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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)
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
Styrene degradation
Microbial metabolism in diverse environments
Orthology
K01502  
aliphatic nitrilase
Genes
EBI: 
PLU: 
PAY: 
KPU: 
KPO: 
XNE: 
PAO: 
EBT: 
PPUN: 
PPUU: 
PST: 
PSB: 
PFN: 
PBA: 
PKC: 
PKB_3246(nita1) PKB_3594(nita3)
SWD: 
TTU: 
MMT: 
ADI: 
RSC: 
RSM: 
RSE: 
RPJ: 
REH: 
H16_A1956(h16_A1956)
CNC: 
BVI: 
BCJ: 
BCED: 
BXE: 
BXB: 
BPH: 
BPY: 
BGL: 
BGE: 
BGF: 
BGD: 
BYI: 
BPX: 
BUO: 
AXO: 
AXN: 
AXS: 
PNA: 
AAA: 
VAP: 
VPE: 
VPD: 
MPT: 
MMS: 
JAG: 
GJA_2887(nitA)
AZA: 
SCL: 
sce9002(nitA)
SCU: 
HOH: 
DTI: 
ARA: 
AVI: 
AGR: 
RLE: 
RLT: 
RLG: 
NGL: 
NGG: 
BJA: 
BJU: 
BRA: 
BRADO4539(nitA)
BBT: 
BBta_4766(nitA)
BRS: 
AOL: 
RPA: 
RPT: 
OCG: 
OCO: 
AZC: 
SNO: 
MEA: 
MCH: 
MRD: 
MPO: 
MOR: 
HMC: 
SIL: 
JAN: 
NPP: 
GOH: 
GDI: 
GDI_3743(nitA)
GDJ: 
GXY: 
GXL: 
APT: 
APW: 
APF: 
APU: 
APG: 
APQ: 
APX: 
APZ: 
APK: 
TMO: 
TMO_c0200(nitA)
MIT: 
MIR: 
MIA: 
MIE: 
MID: 
MSM: 
MSG: 
MSB: 
MSN: 
MSH: 
MRH: 
MMM: 
MLI: 
NFA: 
ROA: 
ARR: 
PDX: 
SESP: 
SYN: 
sll0784(merR)
SYZ: 
SYY: 
SYT: 
SYS: 
SYQ: 
SYJ: 
SYW: 
SYC: 
syc0701_d(merR)
SYD: 
SYP: 
SYNK: 
SYNR: 
AMR: 
CGC: 
DSL: 
CMP: 
LEP: 
PMG: 
FIN: 
 » show all
Taxonomy
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 (1992) 9000-7.
  Sequence
[up:Q02068]
Reference
2  [PMID:11380987]
  Authors
Pace HC, Brenner C.
  Title
The nitrilase superfamily: classification, structure and function.
  Journal
Genome. Biol. 2 (2001) REVIEWS0001.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
UM-BBD (Biocatalysis/Biodegradation Database): 
BRENDA, the Enzyme Database: 
CAS: 
395644-15-2

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