt chloride
-
20% reduced activity at 1 mM
copper sulfate
-
95% reduced activity at 1 mM
-
Cu2+
Corynebacterium nitrilophilus
-
-
Cu2+
-
1-5 mM CuSO4
Cu2+
-
85% inhibition at 10 mM
Cu2+
-
1 mM CuCl2
Cu2+
-
7% inhibition at 1 mM
CuCl2
-
1 mM, relative activity: 4.8%
CuCl2
-
1 mM, strong inhibition of EDTA-dialysed enzyme, 19% remaining activity
CuSO4
Mesorhizobium sp.
-
62% inhibition at 10 mM, 35% inhibition at 1 mM
Cyanovaleramide
-
-
Cyanovaleric acid
-
-
cysteamine
-
1 mM, 20 min at 15C
diethyldithiocarbamate
-
0.1 mM
diisopropylfluorophosphate
-
0.05 mM, 100% inhibition
Disodium 4,5-dihydroxy-m-benzene disulfonate
-
0.1-5 mM
dithiothreitol
-
18% reduced activity at 1 mM
EDTA
-
1 mM, relative activity: 96.2%
EDTA
-
15% reduced activity at 1 mM
EDTA
Mesorhizobium sp.
-
64% inhibition at 10 mM, 22% inhibition at 1 mM
EDTA
-
12.1% inhibition at 1 mM
ethanolamine
-
markedly lower activity
Fe2+
-
1 mM, inhibition of EDTA-dialysed enzyme, 38% remaining activity
-
Fe2+
Mesorhizobium sp.
-
22% inhibition at 10 mM, 11% inhibition at 1 mM
-
Fe2+
-
5% inhibition at 1 mM
-
Ferrous sulfate
-
54% reduced activity at 1 mM
FeSO4
-
1-5 mM, weak inhibition
Glutaraldehyde
-
0.05 mM, 58% inhibition
glutaronitrile
-
-
H2O2
-
1 mM, no effect on L-NHase activity
H2O2
Mesorhizobium sp.
-
89% inhibition at 10 mM, 29% inhibition at 1 mM
Hexanoic acid
-
IC50 of 2 mM
Hg+
-
Hg2Cl2, 1 mM, total inhibition, L-NHase
Hg+
-
89.3% inhibition at 1 mM
Hg2+
-
complete inhibition at 0.01 mM Hg2+
Hg2+
Corynebacterium nitrilophilus
-
-
Hg2+
-
complete inactivation at 0.05 mM Hg2+; HgCl2, 0.01-1 mM
Hg2+
-
10 mM, 90% inhibition
Hg2+
-
HgCl2, 0.01-1 mM
Hg2+
-
HgCl2, 0.01-1 mM
Hg2+
-
HgCl2, 0.01-1 mM
hydrogen peroxide
-
1 mM, relative activity: 0%
hydrogen peroxide
-
97% reduced activity at 1 mM
hydroxylamine
-
1 mM, 20 min at 15C
hydroxylamine
-
1 mM
hydroxylamine
-
90.6% inhibition
hydroxylamine
-
62.6% inhibition at 1 mM
iodoacetamide
-
1 mM, relative activity: 68.6%
iodoacetamide
-
22% reduced activity at 1 mM
iodoacetic acid
-
-
iodoacetic acid
-
-
iodoacetic acid
-
at 0.05 mM, 27% inhibition
iodoacetic acid
-
1 mM, relative activity: 93.0%
iodoacetic acid
-
65% inhibition at 1 mM
Isobutyronitrile
-
-
Isobutyronitrile
-
-
KCN
-
complete inhibition at 0.1 mM, competitive with acetonitrile as substrate
KCN
-
weak inhibition at 1 mM
L-ascorbic acid
-
54.6% inhibition at 1 mM
LiCl
-
1 mM, relative activity: 97.3%
Mercury chloride
-
89% reduced activity at 1 mM
Mg2+
Mesorhizobium sp.
-
59% inhibition at 10 mM, 16% inhibition at 1 mM
Mg2+
-
4% inhibition at 1 mM
MgCl2
-
1 mM, relative activity: 73.7%
Mn2+
-
MnCl2, 1 mM
N,N-Dimethylacetamide
-
-
N-bromosuccinimide
-
-
N-bromosuccinimide
-
100% inhibition at 0.005 mM
N-bromosuccinimide
-
1 mM, relative activity: 0.2%
n-butyric acid
-
competitive inhibitor. Complete inhibition beyond 40 mM. IC50 of 4 mM at pH 7.2 in Hepes buffer 100 mM, IC50 of 8 mM at pH 7.2 in sodium phosphate buffer 100 mM, IC50 of 0.8 mM at pH 6.2 in sodium phosphate buffer 100 mM, IC50 of 12 mM at pH 8.2 in sodium phosphate buffer 100 mM
n-butyric acid
-
-
n-butyric acid
-
competitive inhibitor
NaCN
-
non-competitive inhibition
NaNO2
-
NilFe is unaffected by NaNO2
NEM
-
68% inhibition at 0.05 mM
NO
-
reversible inhibition, for recombinant enzyme
NO
-
inhibition of NilCo and NilFe, reversible by photoactivation with 150 W white light
NO
-
Substantial structural changes upon NO ligand binding to the iron center, indicating that some mechanical signals are sent upon NO photodissociation, determination NO diffusion paths in NHase, overview
p-chloromercuribenzoate
-
strong inhibition at 1 mM
p-chloromercuribenzoate
-
1 mM
p-chloromercuribenzoate
-
0.1 mM
Pb2+
-
94.5% inhibition at 1 mM
Penicillamine
-
1 mM, 20 min at 15C; L- and D-isomer
Penicillamine
-
1 mM; L- and D-isomer
phenyl hydrazine
-
68% inhibition at 1 mM
phenylhydrazine
-
1 mM
phenylhydrazine
-
1 mM, 20 min at 15C, irreversible
phenylhydrazine
-
1 mM
phenylhydrazine
-
1 mM
phenylhydrazine
-
100% inhibition
phenylmercuric acetate
-
strong inhibition
PMSF
-
83% reduced activity at 1 mM
propioamide
-
10 mM, product inhibition, reduction of acrylonitrile degrading activity from 1.2 micromol/min/mg to 0.91 micromol/min/mg
Propionamide
-
weak inactivation
Semicarbazide
-
1 mM, 20 min at 15C
Semicarbazide
-
1 mM, weak inhibition
Silver nitrate
-
82% reduced activity at 1 mM
Sodium azide
-
1 mM, relative activity: 61.3%
Sodium azide
Mesorhizobium sp.
-
74% inhibition at 10 mM, 22% inhibition at 1 mM
Sodium azide
-
26.6% inhibition at 1 mM
sulfhydryl reagents
-
-
sulfhydryl reagents
-
1 mM
tert-butylisonitrile
-
substrate inhibition, a Dixon plot shows the reciprocal values of the rate of methacrylonitrile hydration as a function of tert-butylisonitrile concentration, overview
tertiary-butyl isonitrile
-
NilFe is unaffected by tertiary-butyl isonitrile
Thioacetamide
-
-
Thiocyanate
-
weak
Urea
-
13.9% inhibition at 1 mM
Valeric acid
-
IC50 of 0.5 mM
zinc chloride
-
56% reduced activity at 1 mM
Zn2+
-
weak; ZnCl2, 1 mM
Zn2+
-
ZnCl2, 1 mM
Zn2+
-
1 mM, inhibition of EDTA-dialysed enzyme, 56% remaining activity
Zn2+
Mesorhizobium sp.
-
71% inhibition at 10 mM, 54% inhibition at 1 mM
ZnCl2
-
1 mM, relative activity: 77.6%
ZnSO4
-
1 mM, relative activity: 99.5%
Mn2+
-
8% inhibition at 1 mM
additional information
Corynebacterium nitrilophilus
-
activity is strongly and reversibly inhibited by alpha-amino and alpha-hydroxynitriles
-
additional information
-
high concentrations of acrylonitrile inhibit the enzyme activity
-
additional information
-
maleic, succinic, glutaric and pimelic acid do not act as inhibitors
-
additional information
-
enzyme is inactive in the dark due to an endogenous nitric oxide molecule bound to the iron center, and is activated by photodissociation
-
additional information
Mesorhizobium sp.
-
no inhibition by 2-mercaptoethanol
-
additional information
-
not inhibited by dithiothreitol, phenylmethylsulfonylfluoride, and beta-mercaptoethanol
-
additional information
-
the enzyme from Alcaligenes faecalis strain CCTCC M 208168 is resistant to inhibition by cyanide
-
additional information
-
the enzyme from Bacillus subtilis CCTCC M 206038 is resistant to inhibition by cyanide
-
additional information
-
the enzyme from Rhodococcus boritolerans strain CCTCC M 208108 is resistant to inhibition by cyanide
-
additional information
-
the enzyme from Rhodococcus ruber strain CCTCC M 206040 is resistant to inhibition by cyanide
-
additional information
-
the enzyme from Rhodococcus sp. {G20} is resistant to inhibition by cyanide; the enzyme from Rhodococcus sp. strain N595 is resistant to inhibition by cyanide; the enzyme from Rhodococcus sp. strain P4 is resistant to inhibition by cyanide; the enzyme from Rhodococcus sp. strain ZA0707 is resistant to inhibition by cyanide
-
additional information
-
the enzyme from Serratia marcescens CCTCC M 208231 is resistant to inhibition by cyanide
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
acrylonitrile
-
below
crotonamide
-
induces high and low molecular mass forms of the enzyme
cyclohexanecarboxamide
-
induces the low molecular mass form of the enzyme
Dimethylformamide
-
addition to increase the accessibility of nitrile groups at concentration no higher than 0.5% is beneficial for activity
Glycine-NaOH
-
activates
light
Corynebacterium nitrilophilus
-
effective wavelength: 370 nm
-
light
-
-
-
light
-
restores activity inhibited by NO
-
light
-
the enzyme activity is increased by exposure to near ultra-violet light
-
nitric oxide
-
the inactive (dark form) nitric oxide-bound enzyme is activated when exposed to light via the release of nitric oxide from the iron center
P14 protein
-
protein encoded in an open frame of the structural frames that is essential for optimal activity of NHase over-produced in Escherichia coli
-
potassium hexacyanoferrate
-
oxidizing agent that activates the Co-substituted enzyme by oxidizing the Co2+ atom and/or modification of a alphaCys-112 to cysteine-sulfinic acid
Urea
-
induces the high molecular mass form of the enzyme
Urea
Q2UZQ5, Q2UZQ6
required; required
methacrylamide
-
induces the enzyme
additional information
-
enzyme is inactive in the dark due to an endogenous nitric oxide molecule bound to the iron center, and is activated by photodissociation
-
additional information
-
the enzyme is activated by absorption of photons of wavelength of about 630 nm
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.71
-
2-cyanopyrazine
-
pH 7.0, 20C, L-NHase
10
-
2-cyanopyrazine
-
pH 7.0, 20C, H-NHase
0.56
-
2-Cyanopyridine
-
pH 7.0, 20C, L-NHase
5.3
-
2-Cyanopyridine
-
soluble NHase, at 50C
21.7
-
2-Cyanopyridine
-
pH 7.0, 20C, H-NHase
0.25
-
2-nitro-5-thiocyanato-benzoic acid
-
pH 7.2, 28C, recombinant enzyme
0.6
-
2-nitro-5-thiocyanato-benzoic acid
-
pH 7.2, 28C, native enzyme
0.3
-
3-Cyanopyridine
-
pH 7.0, 20C, L-NHase
10.2
-
3-Cyanopyridine
-
soluble NHase, at 50C
17.3
-
3-Cyanopyridine
-
EupergitC-immobilized NHase, at 50C
167
-
3-Cyanopyridine
-
in 0.1 M potassium phosphate buffer, pH 8.0, at 40C
200
-
3-Cyanopyridine
-
pH 7.0, 20C, H-NHase
0.28
-
4-Cyanopyridine
-
pH 7.0, 20C, L-NHase
8.7
-
4-Cyanopyridine
-
soluble NHase, at 50C
18.5
-
4-Cyanopyridine
-
pH 7.0, 20C, H-NHase
45
-
4-Hydroxyphenylacetonitrile
-
suggestion from preliminary characterisation of nitrile hydratase activity in crude extracts
5.4
-
acetonitrile
-
+/- 0.3, 10 mM HEPES, pH 7.5, 37C, Michaelis-Menten behavior at acetonitrile concentrations from 0.1 mM to 50 mM
5.78
-
acetonitrile
-
pH 7, 30C
12.5
-
acetonitrile
-
pH 7, 25C
25
-
acetonitrile
-
pH 7, 30C
0.53
-
acrylonitrile
Mesorhizobium sp.
