KEGG   ENZYME: 3.5.1.30Help
Entry
EC 3.5.1.30                 Enzyme                                 

Name
5-aminopentanamidase;
5-aminovaleramidase;
5-aminonorvaleramidase
Class
Hydrolases;
Acting on carbon-nitrogen bonds, other than peptide bonds;
In linear amides
BRITE hierarchy
Sysname
5-aminopentanamide amidohydrolase
Reaction(IUBMB)
5-aminopentanamide + H2O = 5-aminopentanoate + NH3 [RN:R02273]
Reaction(KEGG)
R02273;
(other) R06134
Show
Substrate
5-aminopentanamide [CPD:C00990];
H2O [CPD:C00001]
Product
5-aminopentanoate [CPD:C00431];
NH3 [CPD:C00014]
Comment
The enzyme from Pseudomonas putida also acts on 4-aminobutanamide and, more slowly, on 6-aminohexanamide.
History
EC 3.5.1.30 created 1972, modified 1976
Pathway
ec00310  Lysine degradation
ec01120  Microbial metabolism in diverse environments
Orthology
K01506  5-aminopentanamidase
Genes
SOD: Sant_4051
TCI: A7K98_01840
TPTY: NCTC11468_00451 NCTC11468_00452
PRE: PCA10_04890
PCQ: PcP3B5_32630(ramA_2)
PPU: PP_0382(davA)
PPF: Pput_0406
PPG: PputGB1_0410
PPW: PputW619_4821
PPT: PPS_0376
PPI: YSA_05768
PPX: T1E_2172
PPUH: B479_02385
PPUT: L483_01945
PPUN: PP4_04110
PPUD: DW66_0390
PMON: X969_00205
PMOT: X970_00205
PSB: Psyr_4668
PSYR: N018_02450
PFL: PFL_5671
PPRO: PPC_5616
PFS: PFLU_5596
PFB: VO64_2483
PMAN: OU5_4019
PEN: PSEEN0400
PSES: PSCI_1279
PSEM: TO66_28750
PSOS: POS17_5603
PANR: A7J50_5327
PSET: THL1_441
PSIL: PMA3_27690
GAI: IMCC3135_25890(ramA)
PLG: NCTC10937_04968(ramA_3)
HYB: Q5W_21185
DSF: UWK_01366
SCL: sce3848
SMER: DU99_13880
EAD: OV14_4057
RHT: NT26_3018
SHZ: shn_25135
SNO: Snov_1550
PLEO: OHA_1_02870(ramA_2) OHA_1_03066(ramA_3)
RBM: TEF_21380
RDE: RD1_1496
OTM: OSB_15800(ramA)
CID: P73_0078
SPSE: SULPSESMR1_04819(ramA)
ACR: Acry_0736
GXL: H845_1510
KEU: S101446_00641(nta1)
BMEG: BG04_5126
BCOA: BF29_1638
MVQ: MYVA_3178
MAB: MAB_0819
MABB: MASS_2857
ASD: AS9A_1375
RER: RER_05780
REY: O5Y_02760
ROP: ROP_33240
RHB: NY08_2003
RFA: A3L23_00335(ramA_1)
RHS: A3Q41_03072(ramA_3)
GOM: D7316_04815(ramA_3)
TPR: Tpau_1415
SCO: SCO1455(SCL6.12c)
SALB: XNR_5395
SGR: SGR_6069
SGB: WQO_05050
SCT: SCAT_5363
SFA: Sfla_5403
SHY: SHJG_2888
SVE: SVEN_1052
SALS: SLNWT_6480
STRP: F750_1216
SFI: SFUL_974
SALU: DC74_1909
SALL: SAZ_10125
STRE: GZL_07239
SLD: T261_6800
SPRI: SPRI_6107
SRW: TUE45_01868(ramA)
SLE: sle_56440(sle_56440)
SRN: A4G23_00702(ramA_1)
STRD: NI25_31930
SLAU: SLA_0955
SALJ: SMD11_5569
SLX: SLAV_30450(ramA)
SFK: KY5_1237c
ACH: Achl_1183
PSIM: KR76_13975
NDA: Ndas_3619
NAL: B005_0761
GOB: Gobs_1731
KRA: Krad_2723
AMD: AMED_6945
AMN: RAM_35630
AMM: AMES_6838
AMZ: B737_6838
AOI: AORI_4878
PSEA: WY02_17475
PSEE: FRP1_25150
CAI: Caci_8156
MEAR: Mpt1_c08000(amiF)
MARC: AR505_0376
 » show all
Taxonomy
Reference
1  [PMID:5432799]
  Authors
Reitz MS, Rodwell VW.
  Title
Delta-aminovaleramidase of Pseudomonas putida.
  Journal
J Biol Chem 245:3091-6 (1970)
Reference
2  [PMID:5772467]
  Authors
Takeda H, Yamamoto S, Kojima Y, Hayaishi O.
  Title
Studies on monooxygenases. I. General properties of crystalline L-lysine monooxygenase.
  Journal
J Biol Chem 244:2935-41 (1969)
Other DBs
ExplorEnz - The Enzyme Database: 3.5.1.30
IUBMB Enzyme Nomenclature: 3.5.1.30
ExPASy - ENZYME nomenclature database: 3.5.1.30
BRENDA, the Enzyme Database: 3.5.1.30
CAS: 9054-60-8

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