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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
ec00643  Styrene degradation
ec01120  Microbial metabolism in diverse environments
Orthology
K01502  aliphatic nitrilase
Genes
KPO: KPN2242_25871
KVQ: SP68_24535
GQU: AWC35_07540 AWC35_21755
EBT: EBL_c27840
RON: TE10_14560
BGJ: AWC36_03710
EBI: EbC_pEb17201250
PAO: Pat9b_4185 Pat9b_4750 Pat9b_4815
TCI: A7K98_09695 A7K98_12340
PLU: plu1231
XBV: XBW1_2736
XNE: XNC1_2121
XNM: XNC2_2050
XDO: XDD1_0585
PRG: RB151_005010(nitA)
PPSE: BN5_1632(merR1) BN5_1925
PPUN: PP4_48150
PSB: Psyr_0007
PKC: PKB_3246(nita1) PKB_3594(nita3)
PSIL: PMA3_12875
SWD: Swoo_0212
HAM: HALO0519
AXE: P40_07670
RSO: RSc1823
RSE: F504_1566
REH: H16_A1956(h16_A1956)
BVE: AK36_5522
BCJ: BCAL2585
BCED: DM42_6468
BXB: DR64_3321(nitA) DR64_3571
BHZ: ACR54_00880(nitA)
AXX: ERS451415_00457(nitA_1)
ODI: ODI_R1779
PNA: Pnap_2104
AAA: Acav_3339
MMS: mma_3076
JAG: GJA_2887(nitA)
AZA: AZKH_2480
SCL: sce9002(nitA)
HOH: Hoch_4751
AVI: Avi_7576
RLG: Rleg_0020
BJA: bll6402
BRA: BRADO4539(nitA)
BBT: BBta_4766(nitA)
AOL: S58_31930
BRAD: BF49_6424
BRO: BRAD285_4314(nitA)
RPA: RPA1563
RPT: Rpal_1751
AZC: AZC_0072
SNO: Snov_3713
MCH: Mchl_5393
MPO: Mpop_0056
MOR: MOC_3691
HDI: HDIA_3574(nitA)
SIL: SPOA0114
JAN: Jann_3735
RMM: ROSMUCSMR3_04023(nitA)
SPHP: LH20_08400
SMAZ: LH19_12410
GDI: GDI3743(nitA)
GDJ: Gdia_2619
GXY: GLX_30100
APK: APA386B_1P14(nitA)
ASZ: ASN_3201(nitA)
TMO: TMO_c0200(nitA)
MIT: OCO_40500
MIA: OCU_40410
MID: MIP_06104
MIR: OCQ_41590
MMM: W7S_20220
MVQ: MYVA_2107
NFA: NFA_32690
NFR: ERS450000_00807(nitA)
SALS: SLNWT_4233
SMAL: SMALA_8274
SLAU: SLA_0013
ARR: ARUE_c20300(nitA)
PSIM: KR76_04335
PDX: Psed_4247
SESP: BN6_40650
SYN: sll0784(merR)
SYZ: MYO_127800(merR)
SYY: SYNGTS_2754(merR)
SYT: SYNGTI_2753(merR)
SYS: SYNPCCN_2752(merR)
SYQ: SYNPCCP_2752(merR)
SYJ: D082_51050(merR)
SYW: SYNW1425
SYC: syc0701_d(merR)
SYNR: KR49_01065
LET: O77CONTIG1_03060(nitA)
AMR: AM1_2228
PLH: VT85_22105(nitA)
FIN: KQS_01640
 » 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
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: 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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