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
LITERATURE
an aliphatic amide = a nitrile + H2O
show the reaction diagram
light
-
-
-
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
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
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
substrate binding occurs via breathing and flip-flop mechanisms
-
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
reaction mechanism, 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
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
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
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
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
detailed reaction mechanism using large quantum-mechanical active site models, overview. The attack of Cys114-SO- on the coordinated nitrile forms a cyclic intermediate. Cys109-S-S-Cys114 disulfide formation promotes cleavage of the latter to give the amide. Active-site regeneration occurs through attack of water on the disulfide, putative cyclic intermediate structure, overview
-
an aliphatic amide = a nitrile + H2O
show the reaction diagram
mechanism of action for the hydration of nitriles by NHase, overview. The cysteine-sulfenic acid ligand acts as the catalytic nucleophile. The first step in catalysis involves the direct ligation of the nitrile to the active site lowspin, trivalent metal ion. One proton transfer occurs between the alphaCys113-OH ligand and the nitrile N-atom, while the second transfer occurs between the water molecule that reforms alphaCys113-OH and the newly forming imidate N-atom
-
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
thermal-stable mechanism of thermophilic nitrile hydratases, molecular dynamic simulation, overview
Pseudonocardia thermophila JCM3095
-
-
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
-
-
an aliphatic amide = a nitrile + H2O
show the reaction diagram
possible role of water and active center residues in reaction mechanism is shown, reaction mechanism, overview, 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, 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, mechanism of action for the hydration of nitriles by NHase, overview. The cysteine-sulfenic acid ligand acts as the catalytic nucleophile. The first step in catalysis involves the direct ligation of the nitrile to the active site lowspin, trivalent metal ion. One proton transfer occurs between the alphaCys113-OH ligand and the nitrile N-atom, while the second transfer occurs between the water molecule that reforms alphaCys113-OH and the newly forming imidate N-atom
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
Bacillus sp. SC-105-1
-
-
REACTION TYPE
ORGANISM
UNIPROT
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, 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
BRENDA Link
KEGG Link
MetaCyc Link
acrylonitrile degradation I
-
-
aldoxime degradation
-
-
Aminobenzoate degradation
-
-
degradation of aromatic, nitrogen containing compounds
-
-
Fluorobenzoate degradation
-
-
IAA biosynthesis
-
-
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
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
Q7SID3
-
Co-type NHase
Pseudonocardia thermophila JCM 3095
Q7SID2
;
-
Co-type NHase
Pseudonocardia thermophila JCM 3095
Q7SID3
-
-
Co-type nitrile hydratase
-
-
Co-type nitrile hydratase
Pseudomonas putida NRRL-18668
-
-
-
cobalt-containing nitrile hydratase
Q7SID2, Q7SID3
-
cobalt-containing nitrile hydratase
Pseudonocardia thermophila JCM 3095
Q7SID2, Q7SID3
;
-
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
-
-
-
-
iron-type nitrile hydratase
Rhodococcus hoagii
-
-
iron-type nitrile hydratase
Rhodococcus hoagii TG328-2
-
-
-
L-Nhase
-
-
-
-
L-Nhase
Rhodococcus fascians DSM 43985
-
-
-
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
Q7SID2, Q7SID3
-
NHase
Bacillus sp. SC-105-1
Q7SID2, Q7SID3
-
-
NHase
Bacillus subtilis CCTCC M 206038
-
-
-
NHase
Q5XPL4, Q5XPL5
-
NHase
Comamonas testosteroni 5-MGAM-4D
Q5XPL4, Q5XPL5
-
-
NHase
Mesorhizobium sp.
-
-
NHase
Mesorhizobium sp. BNC1
-
-
-
NHase
Q8GJG6
-
NHase
Q8GJG6
-
-
NHase
A5W402
-
NHase
Pseudomonas putida NRRL-18668
-
;
-
NHase
Pseudonocardia thermophila JCM 3095
Q7SID2, Q7SID3
-
-
NHase
Pseudonocardia thermophila JCM3095
Q7SID2, Q7SID3
-
-
NHase
Rhodococcus boritolerans CCTCC M 208108
-
-
-
NHase
Rhodococcus erythropolis AJ270
P13448
-
-
NHase
Rhodococcus erythropolis MTCC 1526, Rhodococcus erythropolis N4, Rhodococcus erythropolis N771
-
-
-
NHase
Rhodococcus hoagii
-
-
NHase
Rhodococcus hoagii TG328-2
-
;
-
NHase
Rhodococcus qingshengii ZA0707
-
-
-
NHase
Rhodococcus rhodochrous PA-34
-
-
-
NHase
Rhodococcus ruber CCTCC M 206040, Rhodococcus ruber CGMCC3090, Rhodococcus ruber TH
-
-
-
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
-
-
-
NHase
B6CWJ3, B6CWJ4, B6CWJ5
-
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
-
-
NthAB
K9NKC3, K9NLN7
gene name
NthAB
K9NKC3, K9NLN7
gene name
-
ppNHase
Pseudomonas putida NRRL-18668
-
-
-
ReNHase
Rhodococcus hoagii
-
-
ReNHase
Rhodococcus hoagii TG328-2
-
-
-
TNHase
B6CWJ3, B6CWJ4, B6CWJ5
-
toyocamycin nitrile hydratase
B6CWJ3, B6CWJ4, B6CWJ5
-
CAS REGISTRY NUMBER
COMMENTARY
82391-37-5
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
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
contain at least two NHases, it is currently not known whether the aeroplysinin-1-hydrating enzyme is of sponge origin or produced by its symbiotic microorganisms
-
-
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; beta-subunit; strain SC-J05-1
-
-
Manually annotated by BRENDA team
Bacillus smithii SC-J05-1
alpha-subunit; strain SC-J05-1; beta-subunit; strain SC-J05-1
-
-
Manually annotated by BRENDA team
alpha-subunit
UniProt
Manually annotated by BRENDA team
beta-subunit
UniProt
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
alpha-subunit
UniProt
Manually annotated by BRENDA team
Bacillus sp. SC-105-1
beta-subunit
UniProt
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
alpha subunit
UniProt
Manually annotated by BRENDA team
beta subunit
Swissprot
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
alpha subunit
UniProt
Manually annotated by BRENDA team
Comamonas testosteroni 5-MGAM-4D
beta subunit
Swissprot
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
gene Pput_2728 encoding subunit alpha; gene Pput_2729 encoding subunit alpha
UniProt
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
gene nthA, alpha-subunit; gene nthAB
UniProt
Manually annotated by BRENDA team
gene nthB, beta-subunit; gene nthAB
UniProt
Manually annotated by BRENDA team
gene nthA, alpha-subunit; gene nthAB
UniProt
Manually annotated by BRENDA team
gene nthB, beta-subunit; gene nthAB
UniProt
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
-
-
-
Manually annotated by BRENDA team
Pseudonocardia thermophila JCM 3095
alpha-subunit
SwissProt
Manually annotated by BRENDA team
Pseudonocardia thermophila JCM 3095
beta-subunit
UniProt
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
beta-subunit
UniProt
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
a soil isolate
-
-
Manually annotated by BRENDA team
alpha subunit; recombinant enzyme
Swissprot
Manually annotated by BRENDA team
alpha-subunit, gene nha1; genes nha1 and nha2 encoding the alpha and beta subunits of nitrile hydratase
UniProt
Manually annotated by BRENDA team
beta-subunit, gene nha2; genes nha1 and nha2 encoding the alpha and beta subunits of nitrile hydratase
UniProt
Manually annotated by BRENDA team
gene nha1, alpha-subunit; genes nha1 and nha2 encoding the subunits of nitrile hydratase
UniProt
Manually annotated by BRENDA team
gene nha1, beta-subunit; genes nha1 and nha2 encoding the subunits of nitrile hydratase; gene nha2, beta-subunit; genes nha1 and nha2 encoding the subunits of nitrile hydratase
UniProt
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 A4
a soil isolate
-
-
Manually annotated by BRENDA team