-
pH 7.5, 37C
0.88
-
acrylonitrile
-
pH 7, 30C
1.89
-
acrylonitrile
-
pH 7.0, 20C, H-NHase
1.89
-
acrylonitrile
-
-
1.89
-
acrylonitrile
-
pH 7.0, 20C, H-NHase
2.67
-
acrylonitrile
-
pH 7.0, 20C, L-NHase
6.4
-
acrylonitrile
-
+/- 0.3, 10 mM HEPES, pH 7.5, 37C
14
-
acrylonitrile
-
pH 7, 37C
16.6
-
acrylonitrile
-
pH 7, 25C
16.7
-
acrylonitrile
-
pH 7, 20C
17
-
acrylonitrile
-
pH 7.2, 28C, L-NHase
34.6
-
acrylonitrile
-
pH 7.0, 20C
82
-
acrylonitrile
Q8GJG6, Q8GJG7
recombinant NHase with modified start codon only
86
-
acrylonitrile
Q8GJG6, Q8GJG7
wild type NHase
95
-
acrylonitrile
-
-
210
-
acrylonitrile
-
pH 7.5, 25C
30
-
adiponitrile
-
R312 strain
38
-
adiponitrile
-
ACV2 mutant
0.05
-
Benzonitrile
-
pH 7.0, 20C, L-NHase
0.8
-
Benzonitrile
-
pH 7, 37C
28.6
-
Benzonitrile
-
pH 7.0, 20C, H-NHase
33.3
-
Benzonitrile
-
pH 7, 25C
1.9
-
Butyronitrile
-
+/- 0.2, 10 mM HEPES, pH 7.5, 37C
6.25
-
Chloroacetonitrile
-
pH 7.0, 20C, L-NHase
10.9
-
Chloroacetonitrile
-
pH 7, 30C
12.2
-
Chloroacetonitrile
-
pH 7.0, 20C, H-NHase
22.2
-
Chloroacetonitrile
-
pH 7.0, 20C
30.3
-
Chloroacetonitrile
-
pH 7, 20C
4.55
-
Crotononitrile
-
pH 7.0, 20C, L-NHase
4.88
-
Crotononitrile
-
pH 7.0, 20C, H-NHase
10
-
Cyanopyrazine
-
pH 7.0, 20C
156
-
Cyanovaleramide
-
R312 strain
370
-
Cyanovaleramide
-
ACV2 mutant
2.5
-
Cyanovaleric acid
-
pH 7.2, 28C, native enzyme
3.2
-
Cyanovaleric acid
-
pH 7.2, 28C, recombinant enzyme
21
-
Cyanovaleric acid
-
ACV2 mutant
28
-
Cyanovaleric acid
-
R312 strain
0.0079
-
indole-3-acetonitrile
-
-
0.0079
-
indole-3-acetonitrile
-
pH 7.5, temperature not specified in the publication
1.51
-
Isobutyronitrile
-
pH 7.0, 20C, L-NHase
1.85
-
Isobutyronitrile
-
pH 7.0, 20C, H-NHase
10
-
Isobutyronitrile
-
pH 7, 25C
0.28
-
Methacrylonitrile
-
mutant alphaQ90E, vmax: 280 micromol/min/mg
0.44
-
Methacrylonitrile
-
pH 7.0, 20C, L-NHase
0.68
-
Methacrylonitrile
-
wild type, vmax: 1200 micromol/min/mg
0.75
-
Methacrylonitrile
-
wild type enzyme, in 50 mM sodium phosphate, pH 7.5, at 22C
1.3
-
Methacrylonitrile
-
mutant enzyme S113A, in 50 mM sodium phosphate, pH 7.5, at 22C
1.9
-
Methacrylonitrile
-
mutant betaR56K, vmax: 2.5 micromol/min/mg
2.6
-
Methacrylonitrile
-
mutant alphaQ90N, vmax: 57 micromol/min/mg
3.8
-
Methacrylonitrile
-
-
6.76
-
Methacrylonitrile
-
pH 7.0, 20C
6.76
-
Methacrylonitrile
-
pH 7.0, 20C, H-NHase
8.77
-
Methacrylonitrile
-
pH 7, 30C
9.5
-
Methacrylonitrile
-
pH 7, 20C
0.65
-
n-butyronitrile
-
pH 7.0, 20C, L-NHase
1.03
-
n-butyronitrile
-
pH 7.0, 20C
8.3
-
n-butyronitrile
-
pH 7, 20C
10.8
-
n-butyronitrile
-
pH 7, 30C
21.7
-
n-butyronitrile
-
pH 7.0, 20C, H-NHase
0.32
-
n-valeronitrile
-
pH 6.7, 0C, recombinant mutant alphaR170N
1.8
-
n-valeronitrile
-
pH 6.7, 0C, recombinant mutant alphaD164N
2.33
-
n-valeronitrile
-
pH 7.0, 20C
2.7
-
n-valeronitrile
-
pH 6.7, 0C, recombinant mutant betaY215F
3.6
-
n-valeronitrile
-
pH 7, 20C
4.5
-
n-valeronitrile
-
pH 6.7, 0C, recombinant mutant alphaE168Q
6.6
-
n-valeronitrile
-
pH 6.7, 0C, recombinant wild-type enzyme
9.3
-
n-valeronitrile
-
pH 6.7, 0C, recombinant mutant alphaY171F
10
-
n-valeronitrile
-
pH 6.7, 0C, recombinant mutant betaH71L
15.3
-
n-valeronitrile
-
pH 6.7, 0C, recombinant mutant betaE56Q
20.1
-
n-valeronitrile
-
pH 6.7, 0C, recombinant mutant betaH71N
21.2
-
n-valeronitrile
-
pH 6.7, 0C, recombinant mutant betaH71F
26.4
-
n-valeronitrile
-
pH 6.7, 0C, recombinant mutant betaH147N
0.001
-
Phenylacetonitrile
-
-
0.01
-
Phenylacetonitrile
-
pH 7.5, temperature not specified in the publication
57
-
pivalonitrile
-
pH 7, 25C
0.38
-
Propionitrile
-
+/- 0.1, 10 mM HEPES, pH 7.5, 37C
1.89
-
Propionitrile
-
pH 7.0, 20C, L-NHase
1.9
-
Propionitrile
-
pH 7, 30C
1.92
-
Propionitrile
-
pH 7.0, 20C, H-NHase
6
-
Propionitrile
-
pH 7, 37C
8
-
Propionitrile
-
R312 strain
10.5
-
Propionitrile
-
pH 7, 20C
14.3
-
Propionitrile
-
pH 7, 25C
21.6
-
Propionitrile
-
pH 7.4, 10C
29.4
-
Propionitrile
-
pH 7.0, 20C
50
-
Propionitrile
-
ACV2 mutant
25
-
Succinonitrile
-
pH 7, 20C
3.06
-
trans-4-Cyanocyclohexane-1-carboxylic acid
-
-
16
-
Methacrylonitrile
-
pH 7.2, 25C
additional information
-
additional information
-
values for 12 different substrates, affinity increases as the side chain of the substrate becomes longer
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
enzyme-ligand complex kinetic constants, overview
-
additional information
-
additional information
-
thermodynamics
-
additional information
-
additional information
-
relative binding affinities of water, nitriles, and amides in a nitrile hydratase model, direct competition studies using ion complexes, e.g. five-coordinate iron dithiolate (N,N'-bis-(2'-methyl-2'-mercaptopropyl)-1-thia-4,7-diazacyclononane)iron(III) triflate or [LFe]OTf, detailed overview
-
additional information
-
additional information
-
recombinant wild-type and mutant enzymes, kinetics analysis, overview
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
443.3
-
2-Cyanopyridine
-
soluble NHase, at 50C
17.3
-
3-Cyanopyridine
-
EupergitC-immobilized NHase, at 50C
629.6
-
3-Cyanopyridine
-
soluble NHase, at 50C
59.05
-
4-Cyanopyridine
-
soluble NHase, at 50C
12.4
-
acetonitrile
-
-
41
-
acetonitrile
-
+/- 0.9, 10 mM HEPES, pH 7.5, 37C
2
8
acrylonitrile
-
+/- 0.5, 10 mM HEPES, pH 7.5, 37C
0.99
-
Butyronitrile
-
+/- 0.04, 10 mM HEPES, pH 7.5, 37C
0.0000065
-
Methacrylonitrile
-
mutant enzyme S113A, in 50 mM sodium phosphate, pH 7.5, at 22C
0.000016
-
Methacrylonitrile
-
wild type enzyme, in 50 mM sodium phosphate, pH 7.5, at 22C
120
-
Methacrylonitrile
-
mutant betaR56K
2600
-
Methacrylonitrile
-
mutant alphaQ90N
13000
-
Methacrylonitrile
-
mutant alphaQ90E
55000
-
Methacrylonitrile
-
wild type
0.0035
-
n-valeronitrile
-
pH 6.7, 0C, recombinant mutant betaE56Q
0.0045
-
n-valeronitrile
-
pH 6.7, 0C, recombinant mutant alphaD164N
0.01
-
n-valeronitrile
-
pH 6.7, 0C, recombinant mutant alphaR170N
0.012
-
n-valeronitrile
-
pH 6.7, 0C, recombinant mutant betaH147N
0.02
-
n-valeronitrile
-
pH 6.7, 0C, recombinant mutant betaH71L
0.025
-
n-valeronitrile
-
pH 6.7, 0C, recombinant mutant betaH71N
0.027
-
n-valeronitrile
-
pH 6.7, 0C, recombinant mutant betaH71F
0.04
-
n-valeronitrile
-
pH 6.7, 0C, recombinant mutant betaY215F
0.0617
-
n-valeronitrile
-
pH 6.7, 0C, recombinant mutant alphaE168Q
0.217
-
n-valeronitrile
-
pH 6.7, 0C, recombinant mutant alphaY171F
0.327
-
n-valeronitrile
-
pH 6.7, 0C, recombinant wild-type enzyme
2.6
-
Propionitrile
-
+/- 0.2, 10 mM HEPES, pH 7.5, 37C
30.7
-
Propionitrile
-
-
76.3
-
Valeronitrile
-
-
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0002
-
n-valeronitrile
-
