KEGG   ORTHOLOGY: K01502
Entry
K01502            Tight     KO                                     

Name
E3.5.5.7
Definition
aliphatic nitrilase [EC:3.5.5.7]
Pathway
ko00643  Styrene degradation
ko01120  Microbial metabolism in diverse environments
Brite
KEGG Orthology (KO) [BR:ko00001]
 09100 Metabolism
  09111 Xenobiotics biodegradation and metabolism
   00643 Styrene degradation
    K01502  E3.5.5.7; aliphatic nitrilase
Enzymes [BR:ko01000]
 3. Hydrolases
  3.5  Acting on carbon-nitrogen bonds, other than peptide bonds
   3.5.5  In nitriles
    3.5.5.7  aliphatic nitrilase
     K01502  E3.5.5.7; aliphatic nitrilase
Other DBs
RN: R05358
COG: COG0388
GO: 0018762
Genes
AG: BAA02127
Reference
PMID:1390687
  Authors
Kobayashi M, Yanaka N, Nagasawa T, Yamada H
  Title
Primary structure of an aliphatic nitrile-degrading enzyme, aliphatic nitrilase, from Rhodococcus rhodochrous K22 and expression of its gene and identification of its active site residue.
  Journal
Biochemistry 31:9000-7 (1992)
DOI:10.1021/bi00152a042
  Sequence
LinkDB

KEGG   ENZYME: 3.5.5.7
Entry
EC 3.5.5.7                  Enzyme                                 

Name
aliphatic nitrilase
Class
Hydrolases;
Acting on carbon-nitrogen bonds, other than peptide bonds;
In nitriles
Sysname
aliphatic nitrile aminohydrolase
Reaction(IUBMB)
R-CN + 2 H2O = R-COOH + NH3 [RN:R00540]
Reaction(KEGG)
R00540 > R05358
Substrate
R-CN [CPD:C00726];
H2O [CPD:C00001]
Product
R-COOH [CPD:C00060];
NH3 [CPD:C00014]
Comment
Preferentially hydrolyses aliphatic nitriles, some of which are apparently not substrates for other known nitrilases (EC 3.5.5.1). Substrates include crotononitrile, acrylonitrile and glutaronitrile.
History
EC 3.5.5.7 created 1999
Pathway
ec00643  Styrene degradation
ec01120  Microbial metabolism in diverse environments
Orthology
K01502  aliphatic nitrilase
Reference
1  [PMID:1390687]
  Authors
Kobayashi M, Yanaka N, Nagasawa T, Yamada H
  Title
Primary structure of an aliphatic nitrile-degrading enzyme, aliphatic nitrilase, from Rhodococcus rhodochrous K22 and expression of its gene and identification of its active site residue.
  Journal
Biochemistry 31:9000-7 (1992)
DOI:10.1021/bi00152a042
  Sequence
Reference
2  [PMID:11380987]
  Authors
Pace HC, Brenner C.
  Title
The nitrilase superfamily: classification, structure and function.
  Journal
Genome Biol 2:REVIEWS0001 (2001)
DOI:10.1186/gb-2001-2-1-reviews0001
Other DBs
ExplorEnz - The Enzyme Database: 3.5.5.7
IUBMB Enzyme Nomenclature: 3.5.5.7
ExPASy - ENZYME nomenclature database: 3.5.5.7
UM-BBD (Biocatalysis/Biodegradation Database): 3.5.5.7
BRENDA, the Enzyme Database: 3.5.5.7
CAS: 395644-15-2
LinkDB

KEGG   REACTION: R05358
Entry
R05358                      Reaction                               

Name
Acrylonitrile aminohydrolase
Definition
Acrylonitrile + 2 H2O <=> Acrylic acid + Ammonia
Equation
Reaction class
RC01336  C00511_C01998
Enzyme
Pathway
rn00643  Styrene degradation
rn01120  Microbial metabolism in diverse environments
Orthology
K01502  aliphatic nitrilase [EC:3.5.5.7]
LinkDB

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