Rhodococcus erythropolis A4
gene nha1, alpha-subunit; genes nha1 and nha2 encoding the subunits of nitrile hydratase
UniProt
Manually annotated by BRENDA team
Rhodococcus erythropolis A4
gene nha1, beta-subunit; genes nha1 and nha2 encoding the subunits of nitrile hydratase; gene nha2, beta-subunit; genes nha1 and nha2 encoding the subunits of nitrile hydratase
UniProt
Manually annotated by BRENDA team
Rhodococcus erythropolis AJ270
-
UniProt
Manually annotated by BRENDA team
Rhodococcus erythropolis AJ270
-
-
-
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 CCM 2595
alpha-subunit, gene nha1; genes nha1 and nha2 encoding the alpha and beta subunits of nitrile hydratase
UniProt
Manually annotated by BRENDA team
Rhodococcus erythropolis CCM 2595
beta-subunit, gene nha2; genes nha1 and nha2 encoding the alpha and beta subunits of nitrile hydratase
UniProt
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 DSM 43985
strain DSM43985
-
-
Manually annotated by BRENDA team
Rhodococcus hoagii
-
-
-
Manually annotated by BRENDA team
Rhodococcus hoagii
strain TG328-2
-
-
Manually annotated by BRENDA team
Rhodococcus hoagii TG328-2
-
-
-
Manually annotated by BRENDA team
Rhodococcus hoagii TG328-2
strain TG328-2
-
-
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
a soil isolate
-
-
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
a soil isolate
-
-
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
-
-
-
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
gene toyJ; genes toyJ, toyK, and toyL encoding the three subunits of the enzyme
UniProt
Manually annotated by BRENDA team
gene toyK; genes toyJ, toyK, and toyL encoding the three subunits of the enzyme
UniProt
Manually annotated by BRENDA team
gene toyL; genes toyJ, toyK, and toyL encoding the three subunits of the enzyme
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
A5W402
because of the absence of sequence similarity between the Co- and Fe-type NHase activators, the two types of NHases might be assembled and maturated by different molecular mechanisms
evolution
-
mass spectrometry of the primary structure of the studied NHases does not reveal any homology to known NHases
evolution
-
toyocamycin nitrile hydratase is a unique three-subunit member of the nitrile hydratase family
metabolism
-
hydrolysis mediated by nitrilase, NHase, and amidase is the most common way for nitrile degradation
metabolism
P13448
hydrolysis mediated by nitrilase, NHase, and amidase is the most common way for nitrile degradation
metabolism
-
the enzyme is important in the indole-3-acetic acid biosynthesis pathway together with the nitrilase, EC 3.5.5.1, which produces indole-3-amide, but also indole-3-acetic acid , overview
metabolism
-
the enzyme is important in the indole-3-acetic acid biosynthesis pathway together with the nitrilase, EC 3.5.5.1, which produces indole-3-amide, but also indole-3-acetic acid , overview
-
physiological function
-
formation of aeroplysinin-1 and of the corresponding dienone amide is part of the chemical defence system of the mediterrenean sponge Aplysina cavernicola
physiological function
-
toyocamycin nitrile hydratase is involved in the biosynthesis of pyrrolopyrimidine antibiotics
metabolism
Pseudonocardia thermophila JCM 3095, Rhodococcus erythropolis AJ270
-
hydrolysis mediated by nitrilase, NHase, and amidase is the most common way for nitrile degradation
-
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
-
in Co-type NHase, the side-chain of alphaThr109, located iin the cysteine cluster region, undergoes a hydrophobic interaction with the side-chain of alphaVal136. The hydroxyl group of residue alphaTyr114, located near the cysteine cluster region, forms hydrogen bonds with the main-chain oxygen atoms of alphaLeu119 and alphaLeu121, via a water molecule
additional information
-
structural modeling, overview
additional information
-
the alpha-subunit is the minimal sequence needed for nitrile hydration providing a simplified scaffold to study the mechanism and posttranslational modification of this important class of catalysts
additional information
-
the recombinant enzyme shows almost the same specific activity and other properties as the native enzyme. Structure of the active center of the recombinant enzyme, overview
additional information
Pseudonocardia thermophila JCM 3095
-
in Co-type NHase, the side-chain of alphaThr109, located iin the cysteine cluster region, undergoes a hydrophobic interaction with the side-chain of alphaVal136. The hydroxyl group of residue alphaTyr114, located near the cysteine cluster region, forms hydrogen bonds with the main-chain oxygen atoms of alphaLeu119 and alphaLeu121, via a water molecule, the recombinant enzyme shows almost the same specific activity and other properties as the native enzyme. Structure of the active center of the recombinant enzyme, overview, structural modeling, 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
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
Rhodococcus hoagii
-
39% conversion
-
-
?
(R,S)-2-bromopropionitrile + H2O
?
show the reaction diagram
Rhodococcus hoagii
-
47% conversion
-
-
?
(R,S)-2-chloropropionitrile + H2O
?
show the reaction diagram
Rhodococcus hoagii
-
48% conversion
-
-
?
(R,S)-2-phenylbutyronitrile + H2O
?
show the reaction diagram
Rhodococcus hoagii
-
51% conversion
-
-
?
(R,S)-2-phenylpropionitrile + H2O
?
show the reaction diagram
Rhodococcus hoagii
-
43% conversion
-
-
?
(R,S)-3-oxo-2-phenylbutyronitrile + H2O
?
show the reaction diagram
Rhodococcus hoagii
-
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
-
-
-
-
?
2,2-dimethylcyclopropanecarbonitrile + H2O
?
show the reaction diagram
P13448
-
-
-
?
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-dichlorobenzamide + H2O
2,6-dichlorobenzoic acid
show the reaction diagram
Rhodococcus erythropolis, Rhodococcus erythropolis A4
-
-
-
-
?
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, Alcaligenes faecalis CCTCC M 208168, Rhodococcus boritolerans CCTCC M 208108, Bacillus subtilis CCTCC M 206038, 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-phenylbutanenitrile + H2O
?
show the reaction diagram
P13448
-
-
-
?
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
Rhodococcus hoagii
-
-
-
-
?
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
-
the enzyme is highly enantioselective with the compound
-
-
?
2-phenylpropionitrile + H2O
2-phenylpropionamide
show the reaction diagram
-
the enzyme is not enantioselective with the compound
-
-
?
2-phenylpropionitrile + H2O
2-phenylpropionamide
show the reaction diagram
-
the enzyme is highly enantioselective with the compound
-
-
?
2-phenylpropionitrile + H2O
2-phenylpropionamide
show the reaction diagram
Rhodococcus sp. Novo SP361
-
-
-
-
?
2-phenylpropionitrile + H2O
2-phenylpropionamide
show the reaction diagram
Rhodococcus erythropolis AJ270
-
the enzyme is not enantioselective with the compound
-
-
?
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-(1-cyanoethyl)benzoic acid + H2O
?
show the reaction diagram
-
the enzyme is enantioselective with the compound
-
-
?
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
Rhodococcus hoagii
-
-
-
-
?
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
Q5XPL4, Q5XPL5
-
-
-
?
3-cyanopyridine + H2O
pyridine-3-carbamide
show the reaction diagram
-
-
-
-
?
3-cyanopyridine + H2O
pyridine-3-carbamide
show the reaction diagram
P13448
-
-
-
?
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
-
-
i.e. nicotinamide
-
3-cyanopyridine + H2O
pyridine-3-carbamide
show the reaction diagram
A5W402
lower activity
-
-
?
3-cyanopyridine + H2O
pyridine-3-carbamide
show the reaction diagram
B6CWJ3, B6CWJ4, B6CWJ5
a niacin precursor
-
-
?
3-cyanopyridine + H2O
pyridine-3-carbamide
show the reaction diagram
Comamonas testosteroni 5-MGAM-4D
Q5XPL4, Q5XPL5
-
-
-
?
3-cyanopyridine + H2O
pyridine-3-carbamide
show the reaction diagram
Aeribacillus pallidus RAPc8
-
-
-
-
?