pH 6.7, 0C, recombinant mutant betaE56Q
33843
0.00045
-
n-valeronitrile
-
pH 6.7, 0C, recombinant mutant betaH147N
33843
0.00121
-
n-valeronitrile
-
pH 6.7, 0C, recombinant mutant betaH71F
33843
0.00122
-
n-valeronitrile
-
pH 6.7, 0C, recombinant mutant betaH71N
33843
0.002
-
n-valeronitrile
-
pH 6.7, 0C, recombinant mutant betaH71L
33843
0.0025
-
n-valeronitrile
-
pH 6.7, 0C, recombinant mutant alphaD164N
33843
0.014
-
n-valeronitrile
-
pH 6.7, 0C, recombinant mutant alphaE168Q
33843
0.0152
-
n-valeronitrile
-
pH 6.7, 0C, recombinant mutant betaY215F
33843
0.023
-
n-valeronitrile
-
pH 6.7, 0C, recombinant mutant alphaY171F
33843
0.032
-
n-valeronitrile
-
pH 6.7, 0C, recombinant mutant alphaR170N
33843
0.05
-
n-valeronitrile
-
pH 6.7, 0C, recombinant wild-type enzyme
33843
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.002
-
7-Chloro-4-nitrobenzo-2-oxa-1,3-diazole
-
+/- 0.0005, NilFe; +/- 0.0008, NilCo
0.005
-
acrylonitrile
-
+/- 0.0005, NilCo
0.007
-
acrylonitrile
-
+/- 0.001, NilFe
283
-
acrylonitrile
-
-
3.8
-
Adipamic acid
-
ACV2 mutant
43
-
Adipamic acid
-
R312 strain
14.5
-
adipamide
-
ACV2 mutant
31
-
adipamide
-
R312 strain
35
-
Adipic acid
-
R312 strain
220
-
Adipic acid
-
ACV2 mutant
2.6
-
Butyric acid
-
+/- 0.2, substrate: methacrylonitrile, mutant betaR56K
5.1
-
Butyric acid
-
+/- 0.3, substrate: methacrylonitrile, mutant alphaQ90E
6.2
-
Butyric acid
-
+/- 0.9, substrate: methacrylonitrile, wild type
14
-
Butyric acid
-
+/- 2.7, substrate: methacrylonitrile, mutant alphaQ90N
12
-
Cyanovaleramide
-
R312 strain
73
-
Cyanovaleramide
-
ACV2 mutant
0.35
-
Cyanovaleric acid
-
R312 strain
5
-
Cyanovaleric acid
-
ACV2 mutant
0.0054
-
Isobutyronitrile
-
pH 7, 20C, competitive inhibitor
0.0025
-
KCN
-
+/- 0.001, NilCo
0.003
-
KCN
-
+/- 0.0015, NilFe
0.015
-
KCN
-
pH 7, 30C
2
-
N,N-Dimethylacetamide
-
ACV2 mutant; R312 strain
0.9
-
n-butyric acid
-
pH 7.2, 28C
0.13
-
NaCN
-
pH 7.5, 25C, non-competitive with acrylonitrile
0.003
-
NaNO2
-
+/- 0.0005, NilCo
0.6
-
Propionamide
-
pH 7, 37C, mixed-type inhibitor
0.004
-
tertiary-butyl isonitrile
-
+/- 0.001, NilCo
100
-
Thioacetamide
-
R312 strain
110
-
Thioacetamide
-
ACV2 mutant
8.4
-
Thiocyanate
-
pH 7, 37C, competitive inhibitor
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.005
-
2-Nitrophenol
-
+/- 0.001, NilFe
0.01
-
3-Nitrophenol
-
+/- 0.002, NilFe
0.0086
-
4-nitrophenol
-
pH 7.9, NilCo
0.01
-
4-nitrophenol
-
+/- 0.002, NilFe
0.003
-
7-Chloro-4-nitrobenzo-2-oxa-1,3-diazole
-
+/- 0.001, NilCo
0.004
-
7-Chloro-4-nitrobenzo-2-oxa-1,3-diazole
-
+/- 0.001, NilFe
0.005
-
acrylonitrile
-
+/- 0.003, NilCo
0.009
-
acrylonitrile
-
+/- 0.002, NilFe
0.3
-
Butyric acid
-
+/- 0.1, NilCo
0.4
-
Butyric acid
-
+/- 0.1, NilFe
2
-
Hexanoic acid
-
IC50 of 2 mM
0.003
-
KCN
-
+/- 0.001, NilCo
0.005
-
KCN
-
+/- 0.001, NilFe
12
-
n-butyric acid
-
competitive inhibitor. Complete inhibition beyond 40 mM. IC50 of 4 mM at pH 7.2 in Hepes buffer 100 mM, IC50 of 8 mM at pH 7.2 in sodium phosphate buffer 100 mM, IC50 of 0.8 mM at pH 6.2 in sodium phosphate buffer 100 mM, IC50 of 12 mM at pH 8.2 in sodium
0.008
-
NaNO2
-
+/- 0.001, NilCo
0.5
-
NaNO2
-
value above, NilFe
0.007
-
tertiary-butyl isonitrile
-
+/- 0.001, NilCo
0.1
-
tertiary-butyl isonitrile
-
value above, NilFe
0.5
-
Valeric acid
-
IC50 of 0.5 mM
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.018
-
-
0.5 mM NaNO2, NilFe
0.18
-
-
strain 02-10230, in absence of crotonamide, pH 7.5, temperature not specified in the publication
0.22
-
-
strain 03-03046, in absence of crotonamide, pH 7.5, temperature not specified in the publication
0.27
-
-
strain 02-10041, in absence of crotonamide, pH 7.5, temperature not specified in the publication
0.3
-
-
strain 03-03119, in absence of crotonamide, pH 7.5, temperature not specified in the publication
1.11
-
-
strain 02-10056, in presence of crotonamide, pH 7.5, temperature not specified in the publication
1.12
-
-
strain 02-10230, in presence of crotonamide, pH 7.5, temperature not specified in the publication
1.41
-
-
strain 02-10056, in absence of crotonamide, pH 7.5, temperature not specified in the publication
1.82
-
-
acrylamide (500 g/l)
2.4
-
-
purified recombinant wild-type apo-H-NHase, pH 7.5, 20C
2.6
-
-
+/- 0.2, acrylonitrile, 50 mM, coupled assay with amidase
2.8
-
-
+/- 0.2, acrylonitrile, 50 mM, HPLC-based assay
2.8
-
-
purified recombinant V5L mutant apo-H-NHase, pH 7.5, 20C
3.8
4.6
-
with 0.5% ammonium sulfate or acetonitrile in the incubation medium
4.16
-
-
cell-free extract, at pH 8.0, at 40C
4.9
-
-
with 0.5% acetonitrile and 0.5% yeast extract
5.21
-
-
with the addition of 0.1% w/v CoCl2
5.32
-
-
strain 02-10055, in presence of crotonamide, pH 7.5, temperature not specified in the publication
5.7
-
-
+/- 0.2, acetonitrile, 50 mM, HPLC-based assay
5.9
-
-
+/- 0.4, acetonitrile, 50 mM, coupled assay with amidase
6.8
-
-
recombinant enzyme, with 2-nitro-5-thiocyanato-benzoic acid
6.89
-
-
strain 02-10055, in absence of crotonamide, pH 7.5, temperature not specified in the publication
7.7
-
-
native enzyme, with 2-nitro-5-thiocyanato-benzoic acid
11.04
-
-
pH 7.4, 10C
11.8
-
-
+/- 6.5, in nmol/min per g fresh weight (foliage)
12.3
-
-
acrylonitrile (100 g/l)
13.7
-
-
purified native enzyme, pH 7.5, temperature not specified in the publication
15
-
-
+/- 5, substrate: 2-nitro-5-thiocyanato-benzoic acid, NilCo; +/- 5, substrate: 2-nitro-5-thiocyanato-benzoic acid, NilFe
20.6
-
-
acrylamide (100 g/l)
23.2
-
-
methacrylamide-induced enzyme activity, no activity in absence of methacrylamide
27.99
-
-
acrylonitrile (30 g/l)
46.83
-
-
after 11.3fold purification, at pH 8.0, at 40C
66.6
-
-
+/- 32.0, in nmol/min per g fresh weight (foliage)
94.3
-
Q8GJG6, Q8GJG7
W47E strain 1
95
-
-
native enzyme, with cyanovaleric acid
96.8
-
Q8GJG6, Q8GJG7
W47E strain 2
97
-
-
purified co-substituted enzyme
100
-
-
recombinant enzyme, with cyanovaleric acid
100
-
-
+/- 15, substrate: 5-cyanovaleric acid, NilFe
110
-
-
+/- 10, substrate: 5-cyanovaleric acid, NilCo
116
-
-
strain 02-10101, in presence of crotonamide, pH 7.5, temperature not specified in the publication
128.7
-
Q8GJG6, Q8GJG7
S122C strain 2
133.2
-
Q8GJG6, Q8GJG7
S122C strain 1
168
-
-
strain 02-10101, in absence of crotonamide, pH 7.5, temperature not specified in the publication
189.2
-
Q8GJG6, Q8GJG7
control strain 1
192
-
Mesorhizobium sp.
-
strain F28, substrate acrylonitrile
195.1
-
Q8GJG6, Q8GJG7
control strain 2
270
-
-
purified recombinant V5L mutant R-H-NHase, pH 7.5, 20C
275
-
-
purified recombinant wild-type R-H-NHase, pH 7.5, 20C
371
-
-
purified enzyme
485
-
-
purified enzyme
686
-
Mesorhizobium sp.
