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Information on EC 4.2.1.84 - nitrile hydratase and Organism(s) Monosiga brevicollis and UniProt Accession A9V2C1

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EC Tree
     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.1 Hydro-lyases
                4.2.1.84 nitrile hydratase
IUBMB Comments
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.
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This record set is specific for:
Monosiga brevicollis
UNIPROT: A9V2C1
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The taxonomic range for the selected organisms is: Monosiga brevicollis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
nhase, nitrile hydratase, nilco, l-nhase, h-nhase, co-type nhase, cobalt-containing nitrile hydratase, fe-nhase, ctnhase, anhase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3-cyanopyridine hydratase
-
-
-
-
acrylonitrile hydratase
-
-
-
-
aliphatic nitrile hydratase
-
-
-
-
H-NHase
-
-
-
-
H-nitrilase
-
-
-
-
hydratase, nitrile
-
-
-
-
L-Nhase
-
-
-
-
L-nitrilase
-
-
-
-
NHase
-
-
-
-
NI1 NHase
-
-
-
-
nitrilase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C-O bond cleavage by elimination of water
-
-
-
-
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.
CAS REGISTRY NUMBER
COMMENTARY hide
82391-37-5
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acrylonitrile + H2O
acrylamide
show the reaction diagram
-
-
-
?
benzonitrile + H2O
benzamide
show the reaction diagram
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
the enzyme expressed in the presence of 0.25 mM CoCl2 contains about 1.8 equivalents of cobalt per homodimer while the enzyme expressed in the absence of CoCl2 contains 1.6 cobalt ions per homodimer
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
78
acrylonitrile
pH 7.0, 25°C
18
Benzonitrile
pH 7.0, 25°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
130
acrylonitrile
pH 7.0, 25°C
33
Benzonitrile
pH 7.0, 25°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.7
acrylonitrile
pH 7.0, 25°C
1.8
Benzonitrile
pH 7.0, 25°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
NHAAB_MONBE
496
0
55604
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
2 * 55000, SDS-PAGE
monomer
the two usually separated NHase subunits fused in one protein of the choanoflagellate Monosiga brevicollis
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
genomic organization and phylogenetic analysis, sequence comparison, overview
heterologously expressed in Escherichia coli. The resulting enzyme expressed as a single polypeptide with fused alpha- and beta-subunits linked by a seventeen-histidine region. The enzyme contains its full complement of Co(III) and is fully functional without the coexpression of an activator protein or Escherichia coli GroES/EL molecular chaperones
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Foerstner, K.U.; Doerks, T.; Muller, J.; Raes, J.; Bork, P.
A nitrile hydratase in the eukaryote Monosiga brevicollis
PLoS ONE
3
e3976
2008
Monosiga brevicollis (A9V2C1), Monosiga brevicollis
Manually annotated by BRENDA team
Martinez, S.; Yang, X.; Bennett, B.; Holz, R.C.
A cobalt-containing eukaryotic nitrile hydratase
Biochim. Biophys. Acta
1865
107-112
2017
Monosiga brevicollis (A9V2C1), Monosiga brevicollis
Manually annotated by BRENDA team