3-cyanopyridine + H2O
pyridine-3-carbamide
show the reaction diagram
Pseudonocardia thermophila JCM3095
Q7SID3
-
-
-
?
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
Pseudomonas putida NRRL-18668
-
-
-
-
?
3-cyanopyridine + H2O
pyridine-3-carbamide
show the reaction diagram
Pseudomonas putida NRRL-18668
-
-
i.e. nicotinamide
-
?
3-cyanopyridine + H2O
pyridine-3-carbamide
show the reaction diagram
Pseudonocardia thermophila JCM 3095
-
-
-
-
?
3-cyanopyridine + H2O
pyridine-3-carbamide
show the reaction diagram
Rhodococcus erythropolis AJ270
P13448
-
-
-
?
3-cyanopyridine + H2O
pyridine-3-carbamide
show the reaction diagram
Rhodococcus fascians DSM 43985
-
-
-
-
?
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
Q7SID2, Q7SID3
substrate of recombinant wild-type enzyme, not of mutant enzymes
-
-
?
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
Pseudonocardia thermophila JCM 3095
Q7SID2, Q7SID3
substrate of recombinant wild-type enzyme, not of mutant enzymes
-
-
?
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
A5W402
lower activity
-
-
?
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-hydroxybutanenitrile + H2O
?
show the reaction diagram
P13448
-
-
-
?
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-chlorobutyronitrile + H2O
4-chlorobutyramide
show the reaction diagram
A5W402
-
-
-
?
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
-
-
-
-
?
4-cyanopyridine + H2O
pyridine-4-carbamide
show the reaction diagram
A5W402
lower activity
-
-
?
4-cyanopyridine + H2O
pyridine-4-carbamide
show the reaction diagram
Aeribacillus pallidus RAPc8
-
-
-
-
?
4-cyanopyridine + H2O
isonicotinamide
show the reaction diagram
Q7SID2, Q7SID3
substrate of recombinant wild-type enzyme, not of mutant enzymes
-
-
?
4-cyanopyridine + H2O
isonicotinamide
show the reaction diagram
Pseudonocardia thermophila JCM 3095
Q7SID2, Q7SID3
substrate of recombinant wild-type enzyme, not of mutant enzymes
-
-
?
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
-
-
-
-
?
acetonitrile + H2O
acetamide
show the reaction diagram
P13448
-
-
-
?
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
Pseudonocardia thermophila JCM 3095
-
-
-
-
?
acetonitrile + H2O
acetamide
show the reaction diagram
Rhodococcus erythropolis AJ270
P13448
-
-
-
?
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
Rhodococcus rhodochrous NCIMB 11216
-
-
-
-
?
acrylonitrile + H2O
2-propenoic acid amide
show the reaction diagram
Brevibacterium sp. R312
-
-
-
-
-
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
?
show the reaction diagram
Pseudonocardia thermophila, Pseudonocardia thermophila JCM 3095
-
-
-
-
?
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
-
-
-
-
?
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
Q7SID2, Q7SID3
-
-
-
?
acrylonitrile + H2O
acrylamide
show the reaction diagram
P13448
-
-
-
?
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
A5W402
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
Q7SID2, Q7SID3
substrate of recombinant wild-type and mutant enzymes
-
-
?
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
-
-
-
-
r
acrylonitrile + H2O
acrylamide
show the reaction diagram
Rhodococcus ruber CGMCC3090
-
highest activity
-
-
?
acrylonitrile + H2O
acrylamide
show the reaction diagram
Pseudomonas putida NRRL-18668
-
-
-
-
?
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
Pseudonocardia thermophila JCM 3095
Q7SID2, Q7SID3
substrate of recombinant wild-type and mutant enzymes
-
-
?
acrylonitrile + H2O
acrylamide
show the reaction diagram
Rhodococcus erythropolis AJ270
P13448
-
-
-
?
acrylonitrile + H2O
acrylamide
show the reaction diagram
Rhodococcus sp. RHA1
-
substrate specificity: acetonitrile ~ propionitrile > acrylonitrile >> butyronitrile
-
-
r
acrylonitrile + H2O
acrylamide
show the reaction diagram
Rhodococcus sp. SHZ-1
-
-
-
-
?
acrylonitrile + H2O
acrylamide
show the reaction diagram
Bacillus sp. SC-105-1
Q7SID2, Q7SID3
-
-
-
?
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%
-
?
aeroplysinin-1 + H2O
verongiaquinol
show the reaction diagram
-
high substrate specificity towards the physiological substrate aeroplysinin-1
-
-
?
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
-
?
benzeneacetonitrile + H2O
?
show the reaction diagram
A5W402
very low activity
-
-
?
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
Rhodococcus hoagii
-
-
-
-
?
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 erythropolis N4
-
low activity
-
-
?
benzonitrile + H2O
benzoic acid amide
show the reaction diagram
Rhodococcus hoagii TG328-2
-
-
-
-
?
benzonitrile + H2O
?
show the reaction diagram
Pseudonocardia thermophila, Pseudonocardia thermophila JCM 3095
-
-
-
-
?
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
-
-
-
-
?
benzonitrile + H2O
benzamide
show the reaction diagram
P13448
-
-
-
?
benzonitrile + H2O
benzamide
show the reaction diagram
A5W402
lower activity
-
-
?
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
Q7SID2, Q7SID3
substrate of recombinant wild-type and mutant enzymes
-
-
?
benzonitrile + H2O
benzamide
show the reaction diagram
Rhodococcus erythropolis A4
-
-
-
-
?
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 + H2O
benzamide
show the reaction diagram
Pseudonocardia thermophila JCM 3095
Q7SID2, Q7SID3
substrate of recombinant wild-type and mutant enzymes
-
-
?
benzonitrile + H2O
benzamide
show the reaction diagram
Rhodococcus rhodochrous PA-34
-
-
-
-
?
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
bromoxynil acid + H2O
?
show the reaction diagram
Rhodococcus rhodochrous, Rhodococcus erythropolis, Rhodococcus erythropolis A4, Rhodococcus rhodochrous PA-34
-
-
-
-
?
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
-
-
?
butyronitrile + H2O
?
show the reaction diagram
P13448
-
-
-
?
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
-
-
-
-
?
chloroxynil acid + H2O
?
show the reaction diagram
Rhodococcus rhodochrous, Rhodococcus erythropolis, Rhodococcus erythropolis A4, Rhodococcus rhodochrous PA-34
-
-
-
-
?
chloroxynil amide + H2O
?
show the reaction diagram
Rhodococcus rhodochrous, Rhodococcus rhodochrous PA-34
-
-
-
-
?
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
-
-
-
-
?
dichlobenil acid + H2O
?
show the reaction diagram
-
-
-
-
?
dichlobenil amide + 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
-
-
-
-
?
indole-3-nitrile + H2O
indole-3-acetamide
show the reaction diagram
K9NKC3, K9NLN7
-
-
-
?
indole-3-nitrile + H2O
indole-3-acetamide
show the reaction diagram
K9NKC3, K9NLN7
-
the nitrile hydratase produces only indole-3-acetamide, no indole-3-acetic acid
-
?
indole-3-nitrile + H2O
indole-3-acetamide
show the reaction diagram
K9NKC3, K9NLN7
-
-
-
?
indole-3-nitrile + H2O
indole-3-acetamide
show the reaction diagram
K9NKC3, K9NLN7
-
the nitrile hydratase produces only indole-3-acetamide, no indole-3-acetic acid
-
?
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
Rhodococcus hoagii
-
-
-
-
?
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
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
isobutyric acid amide
show the reaction diagram
Rhodococcus hoagii TG328-2
-
-
-
-
?
isobutyronitrile + H2O
isobutyramide
show the reaction diagram
-
-
-
-
?
isobutyronitrile + H2O
isobutyramide
show the reaction diagram
A5W402
-
-
-
?
isobutyronitrile + H2O
?
show the reaction diagram
P13448
-
-
-
?
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
?
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
Rhodococcus hoagii
-
-
-
-
?
methacrylonitrile + H2O
methacrylamide
show the reaction diagram
P13448
-
-
-
?