-
purified native enzyme from strain F28, substrate acrylonitrile
829.5
-
-
purified protein
844
-
-
crude cell extract towards methacrylonitrile, in 50 mM Tris-HCl (pH 7.5)
860
-
-
partially purified enzyme
924
-
-
control, no inducer
1024
-
-
inducer: NH4Cl (75 mM)
1136
-
-
inducer: acrylonitrile (50 mM)
1260
-
-
crystallized enzyme
1325
-
-
in the presence of 0.035 mM n-butyric acid
1358
-
-
inducer: NH4Cl (75 mM) and acrylonitrile (50 mM)
1590
-
-
purified enzyme
1600
-
-
purified enzyme
1840
-
-
crystallized enzyme
2000
-
-
purified enzyme
6290
-
-
after 7.5fold purification towards methacrylonitrile, in 50 mM Tris-HCl (pH 7.5)
additional information
-
-
activity increases by irradiation with light
additional information
-
-
effect of different organic and inorganic compounds on activity
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
141 U/mg of dry cells, Am 324 mutant strain
additional information
-
-
-
additional information
-
-
no conversion of KCN
additional information
-
-
0.18 +/- 0.009, micromol/min/ml, maximum activity after 21 h, strain YHJ-5; 0.3 +/- 0.01, micromol/min/ml, maximum activity after 21 h, strain YHJ-2; 1.12 +/- 0.03, micromol/min/ml, maximum activity after 21 h, strain YHJ-3; 4.96 +/- 0.18, micromol/min/ml, maximum activity after 6 h, strain YHJ-1; chaperone protein DnaK-DnaJ-GrpE (pKJE7) lead to 20% decrease of normal NHase activity in the strains YHJ-1 and YHJ-3; chaperone proteins lead to loss of NHase activity in the strain YHJ-2; GroES/GroEL chaperone leads to doubling of NHase activity in the strain YHJ-3; no detectable effect of chaperone proteins on NHase activity in the strain YHJ-4; no detectable effect of GroES/GroEL chaperone on NHase activity in the strain YHJ-1; no detectable NHase activity in the strains YHJ-4 and YHJ-6
additional information
-
Comamonas oleophilus
-
0.220 +/- 0.006 micromol/h/mg cells, conversion of 2,2-dimethylcyclopropanecarbonitrile into 2,2-dimethylcyclopropanecarboxylic acid by nitrile hydratase/amidase
additional information
-
-
0.078+/-0.003 micromol/h/mg cells, conversion of 2,2-dimethylcyclopropanecarbonitrile into 2,2-dimethylcyclopropanecarboxylic acid by nitrile hydratase/amidase
additional information
-
-
0.096 +/- 0.003 micromol/h/mg cells, conversion of 2,2-dimethylcyclopropane carbonitrile into 2,2-dimethylcyclopropanecarboxylic acid by nitrile hydratase/amidase; optimization of reaction conditions (pH, temperature, organic solvent) for conversion of 2,2-dimethylcyclopropanecarbonitrile into (S)-2,2-dimethylcyclopropanecarboxylic acid by nitrile hydratase/amidase enzyme system
additional information
-
-
0.109 +/- 0.002 micromol/h/mg cells, conversion of 2,2-dimethylcyclopropanecarbonitrile into 2,2-dimethylcyclopropanecarboxylic acid by nitrile hydratase/amidase; 0.438 +/- 0.01 micromol/h/mg cells, conversion of 2,2-dimethylcyclopropanecarbonitrile into 2,2-dimethylcyclopropanecarboxylic acid by nitrile hydratase/amidase
additional information
-
-
vmax: 28 +/- 5 nmol/min/mg, NilCo; vmax: 30 +/- 5 nmol/min/mg, NilFe
additional information
-
Q8GJG6, Q8GJG7
no activity in S122A and S122D mutant proteins
additional information
-
-
no or reduced activity in NhpR transcriptional regulator defective mutants
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.5
7.5
Q8GJG6, Q8GJG7
recombinant NHase with modified start codon only
5.5
8.5
Q8GJG6, Q8GJG7
wild type NHase
6
8
Corynebacterium nitrilophilus
-
-
6.7
-
-
assay at
6.9
7.2
-
NilFe, NilCo
7
7.5
-
-
7
7.5
Mesorhizobium sp.
-
-
7
-
-
hydration of p-hydroxybenzylcyanide, 3,4,5-trimethoxybenzonitrile, p-aminobenzonitrile and o-chlorobenzonitrile
7
-
-
bioconversion in cells in a bioreactor
7.4
-
-
assay at, in vivo in cells
7.5
-
-
substrate: 2,2-dimethylcyclopropanecarbonitrile
7.5
-
-
hydration of acrylonitrile, indole-3-acetonitrile, p-chlorobenzonitrile and 3-cyanopyridine
7.5
-
-
assay at
7.5
-
-
H-NHase activity assay at
8
-
-
assay at, in vivo
8
-
-
assay at
8
-
-
around pH 8.0
8
-
-
the optimum nitrile hydratase activity is observed in the Tris-HCl buffer at a pH of 8.0
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
12
-
pH profile of soluble and immobilized enzymes, overview
5
8
-
about 50% of activity maximum at pH 5, about 60% of activity maximum at pH 8
5
9
-
about 60% of activity maximum at pH 5, about 55% of activity maximum at pH 9
5.1
8.7
-
about 50% of maximum activity
5.5
10
-
activity drops sharply below pH 5.5 and above pH 10.0
5.5
11
Corynebacterium nitrilophilus
-
sharp drop of activity below pH 5.5, moderate decrease of activity at pH 8-11
6
10
-
hydration of acrylonitrile, pH
6
8.3
-
about 50% of activity maximum at pH 6, about 35% of activity maximum at pH 8.3
6.4
7.6
-
pH 4.0: no NHase activity
7
8.5
-
pH 7.0: about 80% of maximal activity, pH 8.5: about 75% of maximal activity
7.2
7.6
-
hydration of acrylonitrile at 25C, rapid decrease of activity below pH 6.4
additional information
-
-
different buffer systems including phthalate, phosphate and borax buffer are tested for influence on hydration of acrylonitrile
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0
-
-
assay at
5
-
-
bioconversion in cells in a bioreactor
20
-
-
assay at
20
-
-
with propionitrile and acrylonitrile as substrates
20
-
-
H-NHase activity assay at
21
-
-
assay at
22
-
-
assay at room temperature
25
-
-
hydration of acrylonitrile
25
-
-
assay at, in vivo
28
-
-
-
28
-
-
assay at, in vivo in cells
30
-
-
substrate: 2,2-dimethylcyclopropanecarbonitrile
37
45
Mesorhizobium sp.
-
-
additional information
-
-
Arrhenius plot: activation energy: 90.2 kJ/mol (substrate acrylonitrile), evaluation in the temperatur range from 5 to 30 C
additional information
-
Q8GJG6, Q8GJG7
reaction activation energy of the recombinant NHase with modified start codon is 24.4 +/- 0.5 kJ/mol, this is 37.2% of wild type NHase
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
24
-
-
10
30
-
79% of activity maximum at 10C, 13% of activity maximum at 30C
15
28
-
10C: 510.5 U/g DCW (dry cell weight), 28C: 1209.8 U/g DCW (dry cell weight), 30C: 1155.8 U/g DCW (dry cell weight), 40C: 677.0 U/g DCW (dry cell weight)
15
35
-
15C: about 60% of maximal activity, 35C: about 55% of maximal activity, temperature profile
20
45
Mesorhizobium sp.
-
at 30C and 20C the enzyme activity decreases by 13% and 26% of the maximal activity, respectively, the enzyme is inactive at 55-65C, high activity at 45C
25
50
-
about 50% of activity maximum at 25C, about 70% of activity maximum at 50C
30
35
-
optimum temperature for acetonitrile hydrolysis
30
60
-
about 60% of activity maximum at 30C, about 50% of activity maximum at 60C
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.2
-
-
polyacrylamide isoelectrofocusing
5.75
-
-
polyacrylamide isoelectrofocusing
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
additional information
Mesorhizobium sp.
-
optimum growth temperature of strain F28 is 37C
Manually annotated by BRENDA team
additional information
-
analysis of optimal growth conditions: glycerol, mannitol, sorbitol, lactose, sucrose, citrate, acetate, succinate increase enzyme production, as well as KH2PO4, K2HPO4 MgSO4, FeCl3, and CoCl2 addition to the medium at pH 7.0-9.0, 25C, kinetics, overview
Manually annotated by BRENDA team
additional information
Mesorhizobium sp. BNC1
-
optimum growth temperature of strain F28 is 37C
-
Manually annotated by BRENDA team
additional information
Rhodococcus erythropolis MTCC 1526
-
analysis of optimal growth conditions: glycerol, mannitol, sorbitol, lactose, sucrose, citrate, acetate, succinate increase enzyme production, as well as KH2PO4, K2HPO4 MgSO4, FeCl3, and CoCl2 addition to the medium at pH 7.0-9.0, 25C, kinetics, overview
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Rhodococcus sp. 7
-
-
-
Manually annotated by BRENDA team
Corynebacterium nitrilophilus
-
-
Manually annotated by BRENDA team
Arthrobacter sp. J-1
-
-
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
52000
-
-
gel filtration
52000
-
-
-
54000
-
-
chromatography on Sephacryl S-400 and Sepharose CL-6B, alpha-beta form
61400
-
-
gel filtration
70000
-
-
N774 strain
70000
-
-
gel filtration
77000
-
-
gel filtration on Sephadex-G150
80000
-
-
gradient gel electrophoresis
80000
-
-
gel filtration
84000
-
-
gel filtration
85000
-
-
sedimentation equilibrium method
86000
-
-
holoenzyme, native PAGE
87000
-
-
gel filtration, HPLC
90000
94000
-
-
90000
94000
-
gel filtration on Cellulofine GCL-2000sf
90000
94000
-
gel filtration
90000
-
-
gel filtration
92300
-
-
gel filtration
94000
-
-
gel chromatography on Superdex 200 , (alpha-beta)2 form
100000
-
-
gel filtration
100000
-
-
gel filtration
101000
-
-
sedimentation equilibrium, low molecular mass enzyme, L-NHase
102000
-
-
gel filtration
110000
-
-
-
110000
-
E13931, E13932
dynamic light-scattering; dynamic light-scattering
130000
-
-
gel filtration, low molecular mass enzyme, L-NHase
278000
-
-
gel filtration
278000
-
-
strain 7
364000
-
-
proposal for holoenzyme subunit composition: alpha2 beta4, based on calibrated gel filtration and absorption spectra
420000
-
-
gel filtration
420000
-
-
-
505000
530000
-
sedimentation equilibrium method, gel permeation HPLC
505000
530000
-
-
505000
530000
-
sedimentation equilibrium method, gel permeation HPLC
520000
-
-
high molecular mass enzyme, H-NHase
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 25000 + x * 28000, SDS-PAGE
?
-
x * 26000, alpha, + x * 27500, beta, SDS-PAGE
?
-
x * 26000, alpha + x * 32000, beta, SDS-PAGE, strain 7
?
-
x * 26000 + x * 27500, SDS-PAGE
?
-
x * 24000 + x * 27000, SDS-disc gel electrophoresis
?
-
x * 27000, alpha, + x * 27500, beta, SDS-PAGE
?
-
x * 29000, alpha, + x * 26000, beta, SDS-PAGE
?
-
x * 26000, alpha + x * 32000, beta, SDS-PAGE, strain 7; x * 28500, alpha + x * 29000, beta, SDS-PAGE, N774 strain
?
-
x * 26000, alpha, + x * 29000, beta, SDS-PAGE
?
-
x * 28500, alpha + x * 29000, beta, SDS-PAGE, N774 strain
?
-
x * 23000, alpha + x * 23000, beta
?
Q5XPL4
x * 23000, alpha-subunit, + x * 24000, beta-subunit, calculated
?
Arthrobacter sp. J-1
-
x * 24000 + x * 27000, SDS-disc gel electrophoresis
-
?
Brevibacterium sp. R312
-
x * 26000, alpha, + x * 27500, beta, SDS-PAGE; x * 26000 + x * 27500, SDS-PAGE; x * 27000, alpha, + x * 27500, beta, SDS-PAGE
-
?
Comamonas testosteroni 5-MGAM-4D
-
x * 23000, alpha-subunit, + x * 24000, beta-subunit, calculated
-
?
Corynebacterium pseudodiphtheriticum ZBB-41
-
x * 25000 + x * 28000, SDS-PAGE
-
?
Rhodococcus rhodochrous J1
-
x * 26000, alpha, + x * 29000, beta, SDS-PAGE; x * 29000, alpha, + x * 26000, beta, SDS-PAGE; x * 29000, alpha, + x * 26000, beta, SDS-PAGE
-
?
