KEGG   ENZYME: 3.5.5.7Help
Entry
EC 3.5.5.7                  Enzyme                                 

Name aliphatic nitrilase
Class Hydrolases;
Acting on carbon-nitrogen bonds, other than peptide bonds;
In nitriles
BRITE hierarchy
Sysname aliphatic nitrile aminohydrolase
Reaction(IUBMB) R-CN + 2 H2O = R-COOH + NH3 [RN:R00540]
Reaction(KEGG) R00540 > R05358
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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.
Pathway PATH: ec00643  Styrene degradation
Orthology KO: K01502  aliphatic nitrilase
Genes PLU: plu1231
PAY: PAU_02090 PAU_03235
PST: PSPTO_0189
PSB: Psyr_0007
REH: H16_A1956
BVI: Bcep1808_6052
BXE: Bxe_A1162 Bxe_A1408
PNA: Pnap_2104
MPT: Mpe_A0993 Mpe_A3478
RLE: RL0660 pRL80076
BJA: bll6402
BRA: BRADO4539(nitA)
BBT: BBta_4766(nitA)
RPA: RPA1563
SIL: SPOA0114
GDI: GDI_3743(nitA)
MSM: MSMEG_4138
NFA: nfa32690
SYN: sll0784(merR)
SYW: SYNW1425
SYC: syc0701_d(merR)
SYD: Syncc9605_1108
SYP: SYNPCC7002_A0664
PMG: P9301_13131
Taxonomy
Reference
  Authors
  Title


  Journal
  Organism
1  [PMID:1390687]
Kobayashi M, Yanaka N, Nagasawa T, Yamada H.
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.
Biochemistry. 31 (1992) 9000-7.
Rhodococcus rhodochrous
Reference
  Authors
  Title
  Journal
2  [PMID:11380987]
Pace HC, Brenner C.
The nitrilase superfamily: classification, structure and function.
Genome. Biol. 2 (2001) 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

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