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
Q7SID2, Q7SID3
substrate of recombinant wild-type and mutant enzymes
-
-
?
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
Pseudonocardia thermophila JCM 3095
Q7SID2, Q7SID3
substrate of recombinant wild-type and mutant enzymes
-
-
?
methacrylonitrile + H2O
methacrylamide
show the reaction diagram
Rhodococcus hoagii TG328-2
-
-
-
-
?
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
-
-
-
-
?
naproxennitrile + H2O
?
show the reaction diagram
-
the enzyme is enantioselective with the compound
-
-
?
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
Rhodococcus rhodochrous NCIMB 11216
-
10% of conversion in 24 h
i.e. propionamide
?
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 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
P13448
-
-
-
?
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
-
-
-
-
r
propionitrile + H2O
propionamide
show the reaction diagram
Rhodococcus sp. RHA1
-
substrate specificity: acetonitrile ~ propionitrile > acrylonitrile >> butyronitrile
-
-
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
-
-
-
-
?
tert-butylisonitrile + H2O
?
show the reaction diagram
-
-
-
-
?
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
toyocamycin + H2O
toyocamycin acid amide
show the reaction diagram
B6CWJ3, B6CWJ4, B6CWJ5
-
-
-
?
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 hoagii
-
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
n-pentanoic acid amide
show the reaction diagram
Rhodococcus hoagii TG328-2
-
almost 9000fold higher activity towards valeronitrile compared to (R,S)-2-phenylpropionitrile
-
-
?
valeronitrile + H2O
valeramide
show the reaction diagram
-
-
-
-
?
valeronitrile + H2O
?
show the reaction diagram
A5W402
-
-
-
?
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
?
-
-
substrate specificity, overview
-
-
-
additional information
?
-
P13448
substrate 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
?
-
Rhodococcus hoagii
-
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
?
-
P13448
molecular modeling study of enzyme-substrate binding modes in the bi-enzyme pathway for degradation of nitrile to acid, specific residues within the enzyme's binding pockets form diverse contacts with the substrate, molecular docking, overview. Top substrate having favorable interactions with nitrile hydratase is benzonitrile
-
-
-
additional information
?
-
-
molecular modeling study of enzyme-substrate binding modes in the bi-enzyme pathway for degradation of nitrile to acid, specific residues within the enzyme's binding pockets formed diverse contacts with the substrate, molecular docking, overview. Top substrate having favorable interactions with nitrile hydratase is 3-cyanopyridine
-
-
-
additional information
?
-
-
analysis of enzyme enantioselectivity against a broad range of nitrile substrates, overview. At least one bulky group in close proximity to the alpha-position of the chiral nitriles seems to be necessary for enantioselectivity of NHases. Nitrile groups attached to a quaternary carbon atom are only reluctantly accepted and show no selectivity
-
-
-
additional information
?
-
-
analysis of enzyme enantioselectivity against a broad range of nitrile substrates, overview. The enzyme is aselective with a range of different 2-phenylacetonitriles. At least one bulky group in close proximity to the alpha-position of the chiral nitriles seems to be necessary for enantioselectivity of NHases. Nitrile groups attached to a quaternary carbon atom are only reluctantly accepted and show no selectivity
-
-
-
additional information
?
-
-
no activity with 2,6-dichlorobenzamide and dichlobenil acid
-
-
-
additional information
?
-
-
no activity with aeroplysinin-1 derivatives (1S,2R)-3,5-dibromo-1-(cyanomethyl)-4-methoxycyclohexa-3,5-diene-1,2-diyl diacetate, (2-hydroxy-4-methoxyphenyl)acetonitrile, and (3,5-dibromo-2-hydroxy-4-methoxyphenyl)acetonitrile
-
-
-
additional information
?
-
-
no activity with chloroxynil amide
-
-
-
additional information
?
-
B6CWJ3, B6CWJ4, B6CWJ5
substrate specificity of trimeric enzyme compared to the isolated alpha-subunit, overview. Activity of the alpha-subunit of a nitrile hydratase distinguishes among possible mechanisms of nitrile hydration by adding significant weight to those that rely solely on residues derived from the alpha-subunit. No activity with thiocyanate
-
-
-
additional information
?
-
-
the enzyme shows a preference for aromatic nitriles as substrates rather than aliphatic ones. Tryptophan residue betaTrp72 may be involved in substrate binding
-
-
-
additional information
?
-
A5W402
the Fe-type NHase exhibits broad substrate specificity
-
-
-
additional information
?
-
-
analysis of enzyme enantioselectivity against a broad range of nitrile substrates, overview. At least one bulky group in close proximity to the alpha-position of the chiral nitriles seems to be necessary for enantioselectivity of NHases. Nitrile groups attached to a quaternary carbon atom are only reluctantly accepted and show no selectivity
-
-
-
additional information
?
-
Rhodococcus erythropolis A4
-
no activity with chloroxynil amide
-
-
-
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
?
-
-
analysis of enzyme enantioselectivity against a broad range of nitrile substrates, overview. At least one bulky group in close proximity to the alpha-position of the chiral nitriles seems to be necessary for enantioselectivity of NHases. Nitrile groups attached to a quaternary carbon atom are only reluctantly accepted and show no selectivity
-
-
-
additional information
?
-
Raoultella terrigena 77.1
-
substrate specificity of strain 77.1, no activity with 4-tolunitrile and 3-chlorobenzonitrile, overview
-
-
-
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
?
-
Pseudonocardia thermophila JCM 3095
-
substrate specificity, overview, molecular modeling study of enzyme-substrate binding modes in the bi-enzyme pathway for degradation of nitrile to acid, specific residues within the enzyme's binding pockets formed diverse contacts with the substrate, molecular docking, overview. Top substrate having favorable interactions with nitrile hydratase is 3-cyanopyridine
-
-
-
additional information
?
-
Pseudonocardia thermophila JCM 3095
-
the enzyme shows a preference for aromatic nitriles as substrates rather than aliphatic ones. Tryptophan residue betaTrp72 may be involved in substrate binding
-
-
-
additional information
?
-
Rhodococcus erythropolis AJ270
-
analysis of enzyme enantioselectivity against a broad range of nitrile substrates, overview. The enzyme is aselective with a range of different 2-phenylacetonitriles. At least one bulky group in close proximity to the alpha-position of the chiral nitriles seems to be necessary for enantioselectivity of NHases. Nitrile groups attached to a quaternary carbon atom are only reluctantly accepted and show no selectivity
-
-
-
additional information
?
-
Rhodococcus erythropolis AJ270
P13448
substrate specificity, overview, molecular modeling study of enzyme-substrate binding modes in the bi-enzyme pathway for degradation of nitrile to acid, specific residues within the enzyme's binding pockets form diverse contacts with the substrate, molecular docking, overview. Top substrate having favorable interactions with nitrile hydratase is benzonitrile
-
-
-
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
?
-
Rhodococcus hoagii 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
?
-
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 PA-34
-
no activity with 2,6-dichlorobenzamide and dichlobenil acid
-
-
-
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
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, Alcaligenes faecalis CCTCC M 208168, Rhodococcus boritolerans CCTCC M 208108, Bacillus subtilis CCTCC M 206038, 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
-
-
-
-
?
indole-3-nitrile + H2O
indole-3-acetamide
show the reaction diagram
K9NKC3, K9NLN7
-
the nitrile hydratase produces only indole-3-acetamide, no indole-3-acetic acid
-
?
indole-3-nitrile + H2O
indole-3-acetamide
show the reaction diagram
K9NKC3, K9NLN7
-
the nitrile hydratase produces only indole-3-acetamide, no indole-3-acetic acid
-
?
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
-
-
-
-
?
toyocamycin + H2O
toyocamycin acid amide
show the reaction diagram
B6CWJ3, B6CWJ4, B6CWJ5
-
-
-
?
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
?