Rhodococcus sp. 7
-
x * 26000, alpha + x * 32000, beta, SDS-PAGE, strain 7; x * 26000, alpha + x * 32000, beta, SDS-PAGE, strain 7; x * 28500, alpha + x * 29000, beta, SDS-PAGE, N774 strain
-
?
Rhodococcus sp. N-774
-
x * 26000, alpha + x * 32000, beta, SDS-PAGE, strain 7; x * 28500, alpha + x * 29000, beta, SDS-PAGE, N774 strain; x * 28500, alpha + x * 29000, beta, SDS-PAGE, N774 strain
-
dimer
-
1 * 23000 + 1 * 26000, SDS-PAGE
dimer
-
2 * 26900, SDS-PAGE
dimer
-
2 * 27700
dimer
-
1 * 22982, alpha + 1* 24108, beta, amino acid sequence; gel filtration
dimer
-
1 * 22982, alpha + 1* 24108, beta, amino acid sequence
dimer
Corynebacterium sp. C5
-
2 * 26900, SDS-PAGE
-
dimer
Pseudomonas putida 5B
-
1 * 22982, alpha + 1* 24108, beta, amino acid sequence
-
dimer
Pseudomonas putida NRRL-18668
-
1 * 22982, alpha + 1* 24108, beta, amino acid sequence; gel filtration
-
dimer
Rhodococcus sp. N-774, Rhodococcus sp. R312
-
-
-
heterodimer
-
alphabeta
heterodimer
-
alphabeta, 1 * 22975 + 1 * 23493, MALDI-TOF MS
heterodimer
-
1 * 24000 + 1 * 23000, SDS-PAGE
heterodimer
-
1 * 25040 + 1 * 30600, estimated from SDS-PAGE
heterodimer
-
1 * 23000, about, alpha-subunit + 1 x 23000, about, beta-subunit, Co-type NHases are bacterial heterodimers, consisting of nonhomologous alpha- and beta-subunits
heterodimer
Pseudomonas putida NRRL-18668
-
1 * 23000, about, alpha-subunit + 1 x 23000, about, beta-subunit, Co-type NHases are bacterial heterodimers, consisting of nonhomologous alpha- and beta-subunits
-
heterodimer
Rhodococcus equi TG328-2
-
1 * 24000 + 1 * 23000, SDS-PAGE
-
heterodimer
Rhodococcus erythropolis AJ270
-
alphabeta
-
heterodimer
Rhodococcus rhodochrous PA-34
-
1 * 25040 + 1 * 30600, estimated from SDS-PAGE
-
heterodimer
-
alphabeta, 1 * 22975 + 1 * 23493, MALDI-TOF MS
-
heterotrimer
-
alpha,beta2, 1 * 55746 + 2 * 63001, 32% amino acid sequence identity of subunits, MALDI-TOF MS and HPLC
heterotrimer
Rhodococcus sp. RHA1
-
alpha,beta2, 1 * 55746 + 2 * 63001, 32% amino acid sequence identity of subunits, MALDI-TOF MS and HPLC
-
homotetramer
-
4 * 27000, SDS-PAGE
homotetramer
Agrobacterium tumefaciens IAM B-261
-
4 * 27000, SDS-PAGE
-
tetramer
-
4 * 25000, SDS-PAGE
tetramer
-
2 * 22800, alpha + 2 * 22700, beta, SDS-PAGE
tetramer
-
4 * 95000
tetramer
-
2 * 26000, alpha and 2 * 29000, beta, SDS-PAGE
tetramer
-
2 * 22982, alpha + 2 * 24108, beta, amino acid sequence, gel filtration
tetramer
-
a2b2 heterotetramer
tetramer
E13931, E13932
2 * 25400, alpha-subunit, + 2 * 26700, beta-subunit, calculated; 2 * 25400, alpha-subunit, + 2 * 26700, beta-subunit, calculated
tetramer
-
alpha2beta2, 2 * 22800 + 2 * 22700
tetramer
-
2 * 27000, alpha-subunit, + 2 * 29000, beta-subunit, alpha2beta2 structure, SDS-PAGE, 2 * 22953, alpha-subunit, + 2 * 23486, beta-subunit, alpha2beta2 structure, sequence calculation
tetramer
Bacillus smithii SC-J05-1
-
2 * 25400, alpha-subunit, + 2 * 26700, beta-subunit, calculated; 2 * 25400, alpha-subunit, + 2 * 26700, beta-subunit, calculated
-
tetramer
Brevibacterium sp. R312
-
4 * 95000
-
tetramer
Pseudomonas chlororaphis B23
-
4 * 25000, SDS-PAGE; 4 * 25000, SDS-PAGE
-
tetramer
Pseudomonas putida NRRL-18668
-
2 * 22982, alpha + 2 * 24108, beta, amino acid sequence, gel filtration
-
tetramer
Rhodococcus erythropolis N4
-
2 * 27000, alpha-subunit, + 2 * 29000, beta-subunit, alpha2beta2 structure, SDS-PAGE, 2 * 22953, alpha-subunit, + 2 * 23486, beta-subunit, alpha2beta2 structure, sequence calculation
-
tetramer
Rhodococcus rhodochrous J1
-
; 2 * 26000, alpha and 2 * 29000, beta, SDS-PAGE
-
trimer
-
strain R312
trimer
Brevibacterium sp. R312
-
strain R312; strain R312
-
monomer
A9V2C1, -
the two usually separated NHase subunits fused in one protein of the choanoflagellate Monosiga brevicollis
additional information
-
formation of an heterodimer is indispensable for stabilizing the structure of the two subunits, alpha and beta
additional information
-
enzyme is comprised of a alpha-subunit with cobalt-binding site and a beta subunit, deduced from sequence
additional information
-
sequence similarity and size of subunits is unusual for NHases
additional information
-
structure analysis and salt-bridge interactions involving main chain atoms in region A1 of 1V29, overview
additional information
Q7SID2
structure analysis, overview
additional information
-
NhhG forms a complex with the alpha-subunit of H-NHase. NhhAG is very similar to the mediator of L-NHase, NhlAE, which is a heterotrimer complex consisting of the cobaltcontaining alpha-subunit of L-NHase and NhlE. Formation of large-sized complexes during self-subunit swapping in H-NHase. Self-subunit swapping mechanisms, detailed overview
additional information
Bacillus sp. SC-105-1
-
structure analysis and salt-bridge interactions involving main chain atoms in region A1 of 1V29, overview
-
additional information
Pseudonocardia thermophila JCM3095
-
structure analysis, overview
-
additional information
Rhodococcus pyridinivorans S85-2
-
enzyme is comprised of a alpha-subunit with cobalt-binding site and a beta subunit, deduced from sequence
-
additional information
Rhodococcus rhodochrous J1
-
NhhG forms a complex with the alpha-subunit of H-NHase. NhhAG is very similar to the mediator of L-NHase, NhlAE, which is a heterotrimer complex consisting of the cobaltcontaining alpha-subunit of L-NHase and NhlE. Formation of large-sized complexes during self-subunit swapping in H-NHase. Self-subunit swapping mechanisms, detailed overview
-
additional information
Rhodococcus sp. RHA1
-
sequence similarity and size of subunits is unusual for NHases
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
side-chain modification
-
alphaCys112 and alphaCys114 are modified to cysteine sulfinic acids and isobutyronitrile is included in active site, evidence from crystallographic data
side-chain modification
Rhodococcus erythropolis AJ270
-
alphaCys112 and alphaCys114 are modified to cysteine sulfinic acids and isobutyronitrile is included in active site, evidence from crystallographic data
-
additional information
-
two cysteine ligands, alphaCys112 and alphaCys114, are oxidized to a cysteine sulfinic acid and a cysteine sulfenic acid, respectively. Cysteine sulfinic acid in 112 is responsible for the catalytic activity. First metalloprotein having posttranslationally modified cysteine ligands
additional information
-
alphaCys112 is modified to a cysteine-sulfinic acid in both recombinant and native enzymes
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
;
E13931, E13932
in presence of MgCl2
-
purified recombinant wild-type and mutant enzymes, hanging drop vapour diffusion method, 25C, from 20 mg/mL ppNHase and a reservoir containing 22% polyacrylic acid sodium salt 5100, 100 mM HEPES, pH 7.5, 20 mM magnesium chloride, and 4% acetone, single crystals are transferred to 17.6% polyacrylic acid sodium salt 5100 and 20% glycerol in 100 mM HEPES, pH 7.5, as cryoprotectant, X-ray diffraction structure determination and analysis
-
dockings and interactions of a series of aliphatic and aromatic nitriles are modelled and the differences are reported
-
dockings of the substates and products to the crystal structure 1IRE, overview
-
in complex with n-butyric acid
-
PaNit without ligands, and with an acetate ion bound in the active site, or with a bromide ion in the active site, by hanging drop vapour diffusion method from 35% PEG 550MME, 0.2 M MgCl2 or Mg(CH3COOH)2 and 0.2 M Tris-HCl, pH 7.5, X-ray diffraction structure determination and analysis at 1.57-1.83 A resolution
-
hanging drop method, X-ray diffraction, resolution: 1.3 A, ferric ion coordinating residues
-
wild type and mutant enzymes S113A and Y72F, hanging drop vapor diffusion method, using 20% (w/v) PEG8000, 0.10 M Tris-HCl, pH 7.5, 0.3 M MgCl2
-
analysis of the crystal structure of inactive NHase, overview
-
hanging-drop vapor diffusion method, N-771 strain
-
x-ray diffraction, special focus on iron center vicinity and hydrogen bond network, similar structures of wild type and alphaQ90N mutant enzyme in nitrosylated state, resolution: 1.43 A
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
12
-
nitrile hydratase cross-linked enzyme aggregates are stable at pH values 2-4 units below the optimum (pH 8.0) and still have a useful activity under these conditions, retains about 20% activity at pH 4, 40% activity at pH 5.0, 65% activity at pH 6.0, 90% activity at pH 7.0, 9.0 and 10.0, 85% activity at pH 12.0
4
9
Mesorhizobium sp.