-
P13448
molecular modeling study of enzyme-substrate binding modes in the bi-enzyme pathway for degradation of nitrile to acid, specific residues within the enzyme's binding pockets form diverse contacts with the substrate, molecular docking, overview. Top substrate having favorable interactions with nitrile hydratase is benzonitrile
-
-
-
additional information
?
-
-
molecular modeling study of enzyme-substrate binding modes in the bi-enzyme pathway for degradation of nitrile to acid, specific residues within the enzyme's binding pockets formed diverse contacts with the substrate, molecular docking, overview. Top substrate having favorable interactions with nitrile hydratase is 3-cyanopyridine
-
-
-
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
?
-
Pseudonocardia thermophila JCM 3095
-
molecular modeling study of enzyme-substrate binding modes in the bi-enzyme pathway for degradation of nitrile to acid, specific residues within the enzyme's binding pockets formed diverse contacts with the substrate, molecular docking, overview. Top substrate having favorable interactions with nitrile hydratase is 3-cyanopyridine
-
-
-
additional information
?
-
Rhodococcus erythropolis AJ270
P13448
molecular modeling study of enzyme-substrate binding modes in the bi-enzyme pathway for degradation of nitrile to acid, specific residues within the enzyme's binding pockets form diverse contacts with the substrate, molecular docking, overview. Top substrate having favorable interactions with nitrile hydratase is benzonitrile
-
-
-
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
COMMENTARY
LITERATURE
IMAGE
pyrroloquinoline quinone
-
prosthetic group, covalently bound pyrroloquinoline quinone, PQQ or a compound which closely resembles PQQ
pyrroloquinoline quinone
-
-
pyrroloquinoline quinone
Rhodococcus hoagii
-
-
pyrroloquinoline quinone
-
-
pyrroloquinoline quinone
-
-
pyrroloquinoline quinone
-
-
pyrroloquinoline quinone
-
-
METALS and IONS
ORGANISM
UNIPROT
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+
-
cobalt-containing nitrile hydratase; cobalt-containing nitrile hydratase
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
Co2+
-
Co-type NHase
Co2+
-
cobalt-containing nitrile hydratase, noncorrin cobalt at the catalytic center, structure, overview. Two cysteine residues (alphaCys111 and alphaCys113) coordinated to the cobalt are posttranslationally modified to cysteine-sulfinic acid and to cysteine-sulfenic acid, respectively; cobalt-containing nitrile hydratase, noncorrin cobalt at the catalytic center, structure, overview. Two cysteine residues (alphaCys111 and alphaCys113) coordinated to the cobalt are posttranslationally modified to cysteine-sulfinic acid and to cysteine-sulfenic acid, respectively
Co2+
B6CWJ3, B6CWJ4, B6CWJ5
the metal cofactor is located in the alpha-subunit at the interfacial active site of the heterodimeric enzyme; the metal cofactor is located in the alpha-subunit at the interfacial active site of the heterodimeric enzyme; the metal cofactor is located in the alpha-subunit at the interfacial active site of the heterodimeric enzyme
Co2+
-
Co-type NHase; Co-type NHase
Co2+
-
the enzyme is manganese-dependent, cobalt and nickel ions can substitute for it
Co2+
-
cobalt-dependent enzyme type
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
Fe2+
Q6XMT1, Q6XMT2, T1VWN1, T1VX74
Fe-type nitrile hydratase; Fe-type nitrile hydratase; Fe-type nitrile hydratase; Fe-type nitrile hydratase
Fe2+
P13448
Fe-type NHase
Fe2+
K9NKC3, K9NLN7
iron-type metalloenzyme; iron-type metalloenzyme
Fe2+
-
with cobalt substitution for iron, the enzyme activity becomes weak; with cobalt substitution for iron, the enzyme activity becomes weak
Fe2+
-
an FeIII-NHase with a non-heme iron center. Structure of NHase active site showing the FeIII coordination sphere and some conserved residues, overview
Fe2+
Rhodococcus hoagii
-
iron-type nitrile hydratase
Fe2+
A5W402
Fe-type NHase
Fe2+
-
iron-dependent enzyme type
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+
Rhodococcus hoagii
-
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
Mg2+
-
Mg2+ bound in chain B interacts with five water molecules and Asn49B
Na2MoO4
-
1 mM, relative activity: 102.1%
Ni2+
-
the enzyme is manganese-dependent, cobalt and nickel ions can substitute for it
Zn2+
-
component of enzyme, one ion per holoenzyme, ICP-MS
Mn2+
-
the enzyme is manganese-dependent, cobalt and nickel ions can substitute for it. One site binding model with Km = 0.8 mM
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
-
the apoenzyme shows no detectable activity, a disulfide bond between highly conserved Co-binding residues alphaCys108 and alphaCys113 is formed in the apoenzyme structure; the apoenzyme shows no detectable activity, a disulfide bond between highly conserved Co-binding residues alphaCys108 and alphaCys113 is formed in the apoenzyme structure
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
additional information
-
structure comparison with the Fe-type NHase, overview. In cobalt-containing nitrile hydratase, a tryptophan residue betaTrp72, which may be involved in substrate binding, replaces the tyrosine residue of iron-containing nitrile hydratase; structure comparison with the Fe-type NHase, overview. In cobalt-containing nitrile hydratase, a tryptophan residue betaTrp72, which may be involved in substrate binding, replaces the tyrosine residue of iron-containing nitrile hydratase
additional information
-
no activity with Fe2+
INHIBITORS
ORGANISM
UNIPROT
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
1-butaneboronic acid
-
competitive inhibitor, binds directly to the low-spin Co(III) ion in the active site of PtNHase; competitive inhibitor, binds directly to the low-spin Co(III) ion in the active site of PtNHase
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-aminotetrazole 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
-
-
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
Acrylamide
-
NHases exhibit low product acrylamide tolerance
acrylonitrile
-
above > 40 g/l
acrylonitrile
-
-
Adipamic acid
-
-
adipamide
-
-
Adipic 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
Benzoic acid
-
competitive inhibitor; competitive inhibitor
Butyric acid
-
-
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+
-
strong inhibition
Cu2+
-
85% inhibition at 10 mM
Cu2+
-
1 mM CuCl2
Cu2+
-
1-5 mM CuSO4
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
cysteamine
-
1 mM
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
-
weak
EDTA
-
strong inhibition
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+
-
strong inhibition
Hg2+
-
10 mM, 90% inhibition
Hg2+
-
HgCl2, 0.01-1 mM
Hg2+
-
HgCl2, 0.01-1 mM
Hg2+
-
HgCl2, 0.01-1 mM
hydrazine
-
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
-
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
-
; competitive inhibitor, the hydroxyl group of enzyme residue betaTyr68 forms hydrogen bonds with both n-butyric acid and residue alphaSer112, which is located in the active center. Butyric acid acts as a stabilizer of Fe-type NHase, Co-type NHase is more stable; competitive inhibitor, the hydroxyl group of enzyme residue betaTyr68 forms hydrogen bonds with both n-butyric acid and residue alphaSer112, which is located in the active center. Butyric acid acts as a stabilizer of Fe-type NHase, Co-type NHase is more stable
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
phenylboronic acid
-
competitive inhibitor, binds to the enzyme active site; competitive inhibitor, binds to the enzyme active site
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
Propionic acid
-
competitive inhibitor; competitive inhibitor
Semicarbazide
-
1 mM, 20 min at 15C
Semicarbazide
-
1 mM, weak inhibition
Semicarbazide
-
1 mM
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
-
additional information
-
the enzyme shows a high tolerance against acrylamide; the enzyme shows a high tolerance against acrylamide
-
additional information
-
product inhibition at high concentrations
-
additional information
-
enzyme-boronic acid complexes represent a snapshot of reaction intermediates; enzyme-boronic acid complexes represent a snapshot of reaction intermediates
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
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
-
NHase activator protein
A5W402
the activator gene encding activator protein might be involved in protein folding of the alpha- and beta-subunits of NHase
-
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
nitrile hydratase activator protein
-
residue aTyr114 may be involved in the interaction with the nitrile hydratase activator protein of Pseudomonas thermophila; residue aTyr114 may be involved in the interaction with the nitrile hydratase activator protein of Pseudomonas thermophila
-
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
-
additional information
K9NKC3, K9NLN7
the enzyme does not require the help of a P47K activator protein to be active; the enzyme does not require the help of a P47K activator protein to be active
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
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
0.12
3-Cyanopyridine
-
pH 7.6, 25C, recombinant wild-type enzyme; pH 7.6, 25C, recombinant wild-type 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
99
3-Cyanopyridine
B6CWJ3, B6CWJ4, B6CWJ5
pH 65, temperature not specified in the publication, recombinant trimeric enzyme; pH 65, temperature not specified in the publication, recombinant trimeric enzyme; pH 65, temperature not specified in the publication, recombinant trimeric enzyme
167
3-Cyanopyridine
-
in 0.1 M potassium phosphate buffer, pH 8.0, at 40C
200
3-Cyanopyridine
-
pH 7.0, 20C, H-NHase
1100
3-Cyanopyridine
B6CWJ3, B6CWJ4, B6CWJ5
pH 65, temperature not specified in the publication, recombinant monomeric alpha enzyme; pH 65, temperature not specified in the publication, recombinant monomeric alpha enzyme; pH 65, temperature not specified in the publication, recombinant monomeric alpha enzyme
0.079
4-cyanopyridine
-
pH 7.6, 25C, recombinant wild-type enzyme; pH 7.6, 25C, recombinant wild-type enzyme
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
-
-
1.89
acrylonitrile
-
pH 7.0, 20C, H-NHase
2.67
acrylonitrile
-
pH 7.0, 20C, L-NHase
3.6
acrylonitrile
-
pH 7.6, 25C, recombinant wild-type enzyme; pH 7.6, 25C, recombinant wild-type enzyme
6.4
acrylonitrile
-
+/- 0.3, 10 mM HEPES, pH 7.5, 37C
9.9
acrylonitrile
-
pH 7.6, 25C, recombinant mutant alphaY114T; pH 7.6, 25C, recombinant mutant alphaY114T
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
58
acrylonitrile
-
pH 7.6, 25C, recombinant mutant betaY68F; pH 7.6, 25C, recombinant mutant betaY68F
82
acrylonitrile
Q8GJG6, Q8GJG7
recombinant NHase with modified start codon only
86
acrylonitrile
Q8GJG6, Q8GJG7
wild type NHase
95
acrylonitrile
-
-
107
acrylonitrile
-
pH 7.6, 25C, recombinant mutant alphaT109S; pH 7.6, 25C, recombinant mutant alphaT109S
210
acrylonitrile
-
pH 7.5, 25C
30
adiponitrile
-
R312 strain
38
adiponitrile
-
ACV2 mutant
0.02
Benzonitrile
-
pH 7.6, 25C, recombinant wild-type enzyme; pH 7.6, 25C, recombinant wild-type enzyme
0.025
Benzonitrile
-
pH 7.6, 25C, recombinant mutant alphaT109S; pH 7.6, 25C, recombinant mutant alphaT109S
0.05
Benzonitrile
-
pH 7.0, 20C, L-NHase
0.11
Benzonitrile
-
pH 7.6, 25C, recombinant mutant alphaY114T; pH 7.6, 25C, recombinant mutant alphaY114T
0.23
Benzonitrile
-
pH 7.6, 25C, recombinant mutant betaY68F; pH 7.6, 25C, recombinant mutant betaY68F
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
0.49
Methacrylonitrile
-
pH 7.6, 25C, recombinant wild-type enzyme; pH 7.6, 25C, recombinant wild-type enzyme
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
2.3
Methacrylonitrile
-
pH 7.6, 25C, recombinant mutant alphaY114T; pH 7.6, 25C, recombinant mutant alphaY114T
2.6
Methacrylonitrile
-
pH 7.6, 25C, recombinant mutant betaY68F; pH 7.6, 25C, recombinant mutant betaY68F
2.6
Methacrylonitrile
-
mutant alphaQ90N, vmax: 57 micromol/min/mg
3.8
Methacrylonitrile
-
-
4.7
Methacrylonitrile
-
pH 7.6, 25C, recombinant mutant alphaT109S; pH 7.6, 25C, recombinant mutant alphaT109S
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
0.028
Toyocamycin
B6CWJ3, B6CWJ4, B6CWJ5
pH 65, temperature not specified in the publication, recombinant trimeric enzyme; pH 65, temperature not specified in the publication, recombinant trimeric enzyme; pH 65, temperature not specified in the publication, recombinant trimeric enzyme
15
Toyocamycin
B6CWJ3, B6CWJ4, B6CWJ5
pH 65, temperature not specified in the publication, recombinant monomeric alpha enzyme; pH 65, temperature not specified in the publication, recombinant monomeric alpha enzyme; pH 65, temperature not specified in the publication, recombinant monomeric alpha enzyme
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
-
the wild-type enzyme shows significantly lower Km values for aromatic substrates than for aliphatic ones; the wild-type enzyme shows significantly lower Km values for aromatic substrates than for aliphatic ones
-
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
-
additional information
additional information
B6CWJ3, B6CWJ4, B6CWJ5
comparisons of the steady state kinetic parameters of the single subunit variant to the heterotrimeric protein show that the additional subunits impart substrate specificity and catalytic efficiency; comparisons of the steady state kinetic parameters of the single subunit variant to the heterotrimeric protein show that the additional subunits impart substrate specificity and catalytic efficiency; comparisons of the steady state kinetic parameters of the single subunit variant to the heterotrimeric protein show that the additional subunits impart substrate specificity and catalytic efficiency
-
additional information
additional information
Rhodococcus hoagii
-
single turnover stopped-flow experiments and multiple turnover experiments with methacrylonitrile suggest a three-step kinetic model that allows for the reversible binding of substrate, the presence of an intermediate, and the formation of product, identification of catalytic Fe3+-nitrile intermediate species, kinetics, detaiiled overview
-
additional information
additional information
-
the enzymatic in vitro enzyme assay Michaelis-Menten kinetics does not give satisfactory results both for Km and for Vmax as saturation of the enzyme is not reached before the substrate aeroplysinin-1 precipitated at concentrations higher than 36 mM
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
443.3
2-Cyanopyridine
-
soluble NHase, at 50C
17.3
3-Cyanopyridine
-
EupergitC-immobilized NHase, at 50C
35
3-Cyanopyridine
B6CWJ3, B6CWJ4, B6CWJ5
pH 65, temperature not specified in the publication, recombinant monomeric alpha enzyme; pH 65, temperature not specified in the publication, recombinant monomeric alpha enzyme; pH 65, temperature not specified in the publication, recombinant monomeric alpha enzyme
79
3-Cyanopyridine
B6CWJ3, B6CWJ4, B6CWJ5
pH 65, temperature not specified in the publication, recombinant trimeric enzyme; pH 65, temperature not specified in the publication, recombinant trimeric enzyme; pH 65, temperature not specified in the publication, recombinant trimeric enzyme
131
3-Cyanopyridine
-
pH 7.6, 25C, recombinant wild-type enzyme; pH 7.6, 25C, recombinant wild-type enzyme
629.6
3-Cyanopyridine
-
soluble NHase, at 50C
59.05
4-cyanopyridine
-
soluble NHase, at 50C
90
4-cyanopyridine
-
pH 7.6, 25C, recombinant wild-type enzyme; pH 7.6, 25C, recombinant wild-type enzyme
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
15.2
acrylonitrile
-
pH 7.6, 25C, recombinant mutant betaY68F; pH 7.6, 25C, recombinant mutant betaY68F
33.9
acrylonitrile
-
pH 7.6, 25C, recombinant mutant alphaY114T; pH 7.6, 25C, recombinant mutant alphaY114T
621
acrylonitrile
-
pH 7.6, 25C, recombinant mutant alphaT109S; pH 7.6, 25C, recombinant mutant alphaT109S
1910
acrylonitrile
-
pH 7.6, 25C, recombinant wild-type enzyme; pH 7.6, 25C, recombinant wild-type enzyme
4.9
Benzonitrile
-
pH 7.6, 25C, recombinant mutant alphaY114T; pH 7.6, 25C, recombinant mutant alphaY114T