-
the enzyme retains over 50% activity at pH 5.0 and pH 8.8, but loses activity below pH 4.0 or above pH 9.0
4.3
10.4
-
at pH value of 4.3 and 10.4 enzyme activities are reduced to 24 and 25% of the maximum activity, respectively
5
10
-
the pH below 5 and above 10 drastically decreases the activity of purified NHase
6
9
-
20C, 60 min, stable in this range, rapid loss of activity below pH 6.0 and above pH 9.0; 25C, 10 min, stable in this range, rapid loss of activity below pH 6.0 and above pH 9.0
6.5
8
-
25C, 90 min, stable
7
11
-
10C, 30 min, purified enzyme, stable
7
8
-
highly unstable below pH 7.0
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
70
-
highest stability at 4C in thermal inactivation studies between 4C and 50C, the enzyme is inactivated immediately at 70C
5
37
Q8GJG6, Q8GJG7
mutant protein W47E shows higher thermo-stability than recombinant NHase with modified start codon only
5
40
-
30 min, the purified enzyme is stable up to 25C, inactivation at 40C
5
-
-
half-life 38.5 h
10
30
-
at 10C, strain ZA0707 exhibits a better operational stability than at 20C and 30C
10
-
-
stable below
10
-
-
pH 7.5, 10 min, stable
10
-
-
10 min, 22 mM n-butyric acid, stable
10
-
-
half-life 16.5 h
20
28
-
when the hydration temperature is controlled at a relatively higher level such as 28C, the total deactivation rate constant is about 2.8fold of that at 20C
20
50
-
20 min, the stability of aggregated and immobilized enzyme is increased compared to enzyme in cell extract or whole cells
20
-
-
90 min, 60% loss of activity
20
-
-
10 min, 22 mM n-butyric acid, stable
20
-
-
half-life 6.3 h
25
50
-
half-lives: 40C: 2.3 h, 50C: 0.98 h, 25C: 6.31 h, 35C: 5.45 h
25
-
-
5 min, unstable above
25
-
-
10 min, 22 mM n-butyric acid, 12.5% loss of activity
25
-
-
no loss of activity
25
-
-
half-life 3 h
30
-
-
10 min, 22 mM n-butyric acid, 25% loss of activity
30
-
-
4% loss of activity
35
-
-
10 min, 20% loss of activity; 1 hour, 10 mM methacrylonitrile stable up to this temperature
35
-
-
10 min, 22 mM n-butyric acid, 46.6% loss of activity; 1 hour, 10 mM methacrylonitrile stable up to this temperature
35
-
-
12% loss of activity; 1 hour, 10 mM methacrylonitrile stable up to this temperature
35
-
-
1 hour, 10 mM methacrylonitrile stable up to this temperature
40
50
-
half-life is 2 h at 40C and 0.5 h at 50C, below and above 40C NHase activity decreases drastically
40
-
-
pH 7.5, 10 min, stable
40
-
-
10 min, 22 mM n-butyric acid, 94.3% loss of activity
40
-
-
58% loss of activity
40
-
-
stable up to
45
-
-
5 min, complete loss of activity
45
-
-
pH 7.5, 10 min, 60% loss of activity
45
-
-
93.9% loss of activity
45
-
Mesorhizobium sp.
-
purified enzyme, stable up to
50
60
-
the activity is not retained for more than 20 min at temperatures above 50C for the soluble enzyme, at 60C the half-life of the immobilized NHase (Eupergit C with 1-ethyl-3-(dimethylamino-propyl) carbodiimide) is 330 min as compared with 54.5 min for the soluble enzyme. Eupergit C-immobilized NHase shows 80% residual activity after 90 min at 60C
50
65
-
the enzyme activity gradually reduces with the further increase of temperature from 50 to 65C, the thermostability of NHase is comparatively good under 50C, while the enzyme activity is obviously lost when the cells are preincubated over 50C
50
-
-
90 min, complete loss of activity
50
-
-
60 min, about 80% loss of activity
50
-
-
stable up to, 30 min, pH 7.0, 44 mM n-butyric acid
50
-
-
below, stable, H-NHase
50
-
-
97.7% loss of activity
55
-
-
10 min, nearly complete inactivation
55
-
-
20 min, about 90% loss of activity
55
-
-
complete loss of activity
60
-
-
stable in absence of either substrates or analogs
60
-
-
stable up to
additional information
-
-
the enzyme is heat-stable
additional information
-
-
determination of thermal stability of thermophilic nitrile hydratases by molecular dynamics simulation using crystal structures with PDB ID 1V29. In 1V29, region A1 is stabilized by a wellorganized hook-hook like cluster with multiple salt-bridge interactions, region A2 is stabilized by two strong salt-bridge interactions of Glu52-Arg332 and Glu334-Arg332
additional information
-
Q7SID2
determination of thermal stability of thermophilic nitrile hydratases by molecular dynamics simulation using crystal structures with PDB ID 1UGQ. In 1UGQ, the absence of a charged residue decreases the thermal sensitivity of region B1, and the formation of a small beta-sheet containing a stable salt-bridge in C-beta-terminal significantly enhances the thermal stability
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
potassium phosphate buffer has a negative effect on stability
-
loss of activity caused by storage at 0C can be restored by irradiation with light of 370 nm
-
the enzyme becomes more unstable as it becomes purer. Isovalerate, 30 mM, and caprylate stabilize effectively
-
nitrile hydratase cross-linked enzyme aggregates are sensitive to water-immiscible organic solvents as well as to aldehydes and hydrogen cyanide, but are remarkably stable and show useful activity in acidic aqueous environments of pH 4-5
-
KH2PO4-NaOH and Tris-HCl buffer are tested at 28C and pH 7.5. 20% NHase activity is lost after 18 h and is further decreasing. 73.5 h later, NHase activity in Tris-HCl is unchanged while in KH2PO4-NaOH abrupt decrease is observed.
-
completely stabilized by 22 mM n-butyric acid
-
unstable when diluted, but completely stabilized with low-molecular organic acids such as n-butyric acid, n-valeric acid, propionic acid and acetic acid
-
the partially purified enzyme is stable in the presence of organic acids at higher temperatures
-
active in acrylamide up to 60% w/v
-
organic acids stabilize, stable for more than 1 month in 0.1 M HEPES/KOH, pH 7.2, with 44 mM n-butyric acid, n-valeric acid, isovaleric acid, isobutyric acid or n-caproic acid
-
immobilization and stabilization of a nitrile hydratase in the form of a cross-linked enzyme aggregate using ammonium sulfate as an aggregation agent followed by cross-linking with glutaraldehyde, method development and evaluation, overview. The stability of aggregated and immobilized enzyme is increased compared to enzyme in cell extract or whole cells
-
purified mutant NHases are stored in the dark without n-butyric acid, before use, NHases are activated by light irradiation.
-
ORGANIC SOLVENT
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
1,4-dioxane
-
the soluble enzyme shows about 80% relative activity in the presence of 1,4-dioxane
Acetone
-
the soluble enzyme shows about 35% relative activity in the presence of acetone
Acetone
Aeribacillus pallidus RAPc8
-
the soluble enzyme shows about 35% relative activity in the presence of acetone
-
chloroform
-
the soluble enzyme shows about 70% relative activity in the presence of chloroform
chloroform
Aeribacillus pallidus RAPc8
-
the soluble enzyme shows about 70% relative activity in the presence of chloroform
-
dichloromethane
-
the soluble enzyme shows about 80% relative activity in the presence of dichloromethane
dimethylformamide
-
30% v/v, no residual activity
dimethylformamide
Rhodococcus rhodochrous IFO 15564
-
30% v/v, no residual activity
-
Ethanol
-
the soluble enzyme shows about 60% relative activity in the presence of ethanol
Ethanol
Aeribacillus pallidus RAPc8
-
the soluble enzyme shows about 60% relative activity in the presence of ethanol
-
formaldehyde dichloromethane
-
the soluble enzyme shows about 20% relative activity in the presence of formaldehyde
Methanol
-
the soluble enzyme shows about 70% relative activity in the presence of methanol
tetrahydrofuran
-
the soluble enzyme shows about 40% relative activity in the presence of tetrahydrofuran
Methanol
Aeribacillus pallidus RAPc8
-
the soluble enzyme shows about 70% relative activity in the presence of methanol
-
additional information
-
the soluble enzyme is not influenced by n-hexane, cyclohexane, toluene, benzene, ethyl acetate, and propanol
additional information
Aeribacillus pallidus RAPc8
-
the soluble enzyme is not influenced by n-hexane, cyclohexane, toluene, benzene, ethyl acetate, and propanol
-
OXIDATION STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
The enzyme is strongly inhibited by oxidizing agents like H2O2, ammonium persulfate and N-bromosuccinimide.
-
672727
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, pH 7.0, 50% glycerol, stable for at least 40 days, 40% loss of activity after 6 months
-
0C, pH 7.0, 50% loss of activity after 40 days
-
-80C, stable for weeks
-
4C, stable for weeks
-
-40C, pH 7.2, 40 mM butyric acid, stable
-
4C, Tris-HCl buffer pH 7.2
-
-20C, 50% glycerol, 0.01 M HEPES/KOH buffer, pH 7.2, 22 mM n-butyric acid, stable for more than 2 months
-
-20C, 2 weeks, 90% residual activity, with addition of 8% glycerol, complete loss of activity within one week
-
organic acids stabilize, stable for more than 1 month in 0.1 M HEPES/KOH, pH 7.2, with 44 mM n-butyric acid, n-valeric acid, isovaleric acid, isobutyric acid or n-caproic acid
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ammonium sulfate precipitation and Q-Sepharose column chromatography
-
native enzyme to homogeneity
-
to homogeneity, using several chromatographic steps, including DEAE, hydroxyapatite, and Sephadex G-200 column chromatography
-
ammonium sulfate fractionation and chromatography on Q-Sepharose, phenyl-Sepharose and Sephadex G150; ammonium sulfate fractionation, chromatography on DEAE-Sephacel and phenyl-Sepharose CL-4B and gel filtration, R312 strain, 10.2fold purified
-
ammonium sulfate fractionation, chromatography on DEAE-Sephacel and phenyl-Sepharose CL-4B and gel filtration, R312 strain, 10.2fold purified
-
ammonium sulfate precipitation, ion exchange chromatography and chromatography on phenyl-Sepharose CL-4B, 11fold purification, mutant strain ACV2
-
cell-free extract preparation
-
chromatography on Q-Sepharose, phenyl-Sepharose and Uno Q
-
CoCl2, an overexpressed chaperonin system and butyric acid is necessary for fully soluble and active NilCo protein, 95% purity on 12% SDS-PAGE
-
-
Corynebacterium nitrilophilus
-
to homogeneity, using several chromatographic steps, including DEAE, hydroxyapatite, and Sephadex G-200 column chromatography
-
chromatography on DEAE-Cellulose, DEAE-Sephacel and phenyl-Sepharose CL-4B, 130fold purification
-
native enzyme from strain F28 5fold by ammonium sulfate fractionation, anion exchange chromatography and gel filtration
Mesorhizobium sp.
-
(NH4)2SO4 fractionation
-
ammonium sulfate fractionation, chromatography on DEAE-Sephacel, octyl and phenyl-Sepharose CL-4B
-
chromatography on DEAE-Cellulose, hydroxyapatite, phenyl-Sepharose and Sephacryl S-400
-
recombinant soluble wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by anion exchange chromatography, ammonium sulfate fractionation, and hydrophobic interaction chromatography, followed by ultrafiltration and another step of anion exchange chromatography
-
recombinant Nit from Escherichia coli strain Bl21(DE3) by ammonium sulfate fractionation and anion exchange chromatography
-
Sepharose 6 column chromatography
-
native enzyme 78fold by ammonium sulfate fractionation, anion exchange chromatography, and hydrophobic interaction chromatography
-
sonication, (NH4)2SO4 fractionation, DEAE-Sephacel/phenyl Sepharose/Sephacryl S200 column chromatography
-
Resource Q column chromatography and Superdex-200 gel filtration
-
; ammonium sulfate fractionation, chromatography on DEAE-Sephacel, octyl-Sepharose CL-4B and phenyl-Sepharose CL-4B, 4.91fold purification
-
; ammonium sulfate fractionation, chromatography on DEAE-Sephacel, phenyl-Sepharose and Sephacryl S-300, 3.31fold purification
-
ammonium sulfate fractionation, chromatography on DEAE-Sephacel, phenyl-Sepharose CL-4B and gel filtration
-
ammonium sulfate fractionation, Sephacryl S 300 gel filtration, and DEAE column chromatography
-
recombinant L-NHase, NhlAE, and the NhhA-NhlE hybrid mediator complex from Rhodococcus rhodochrous strain ATCC12674 and Rhodococcus fascians DSM43985 by ammonium sulfate fractionation anion exchange chromatography, dialysis, gel filtration, and another step of anion exchange chromatography
-
(NH4)2SO4 fractionation, ion-exchange/hydrophobic/gel-filtration chromatography, stabilization by n-butyric acid, yield of purified protein: 23.96%
-
3 successive column chromatographies in the presence of 40 mM n-butyric acid (only wild type), alphaQ90N mutein is purified in nitrosylated state in the dark
-
ammonium sulfate fractionation, chromatography on DEAE-Cellulofine, phenyl-Sepharose, Sephadex G-150 and octyl-Sepharose, 11.5fold purification, N-774
-
anion exchange and hydrophobic interaction chromatography, yield of purified protein: 1.9% (specific activity 5.9 U/mg), cytosolic proteom of cells grown on 0.1 M acetonitrile and acetic acid/ammonia are compared via quantitative 2D gel electrophoresis, spot identification by MS, no significant amino acid sequence similarity with other NHases
-
anion exchange chromatography and gel filtration, recombinant enzyme
-
chromatography on butyl-toyopearl
-
chromatography on phenyl-Sepharose CL-4B and Bio-Gel HTP
-
chromatography on Sepharose Q, phenyl-Sepharose CL-4B and Sephadex G-200, strain 7
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
-
expression in Escherichia coli
-
nitrile hydratase from Comamonas testosteroni is expressed in Escherichia coli, strain TG1, overexpressed chaperonin system
-
genomic organization and phylogenetic analysis, sequence comparison, overview
A9V2C1, -
Nocardia sp.(strain YS-2002) NHase gene with modified start codon in alpha subunit is overexpressed in Escherichia coli, strain BL21(DE3)
Q8GJG6, Q8GJG7
expression in Escherichia coli
-
genes nhpA and nhpB encoding the alpha and beta subunits of NHase, transcriptional regulation of the nitrile hydratase gene cluster, the NHase gene cluster comprises seven genes: oxdA, amiA, nhpA, nhpB, nhpC, nhpS, and acsA, nhpR codes for a positive transcriptional regulator in the NHase gene cluster, overview
-
expression in Escherichia coli, strain BL21(DE3)
-
expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
-
gene nit-30, DNA and amino acid sequence determination and analysis, overexpression in Escherichia coli strain Bl21(DE3)
-
expressed in Escherichia coli BL21(DE3) cells
-
co-expression of recombinant strains YHJ-1 to YHJ-4 with plasmids encoding the chaperons pG-KJE8, pGro7, pKJE7, pG-Tf2 and pTf16; expression in Escherichia coli, NovaBlue, series of recombinant plasmids with genes encoding NHase (nha1: alpha subunit and nha2: beta subunit) and P44k protein (nha3), different positions and combinations; YHJ-1, Escherichia coli strain BL21(DE3) with plasmid pYHJ1 (alphabeta+P44k); YHJ-2, Escherichia coli strain BL21(DE3) with plasmid pYHJ2 (alpha+betaP44k); YHJ-3, Escherichia coli strain BL21(DE3) with plasmid pYHJ3 (alphabeta); YHJ-4, Escherichia coli strain BL21(DE3) with plasmid pYHJ4 (alpha+beta); YHJ-5, Escherichia coli strain BL21(DE3) co-expressing plasmids pYHJ3/pYHJ5 (P44k); YHJ-6, Escherichia coli strain BL21(DE3) co-expressing plasmids pYHJ4/pYHJ5
-
mutant enzymes are expressed in Escherichia coli HMS174(DE3)pLysS cells
-
high molecular mass-NHase and low molecular mass-NHase genes cloned into Escherichia coli
-
separate expression of L-NHase, NhlAE, an the NhhA-NhlE hybrid mediator complex in Rhodococcus rhodochrous strain ATCC12674 and Rhodococcus fascians DSM43985. Necessity of gene nhhG for functional H-NHase expression
-
expressed in Escherichia coli BL21(DE3) cells
-
Co-substituted NHase produced in Escherichia coli grown in Co supplemented medium; expression in Escherichia coli
-
expression in Escherichia coli
-
expressed in Escherichia coli BL21(DE3) cells
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
no activity in presence of crotonamide in strain 03-03119
-
no activity in strain 02-10041 in absence of crotonamide
-
no activity in presence of crotonamide in strain 03-03119
Rhizobium leguminosarum 02-03119
-
-
no activity in strain 02-10041 in absence of crotonamide
Rhizobium leguminosarum 02-03119
-
-
no activity in presence of crotonamide in strain 03-03119
Rhizobium leguminosarum 02-10041
-
-
no activity in strain 02-10041 in absence of crotonamide
Rhizobium leguminosarum 02-10041
-
-
no activity in presence of crotonamide in strain 03-03119
Rhizobium leguminosarum 02-10230
-
-
no activity in strain 02-10041 in absence of crotonamide
Rhizobium leguminosarum 02-10230
-
-
analysis of optimal growth conditions: glycerol, mannitol, sorbitol, lactose, sucrose, citrate, acetate, succinate induce the enzyme production, as well as KH2PO4, K2HPO4 MgSO4, FeCl3, and CoCl2 addition to the medium at pH 7.0-9.0, 25C, kinetics, overview
-
analysis of optimal growth conditions: glycerol, mannitol, sorbitol, lactose, sucrose, citrate, acetate, succinate induce the enzyme production, as well as KH2PO4, K2HPO4 MgSO4, FeCl3, and CoCl2 addition to the medium at pH 7.0-9.0, 25C, kinetics, overview
Rhodococcus erythropolis MTCC 1526
-
-
no activity in strain 03-03046 in presence of crotonamide
-
no activity in strain 03-03046 in presence of crotonamide
Sinorhizobium meliloti 03-03046
-
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
S122A
Q8GJG6, Q8GJG7
alpha subunit, site-directed mutagenesis of the recombinant NHase with modified start codon
S122C
Q8GJG6, Q8GJG7
alpha subunit, site-directed mutagenesis of the recombinant NHase with modified start codon
S122D
Q8GJG6, Q8GJG7
alpha subunit, site-directed mutagenesis of the recombinant NHase with modified start codon
W47E
Q8GJG6, Q8GJG7
beta subunit, site-directed mutagenesis of the recombinant NHase with modified start codon
S122A
-
alpha subunit, site-directed mutagenesis of the recombinant NHase with modified start codon
-
S122C
-
alpha subunit, site-directed mutagenesis of the recombinant NHase with modified start codon
-
S122D
-
alpha subunit, site-directed mutagenesis of the recombinant NHase with modified start codon
-
W47E
-
beta subunit, site-directed mutagenesis of the recombinant NHase with modified start codon
-
alphaD164N
-
site-directed mutagenesis
alphaE168Q
-
site-directed mutagenesis
alphaR170Q
-
site-directed mutagenesis
betaE56Q
-
site-directed mutagenesis
betaH71F
-
site-directed mutagenesis
betaH71L
-
site-directed mutagenesis
betaH71N
-
site-directed mutagenesis
betaY215F
-
site-directed mutagenesis
alphaD164N
Pseudomonas putida NRRL-18668
-
site-directed mutagenesis
-
alphaE168Q
Pseudomonas putida NRRL-18668
-
site-directed mutagenesis
-
alphaR170Q
Pseudomonas putida NRRL-18668
-
site-directed mutagenesis
-
betaE56Q
Pseudomonas putida NRRL-18668
-
site-directed mutagenesis
-
T109S
-
similar characteristics to the wild-type enzyme
Y114T
-
very low cobalt content and catalytic activity compared to the wild-type enzyme
T109S
Pseudonocardia thermophila JCM 3095
-
similar characteristics to the wild-type enzyme
-
S113A
-
the mutation partially affects catalytic activity and does not change the pH profiles of the kinetic parameters, the electronic state of the Fe center is altered
Y72F
-
the mutant exhibits no activity
S113A
Rhodococcus erythropolis N771
-
the mutation partially affects catalytic activity and does not change the pH profiles of the kinetic parameters, the electronic state of the Fe center is altered
-
Y72F
Rhodococcus erythropolis N771
-
the mutant exhibits no activity
-
alphaV5L
-
site-directed mutagenesis, exchange in the H-NHase does not influence the catalytic activity or the Co2+ content
Q90E
-
alpha subunit
Q90N
-
alpha subunit
R56K
-
beta subunit
Q90E
Rhodococcus sp. N771
-
alpha subunit
-
Q90N
Rhodococcus sp. N771
-
alpha subunit
-
R56K
Rhodococcus sp. N771
-
beta subunit
-
additional information
-
improvement of thermal stability of the industrialized mesophilic NHase by introducing stable salt-bridge interactions into its thermal sensitive regions
additional information
Bacillus sp. SC-105-1
-
improvement of thermal stability of the industrialized mesophilic NHase by introducing stable salt-bridge interactions into its thermal sensitive regions
-
additional information
-
Fe of an Fe-dependent recombinant nitrile hydratase (wild-type, NilFe) is replaced by Co generating an Co-substituted enzyme (NilCo)
betaH71L
Pseudomonas putida NRRL-18668
-
site-directed mutagenesis
-
additional information
Q7SID2
improvement of thermal stability of the industrialized mesophilic NHase by introducing stable salt-bridge interactions into its thermal sensitive regions
Y114T
Pseudonocardia thermophila JCM 3095
-
very low cobalt content and catalytic activity compared to the wild-type enzyme
-
additional information
Pseudonocardia thermophila JCM3095
-
improvement of thermal stability of the industrialized mesophilic NHase by introducing stable salt-bridge interactions into its thermal sensitive regions
-
alphaV5L
Rhodococcus rhodochrous J1
-
site-directed mutagenesis, exchange in the H-NHase does not influence the catalytic activity or the Co2+ content
-
additional information
-
construction of an amidase-negative, amiE-, recombinant strain TH3 with 25% increased nitrile hydratase activity and 60% reduced amidase activity compared to the wild-type strain TH. Usage of TH3 free cells as biocatalysts at 18C for acrylamide production, increased by 23% and 87% reduced acrylic acid by-product formation conmpared to the wild-type
additional information
Rhodococcus ruber TH
-
construction of an amidase-negative, amiE-, recombinant strain TH3 with 25% increased nitrile hydratase activity and 60% reduced amidase activity compared to the wild-type strain TH. Usage of TH3 free cells as biocatalysts at 18C for acrylamide production, increased by 23% and 87% reduced acrylic acid by-product formation conmpared to the wild-type
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
synthesis
-
nitrile hydratase-catalyzed preparation of 2-amino-2,3-dimethylbutyramide, ADBA, a key intermediate for imidazolinone herbicides, method development and optimization, evaluation of the appropriate organism, overview
synthesis
Alcaligenes faecalis CCTCC M 208168
-