7.4
Benzonitrile
-
pH 7.6, 25C, recombinant mutant betaY68F; pH 7.6, 25C, recombinant mutant betaY68F
123
Benzonitrile
-
pH 7.6, 25C, recombinant wild-type enzyme; pH 7.6, 25C, recombinant wild-type enzyme
132
Benzonitrile
-
pH 7.6, 25C, recombinant mutant alphaT109S; pH 7.6, 25C, recombinant mutant alphaT109S
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
14.1
Methacrylonitrile
-
pH 7.6, 25C, recombinant mutant betaY68F; pH 7.6, 25C, recombinant mutant betaY68F
34.6
Methacrylonitrile
-
pH 7.6, 25C, recombinant mutant alphaY114T; pH 7.6, 25C, recombinant mutant alphaY114T
120
Methacrylonitrile
-
mutant betaR56K
482
Methacrylonitrile
-
pH 7.6, 25C, recombinant mutant alphaT109S; pH 7.6, 25C, recombinant mutant alphaT109S
1000
Methacrylonitrile
-
pH 7.6, 25C, recombinant wild-type enzyme; pH 7.6, 25C, recombinant wild-type enzyme
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
-
-
0.44
Toyocamycin
B6CWJ3, B6CWJ4, B6CWJ5
pH 65, temperature not specified in the publication, recombinant monomeric alpha enzyme; pH 65, temperature not specified in the publication, recombinant monomeric alpha enzyme; pH 65, temperature not specified in the publication, recombinant monomeric alpha enzyme
159
Toyocamycin
B6CWJ3, B6CWJ4, B6CWJ5
pH 65, temperature not specified in the publication, recombinant trimeric enzyme; pH 65, temperature not specified in the publication, recombinant trimeric enzyme; pH 65, temperature not specified in the publication, recombinant trimeric enzyme
76.3
Valeronitrile
-
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.032
3-Cyanopyridine
B6CWJ3, B6CWJ4, B6CWJ5
pH 65, temperature not specified in the publication, recombinant monomeric alpha enzyme; pH 65, temperature not specified in the publication, recombinant monomeric alpha enzyme; pH 65, temperature not specified in the publication, recombinant monomeric alpha enzyme
1784
0.8
3-Cyanopyridine
B6CWJ3, B6CWJ4, B6CWJ5
pH 65, temperature not specified in the publication, recombinant trimeric enzyme; pH 65, temperature not specified in the publication, recombinant trimeric enzyme; pH 65, temperature not specified in the publication, recombinant trimeric enzyme
1784
1090
3-Cyanopyridine
-
pH 7.6, 25C, recombinant wild-type enzyme; pH 7.6, 25C, recombinant wild-type enzyme
1784
1140
4-cyanopyridine
-
pH 7.6, 25C, recombinant wild-type enzyme; pH 7.6, 25C, recombinant wild-type enzyme
3975
0.26
acrylonitrile
-
pH 7.6, 25C, recombinant mutant betaY68F; pH 7.6, 25C, recombinant mutant betaY68F
1749
3.4
acrylonitrile
-
pH 7.6, 25C, recombinant mutant alphaY114T; pH 7.6, 25C, recombinant mutant alphaY114T
1749
5.8
acrylonitrile
-
pH 7.6, 25C, recombinant mutant alphaT109S; pH 7.6, 25C, recombinant mutant alphaT109S
1749
537
acrylonitrile
-
pH 7.6, 25C, recombinant wild-type enzyme; pH 7.6, 25C, recombinant wild-type enzyme
1749
32
Benzonitrile
-
pH 7.6, 25C, recombinant mutant betaY68F; pH 7.6, 25C, recombinant mutant betaY68F
1135
45
Benzonitrile
-
pH 7.6, 25C, recombinant mutant alphaY114T; pH 7.6, 25C, recombinant mutant alphaY114T
1135
5290
Benzonitrile
-
pH 7.6, 25C, recombinant mutant alphaT109S; pH 7.6, 25C, recombinant mutant alphaT109S
1135
6150
Benzonitrile
-
pH 7.6, 25C, recombinant wild-type enzyme; pH 7.6, 25C, recombinant wild-type enzyme
1135
5.4
Methacrylonitrile
-
pH 7.6, 25C, recombinant mutant betaY68F; pH 7.6, 25C, recombinant mutant betaY68F
2568
15
Methacrylonitrile
-
pH 7.6, 25C, recombinant mutant alphaY114T; pH 7.6, 25C, recombinant mutant alphaY114T
2568
103
Methacrylonitrile
-
pH 7.6, 25C, recombinant mutant alphaT109S; pH 7.6, 25C, recombinant mutant alphaT109S
2568
2040
Methacrylonitrile
-
pH 7.6, 25C, recombinant wild-type enzyme; pH 7.6, 25C, recombinant wild-type enzyme
2568
0.0002
n-valeronitrile
-
pH 6.7, 0C, recombinant mutant betaE56Q
2592
0.00045
n-valeronitrile
-
pH 6.7, 0C, recombinant mutant betaH147N
2592
0.00121
n-valeronitrile
-
pH 6.7, 0C, recombinant mutant betaH71F
2592
0.00122
n-valeronitrile
-
pH 6.7, 0C, recombinant mutant betaH71N
2592
0.002
n-valeronitrile
-
pH 6.7, 0C, recombinant mutant betaH71L
2592
0.0025
n-valeronitrile
-
pH 6.7, 0C, recombinant mutant alphaD164N
2592
0.014
n-valeronitrile
-
pH 6.7, 0C, recombinant mutant alphaE168Q
2592
0.0152
n-valeronitrile
-
pH 6.7, 0C, recombinant mutant betaY215F
2592
0.023
n-valeronitrile
-
pH 6.7, 0C, recombinant mutant alphaY171F
2592
0.032
n-valeronitrile
-
pH 6.7, 0C, recombinant mutant alphaR170N
2592
0.05
n-valeronitrile
-
pH 6.7, 0C, recombinant wild-type enzyme
2592
0.03
Toyocamycin
B6CWJ3, B6CWJ4, B6CWJ5
pH 65, temperature not specified in the publication, recombinant monomeric alpha enzyme; pH 65, temperature not specified in the publication, recombinant monomeric alpha enzyme; pH 65, temperature not specified in the publication, recombinant monomeric alpha enzyme
10797
5700
Toyocamycin
B6CWJ3, B6CWJ4, B6CWJ5
pH 65, temperature not specified in the publication, recombinant trimeric enzyme; pH 65, temperature not specified in the publication, recombinant trimeric enzyme; pH 65, temperature not specified in the publication, recombinant trimeric enzyme
10797
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0005
1-butaneboronic acid
-
pH 7.5, 25C; pH 7.5, 25C
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
0.033
Benzoic acid
-
pH 7.6, 25C, recombinant wild-type enzyme; pH 7.6, 25C, recombinant wild-type enzyme
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
2
N,N-Dimethylacetamide
-
ACV2 mutant; R312 strain
0.9
n-butyric acid
-
pH 7.2, 28C
1.3
n-butyric acid
-
pH 7.6, 25C, recombinant wild-type enzyme; pH 7.6, 25C, recombinant wild-type enzyme
0.13
NaCN
-
pH 7.5, 25C, non-competitive with acrylonitrile
0.003
NaNO2
-
+/- 0.0005, NilCo
0.00000004
phenylboronic acid
-
pH 7.5, 25C; pH 7.5, 25C
0.6
Propionamide
-
pH 7, 37C, mixed-type inhibitor
9.9
Propionic acid
-
pH 7.6, 25C, recombinant wild-type enzyme; pH 7.6, 25C, recombinant wild-type enzyme
0.004
tertiary-butyl isonitrile
-
+/- 0.001, NilCo
100
Thioacetamide
-
R312 strain
110
Thioacetamide
-
ACV2 mutant
8.4
Thiocyanate
-
pH 7, 37C, competitive inhibitor
0.015
KCN
-
pH 7, 30C
additional information
additional information
-
the wild-type enzyme shows significantly lower Ki values for aromatic inhibitors than for aliphatic ones; the wild-type enzyme shows significantly lower Ki values for aromatic inhibitors than for aliphatic ones
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
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]
ORGANISM
UNIPROT
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
-
cell extract supernatant containing recombinant His-tagged ELK-16 N-terminal fusion enzyme variant, pH 7.5, 20C
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
16.2
-
purified native enzyme, pH 7.8, 41C
20.6
-
acrylamide (100 g/l)
23.2
-
methacrylamide-induced enzyme activity, no activity in absence of methacrylamide
26.61
A5W402
purified recombinant enzyme, pH 8.0, 25C, substrate 3-cyanopyridine
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
109
-
cell extract supernatant containing recombinant His-tagged EAK-16 N-terminal fusion enzyme variant, pH 7.5, 20C
110
-
+/- 10, substrate: 5-cyanovaleric acid, NilCo
110
-
cell extract supernatant containing recombinant His-tagged wild-type enzyme, pH 7.5, 20C
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
372
-
purified recombinant His-tagged ELK-16 N-terminal fusion enzyme variant, pH 7.5, 20C
426
-
purified recombinant His-tagged EAK-16 N-terminal fusion enzyme variant, pH 7.5, 20C
429
-
purified recombinant His-tagged EAK-16 C-terminal fusion enzyme variant, pH 7.5, 20C
439
-
purified recombinant wild-type enzyme, pH 7.5, 20C
439
-
purified recombinant His-tagged wild-type enzyme, pH 7.5, 20C
483
-
purified recombinant chimeric mutant 3ABC, pH 7.5, 20C
485
-
purified enzyme
535
A5W402
purified recombinant enzyme, pH 8.0, 25C, substrate valeronitrile
553
A5W402
purified recombinant enzyme, pH 8.0, 25C, substrate 4-chlorobutyronitrile
614
-
purified recombinant chimeric mutant 3AB, pH 7.5, 20C
686
Mesorhizobium sp.