nitrile hydratase-catalyzed preparation of 2-amino-2,3-dimethylbutyramide, ADBA, a key intermediate for imidazolinone herbicides, method development and optimization, evaluation of the appropriate organism, overview
-
synthesis
-
nitrile hydratase-catalyzed preparation of 2-amino-2,3-dimethylbutyramide, ADBA, a key intermediate for imidazolinone herbicides, method development and optimization, evaluation of the appropriate organism, overview
synthesis
Bacillus subtilis CCTCC M 206038
-
nitrile hydratase-catalyzed preparation of 2-amino-2,3-dimethylbutyramide, ADBA, a key intermediate for imidazolinone herbicides, method development and optimization, evaluation of the appropriate organism, overview
-
synthesis
-
-
synthesis
Brevibacterium sp. R312
-
-
-
degradation
-
treatment of acetonitrile-containing wastes on-site, Brevundimonas diminuta containing enzyme degrades acetonitrile at concentrations up to 6 M
degradation
Brevundimonas diminuta AM10-C-1
-
treatment of acetonitrile-containing wastes on-site, Brevundimonas diminuta containing enzyme degrades acetonitrile at concentrations up to 6 M
-
synthesis
-
useful for acrylamide production
synthesis
Corynebacterium pseudodiphtheriticum ZBB-41
-
useful for acrylamide production
-
synthesis
-
transformation of benzonitrile into benzohydroxamic acid performed by a cascade bienzymatic reaction involving nitrile hydration and acyl transfer of the intermediate benzamide onto hydroxylamine. The first step is catalyzed by a cell-free extract from recombinant Escherichia coli strain expressing nitrile hydratase from Klebsiella oxytoca strain 38.1.2, the second step is a cellfree extract from Rhodococcus erythropolis A4 amidase, EC 3.5.1.4
synthesis
Klebsiella oxytoca 38.1.2
-
transformation of benzonitrile into benzohydroxamic acid performed by a cascade bienzymatic reaction involving nitrile hydration and acyl transfer of the intermediate benzamide onto hydroxylamine. The first step is catalyzed by a cell-free extract from recombinant Escherichia coli strain expressing nitrile hydratase from Klebsiella oxytoca strain 38.1.2, the second step is a cellfree extract from Rhodococcus erythropolis A4 amidase, EC 3.5.1.4
-
synthesis
-
production of propionamide by use of enzyme in ultrafiltration-membrane reactor with maximum volumetric production of 0.5 g propionamide per litre and h
synthesis
-
bioconversion of 3-cyanopyridine using the in situ nitrile hydratase-amidase cascade system of resting Microbacterium imperiale CBS 498-74 cells in an ultrafiltration-membrane reactor, operated in either batch or continuous mode, method optimization, overview
synthesis
-
bioconversion of 3-cyanopyridine using the in situ nitrile hydratase-amidase cascade system of resting Microbacterium imperiale CBS 498-74 cells in an ultrafiltration-membrane reactor, carried out in continuously stirred tank UF-membrane bioreactors arranged in series, the reactor configuration enables both enzymes, involved in the cascade reaction, to work with optimized kinetics, without any purification, exploiting their differing temperature dependences, method optimization, overview
synthesis
Microbacterium imperiale CBS 498-74
-
bioconversion of 3-cyanopyridine using the in situ nitrile hydratase-amidase cascade system of resting Microbacterium imperiale CBS 498-74 cells in an ultrafiltration-membrane reactor, carried out in continuously stirred tank UF-membrane bioreactors arranged in series, the reactor configuration enables both enzymes, involved in the cascade reaction, to work with optimized kinetics, without any purification, exploiting their differing temperature dependences, method optimization, overview; bioconversion of 3-cyanopyridine using the in situ nitrile hydratase-amidase cascade system of resting Microbacterium imperiale CBS 498-74 cells in an ultrafiltration-membrane reactor, operated in either batch or continuous mode, method optimization, overview; production of propionamide by use of enzyme in ultrafiltration-membrane reactor with maximum volumetric production of 0.5 g propionamide per litre and h
-
pharmacology
-
synthesis, biotransformation and biocatalysis of unsaturated/saturated aliphatic, aromatic and heterocyclic nitriles
pharmacology
Nocardia sp. 108
-
synthesis, biotransformation and biocatalysis of unsaturated/saturated aliphatic, aromatic and heterocyclic nitriles
-
synthesis
Pseudomonas chlororaphis B23
-
-
-
synthesis
-
production of alpha-hydroxy nitriles by use of enzyme
synthesis
-
nitrile hydratase is used for large scale industrial production of important commodities such as acrylamide and nicotinamide
synthesis
Pseudonocardia thermophila JCM 3095
-
nitrile hydratase is used for large scale industrial production of important commodities such as acrylamide and nicotinamide
-
synthesis
-
transformation of benzonitrile into benzohydroxamic acid performed by a cascade bienzymatic reaction involving nitrile hydration and acyl transfer of the intermediate benzamide onto hydroxylamine. The first step is catalyzed by a cell-free extract from recombinant Escherichia coli strain expressing nitrile hydratase from Raoultella terrigena srain 77.1, the second step is a cell-free extract from Rhodococcus erythropolis A4 amidase, EC 3.5.1.4
synthesis
Raoultella terrigena 77.1
-
transformation of benzonitrile into benzohydroxamic acid performed by a cascade bienzymatic reaction involving nitrile hydration and acyl transfer of the intermediate benzamide onto hydroxylamine. The first step is catalyzed by a cell-free extract from recombinant Escherichia coli strain expressing nitrile hydratase from Raoultella terrigena srain 77.1, the second step is a cell-free extract from Rhodococcus erythropolis A4 amidase, EC 3.5.1.4
-
synthesis
-
nitrile hydratase-catalyzed preparation of 2-amino-2,3-dimethylbutyramide, ADBA, a key intermediate for imidazolinone herbicides, method development and optimization, evaluation of the appropriate organism, overview
synthesis
Rhodococcus boritolerans CCTCC M 208108
-
nitrile hydratase-catalyzed preparation of 2-amino-2,3-dimethylbutyramide, ADBA, a key intermediate for imidazolinone herbicides, method development and optimization, evaluation of the appropriate organism, overview
-
synthesis
-
production of D-tert-leucine-nitrile from racemic tert-leucine-nitrile by use of enzyme plus D-selective amidase from Variovorax paradoxus
synthesis
-
industrial production of (S)-2,2-dimethylcyclopropanecarboxylic acid
synthesis
-
the enzyme is useful in synthesis of compounds by hydrating biotransformations, optimization of strain cultivation and enzyme production and activity, overview
synthesis
-
enzyme can be used in conjunction with a stereoselective amidase to synthesize ethyl (S)-4-chloro-3-hydroxybutyrate, an intermediate for a hypercholesterolemia drug, Atorvastatin
synthesis
-
transformation of benzonitrile into benzohydroxamic acid performed by a cascade bienzymatic reaction involving nitrile hydration and acyl transfer of the intermediate benzamide onto hydroxylamine. The first step is catalyzed by a cell-free extract from Rhodococcus erythropolis A4 containing nitrile hydratase, the second step is a cell-free extract from Rhodococcus erythropolis A4 amidase, EC 3.5.1.4
synthesis
Rhodococcus erythropolis 870-AN019
-
production of D-tert-leucine-nitrile from racemic tert-leucine-nitrile by use of enzyme plus D-selective amidase from Variovorax paradoxus
-
synthesis
Rhodococcus erythropolis A4
-
transformation of benzonitrile into benzohydroxamic acid performed by a cascade bienzymatic reaction involving nitrile hydration and acyl transfer of the intermediate benzamide onto hydroxylamine. The first step is catalyzed by a cell-free extract from Rhodococcus erythropolis A4 containing nitrile hydratase, the second step is a cell-free extract from Rhodococcus erythropolis A4 amidase, EC 3.5.1.4
-
synthesis
Rhodococcus erythropolis MTCC 1526
-
the enzyme is useful in synthesis of compounds by hydrating biotransformations, optimization of strain cultivation and enzyme production and activity, overview
-
synthesis
Rhodococcus erythropolis N4
-
enzyme can be used in conjunction with a stereoselective amidase to synthesize ethyl (S)-4-chloro-3-hydroxybutyrate, an intermediate for a hypercholesterolemia drug, Atorvastatin
-
degradation
-
treatment of acetonitrile-containing wastes on-site, Rhodococcus pyridinivorans S85-2 containing enzyme degrades acetonitrile at concentrations up to 6 M
environmental protection
-
NHase is used in two-step degradation (including amidase, EC 3.5.1.4) of acetonitrile-containing waste
environmental protection
Rhodococcus pyridinivorans S82-2
-
NHase is used in two-step degradation (including amidase, EC 3.5.1.4) of acetonitrile-containing waste
-
degradation
Rhodococcus pyridinivorans S85-2
-
treatment of acetonitrile-containing wastes on-site, Rhodococcus pyridinivorans S85-2 containing enzyme degrades acetonitrile at concentrations up to 6 M
-
synthesis
-
H-NHase is used in the industrial production of acrylamide and nicotinamide
synthesis
-
useful for modification of polyacrylonitrile fibers and granulates
synthesis
-
production of nicotinamide (=vitamin B3) for vitamin supplement for food and animal feed
synthesis
-
production of 2-naphthylacetamide by one-pot chemo-enzymatic conversion
synthesis
Rhodococcus rhodochrous IFO 15564
-
production of 2-naphthylacetamide by one-pot chemo-enzymatic conversion
-
synthesis
Rhodococcus rhodochrous J1
-
; H-NHase is used in the industrial production of acrylamide and nicotinamide; production of nicotinamide (=vitamin B3) for vitamin supplement for food and animal feed
-
synthesis
Rhodococcus rhodochrous NCIMB 11216
-
useful for modification of polyacrylonitrile fibers and granulates
-
synthesis
-
nitrile hydratase-catalyzed preparation of 2-amino-2,3-dimethylbutyramide, ADBA, a key intermediate for imidazolinone herbicides, method development and optimization, evaluation of the appropriate organism, overview
synthesis
Rhodococcus ruber CCTCC M 206040
-
nitrile hydratase-catalyzed preparation of 2-amino-2,3-dimethylbutyramide, ADBA, a key intermediate for imidazolinone herbicides, method development and optimization, evaluation of the appropriate organism, overview
-
environmental protection
-
degradation of nitrile waste
synthesis
-
-
synthesis
-
industrial production of nicotinamide; useful for acrylamide production
synthesis
-
useful for acrylamide production
synthesis
-
nitrile hydratase is an enzyme used in the industrial biotechnological production of acrylamide
synthesis
-
nitrile hydratase-catalyzed preparation of 2-amino-2,3-dimethylbutyramide, ADBA, a key intermediate for imidazolinone herbicides, method development and optimization, evaluation of the appropriate organism, overview
synthesis
Rhodococcus sp. N-774
-
-
-
synthesis
Rhodococcus sp. N595
-
nitrile hydratase-catalyzed preparation of 2-amino-2,3-dimethylbutyramide, ADBA, a key intermediate for imidazolinone herbicides, method development and optimization, evaluation of the appropriate organism, overview
-
environmental protection
Rhodococcus sp. RHA1
-
degradation of nitrile waste
-
synthesis
-
nitrile hydratase-catalyzed preparation of 2-amino-2,3-dimethylbutyramide, ADBA, a key intermediate for imidazolinone herbicides, method development and optimization, evaluation of the appropriate organism, overview
synthesis
Serratia marcescens CCTCC M 208231
-
nitrile hydratase-catalyzed preparation of 2-amino-2,3-dimethylbutyramide, ADBA, a key intermediate for imidazolinone herbicides, method development and optimization, evaluation of the appropriate organism, overview
-