-
purified native enzyme from strain F28, substrate acrylonitrile
775
A5W402
purified recombinant enzyme, pH 8.0, 25C, substrate isobutyronitrile
829.5
-
purified protein
844
Rhodococcus hoagii
-
crude cell extract towards methacrylonitrile, in 50 mM Tris-HCl (pH 7.5)
860
-
partially purified enzyme
924
-
control, no inducer
941
A5W402
purified recombinant enzyme, pH 8.0, 25C, substrate acrylonitrile
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
Rhodococcus hoagii
-
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
additional information
-
thhe enzyme exhibits high activity; thhe enzyme exhibits high activity
pH OPTIMUM
ORGANISM
UNIPROT
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 - 8.5
Rhodococcus hoagii
-
-
6.5
B6CWJ3, B6CWJ4, B6CWJ5
assay at; assay at; assay at
6.7
-
assay at
6.9 - 7.2
-
NilFe, NilCo
7 - 7.2
-
-
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
Rhodococcus hoagii
-
assay at
7
Q7SID2, Q7SID3
assay at; assay at
7.2 - 7.8
-
-
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
7.5
Q6XMT1, Q6XMT2, T1VWN1, T1VX74
assay at; assay at; assay at; assay at
7.5
K9NKC3, K9NLN7
narrow optimum, about 20% of maximal activity at pH 7.0 and about 40% at pH 8.0, profile overview; narrow optimum, about 20% of maximal activity at pH 7.0 and about 40% at pH 8.0, profile overview
7.5
Q5XPL4, Q5XPL5
assay at; assay at
7.5
-
assay at; assay at
7.6
-
assay at; assay at
8
-
assay at, in vivo
8
-
assay at
8
-
the optimum nitrile hydratase activity is observed in the Tris-HCl buffer at a pH of 8.0
pH RANGE
ORGANISM
UNIPROT
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 - 10
A5W402
activity range, profile overview
6 - 8
-
-
6 - 8.3
-
about 50% of activity maximum at pH 6, about 35% of activity maximum at pH 8.3
6 - 8.5
-
H-NHase
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
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0
-
assay at
4
K9NKC3, K9NLN7
;
5
-
bioconversion in cells in a bioreactor
20
-
assay at
20
-
with propionitrile and acrylonitrile as substrates
20
-
H-NHase activity assay at
20
Q5XPL4, Q5XPL5
assay at; assay at
20
-
assay at
20
-
assay at; assay at
20
-
assay at
21
-
assay at
22
-
assay at room temperature
25
-
assay at; assay at
25
-
hydration of acrylonitrile
25
-
assay at, in vivo
25
-
assay at; assay at
25
Rhodococcus hoagii
-
assay at
28
-
assay at, in vivo in cells
28
Q7SID2, Q7SID3
assay at; assay at
30
-
substrate: 2,2-dimethylcyclopropanecarbonitrile
30
Rhodococcus hoagii
-
-
30
Q6XMT1, Q6XMT2, T1VWN1, T1VX74
assay at; assay at; assay at; assay at
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
additional information
-
the enzyme exhibits a high optimum temperature; the enzyme exhibits a high optimum temperature
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0 - 20
K9NKC3, K9NLN7
maximal activity at 4C, over 50% of maximal activity at temperatures of 10 to 20C, the activity decreases significantly as the temperature increases above 20C; maximal activity at 4C, over 50% of maximal activity at temperatures of 10 to 20C, the activity decreases significantly as the temperature increases above 20C
4 - 24
-
-
10 - 30
-
79% of activity maximum at 10C, 13% of activity maximum at 30C
10 - 45
A5W402
activity range, profile overview
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
additional information
K9NKC3, K9NLN7
maximal activity at 4C, over 50% of maximal activity at temperatures of 10 to 20C, the activity decreases significantly as the temperature increases above 20C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.2
-
polyacrylamide isoelectrofocusing
5.75
-
polyacrylamide isoelectrofocusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
K9NKC3, K9NLN7
optimum growth temperature of the bacterium is 25C to 30C, but it is able to grow at 4C
Manually annotated by BRENDA team
-
optimum growth temperature of the bacterium is 25C to 30C, but it is able to grow at 4C
-
Manually annotated by BRENDA team
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
K9NKC3, K9NLN7
optimum growth temperature of the bacterium is 25C to 30C, but it is able to grow at 4C
Manually annotated by BRENDA team
additional information
-
Rhodococcus erythropolis A4 does not show significant differences in the nitrile hydratase activity between cultures grown on NH4NO3, acetonitrile or acetamide as a sole nitrogen source, respectively
Manually annotated by BRENDA team
additional information
Rhodococcus erythropolis A4
-
Rhodococcus erythropolis A4 does not show significant differences in the nitrile hydratase activity between cultures grown on NH4NO3, acetonitrile or acetamide as a sole nitrogen source, respectively
-
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
additional information
-
optimum growth temperature of the bacterium is 25C to 30C, but it is able to grow at 4C
-
Manually annotated by BRENDA team
additional information
Mesorhizobium sp. BNC1
-
optimum growth temperature of strain F28 is 37C
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
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
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
52000
-
gel filtration
648425
52000
-
-
648436
54000
-
chromatography on Sephacryl S-400 and Sepharose CL-6B, alpha-beta form
648451
61400
-
-
648436
61400
-
gel filtration
648437
70000
-
N774 strain
648436
70000
-
gel filtration
648441
77000
-
gel filtration on Sephadex-G150
648432
80000
-
gradient gel electrophoresis
648429
80000
-
gel filtration
648435
84000
-
gel filtration
648443
85000
-
-
648427
85000
-
sedimentation equilibrium method
648432
86000
-
holoenzyme, native PAGE
703995
87000
-
gel filtration, HPLC
648432
90000 - 94000
-
-
648431
90000 - 94000
-
gel filtration on Cellulofine GCL-2000sf
648432
90000 - 94000
-
gel filtration
648436
90000