KEGG   ENZYME: 1.5.1.28Help
Entry
EC 1.5.1.28                 Enzyme                                 

Name
opine dehydrogenase;
(2S)-2-{[1-(R)-carboxyethyl]amino}pentanoate dehydrogenase (NAD+, L-aminopentanoate-forming)
Class
Oxidoreductases;
Acting on the CH-NH group of donors;
With NAD+ or NADP+ as acceptor
BRITE hierarchy
Sysname
(2S)-2-{[1-(R)-carboxyethyl]amino}pentanoate:NAD+ oxidoreductase (L-aminopentanoate-forming)
Reaction(IUBMB)
(2S)-2-{[1-(R)-carboxyethyl]amino}pentanoate + NAD+ + H2O = L-2-aminopentanoic acid + pyruvate + NADH + H+ [RN:R03732]
Reaction(KEGG)
Substrate
(2S)-2-{[1-(R)-carboxyethyl]amino}pentanoate [CPD:C06326];
NAD+ [CPD:C00003];
H2O [CPD:C00001]
Product
L-2-aminopentanoic acid [CPD:C01826];
pyruvate [CPD:C00022];
NADH [CPD:C00004];
H+ [CPD:C00080]
Comment
In the forward direction, the enzyme from Arthrobacter sp. acts also on secondary amine dicarboxylates such as N-(1-carboxyethyl)methionine and N-(1-carboxyethyl)phenylalanine. Dehydrogenation forms an imine, which dissociates to the amino acid and pyruvate. In the reverse direction, the enzyme acts also on neutral amino acids as an amino donor. They include L-amino acids such as 2-aminopentanoic acid, 2-aminobutyric acid, 2-aminohexanoic acid, 3-chloroalanine, O-acetylserine, methionine, isoleucine, valine, phenylalanine, leucine and alanine. The amino acceptors include 2-oxoacids such as pyruvate, oxaloacetate, glyoxylate and 2-oxobutyrate.
History
EC 1.5.1.28 created 1999
Orthology
K04940  
opine dehydrogenase
Genes
KPY: 
DDA: 
PPR: 
PGB: 
PPJ: 
PSW: 
COM: 
PSY: 
LLO: 
HAK: 
ASR: 
BTE: 
BTQ: 
BTJ: 
BTZ: 
BTV: 
BTHE: 
BTHM: 
BTHA: 
BTHL: 
BOK: 
BOC: 
BUR: 
BCN: 
BCH: 
BCM: 
BCJ: 
BCEN: 
BCEO: 
BAM: 
BAC: 
BMU: 
BMK: 
BMUL: 
BCED: 
BPYR: 
BCON: 
BCAI: 
AXY: 
AXO: 
AXN: 
AXS: 
AFA: 
ACK: 
VEI: 
VAP: 
VPE: 
VPD: 
LIM: 
MNR: 
GLO: 
DRT: 
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ATF: 
ATA: 
RIR: 
SHZ: 
BJA: 
BJU: 
BJP: 
BRA: 
BBT: 
BRS: 
AOL: 
BRC: 
BOP: 
CHEL: 
MEY: 
SIL: 
RDE: 
RLI: 
OAT: 
SWI: 
BCER: 
AXL: 
LAO: 
SAU: 
SAV: 
SAW: 
SAH: 
SAJ: 
SAM: 
SAS: 
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SAC: 
SAX: 
SAA: 
SAO: 
SAE: 
SAD: 
SUU: 
SUV: 
SUE: 
SUJ: 
SUK: 
SUC: 
SUT: 
SUQ: 
SUZ: 
SUD: 
SUX: 
SUW: 
SUG: 
SUF: 
SAUA: 
SAUE: 
SAUN: 
SAUS: 
SAUU: 
SAUG: 
SAUZ: 
SAUT: 
SAUJ: 
SAUK: 
SAUQ: 
SAUV: 
SAUW: 
SAUX: 
SAUY: 
SAB: 
SUY: 
SAUB: 
SAUM: 
SAUC: 
SAUR: 
SAUI: 
SAUD: 
SAUF: 
SUH: 
SEP: 
SER: 
SEPP: 
SEPS: 
SHH: 
SSP: 
SCA: 
SLG: 
SLN: 
SDT: 
SWA: 
SPAS: 
SXY: 
SXL: 
SXO: 
SHU: 
SCAP: 
SSCH: 
SAGQ: 
SEQO: 
SHV: 
PSAB: 
PBJ: 
PKU: 
PRT: 
LFF: 
LRG: 
AVS: 
AMT: 
RAL: 
HSD: 
STH: 
DDL: 
TJR: 
DOR: 
ELM: 
AWO: 
TMR: 
TTE: 
TEX: 
THX: 
TPD: 
TIT: 
TMT: 
TBO: 
TWI: 
TKI: 
TEP: 
TAE: 
TOC: 
TTM: 
TTO: 
TXY: 
TSH: 
MAS: 
HOR: 
AAR: 
PED: 
AIN: 
ERH: 
ERS: 
LPIL: 
NFA: 
NBR: 
GOR: 
GOQ: 
SRC: 
MIO: 
BCV: 
MPH: 
CEP: 
RRS: 
RCA: 
ATM: 
STR: 
ACO: 
TLI: 
AMO: 
TLE: 
TTA: 
PHY: 
TME: 
TAF: 
FPE: 
PMO: 
DTN: 
KOL: 
KPF: 
MPG: 
LOKI: 
BARC: 
 » show all
Taxonomy
Reference
1  [PMID:2753861]
  Authors
Asano Y, Yamaguchi K, Kondo K.
  Title
A new NAD+-dependent opine dehydrogenase from Arthrobacter sp. strain 1C.
  Journal
J. Bacteriol. 171 (1989) 4466-71.
Reference
2  [PMID:7487048]
  Authors
Dairi T, Asano Y.
  Title
Cloning, nucleotide sequencing, and expression of an opine dehydrogenase gene from Arthrobacter sp. strain 1C.
  Journal
Appl. Environ. Microbiol. 61 (1995) 3169-71.
  Sequence
Reference
3
  Authors
Kato, Y., Yamada, H. and Asano, Y.
  Title
Stereoselective synthesis of opine-type secondary amine carboxylic acids by a new enzyme opine dehydrogenase. Use of recombinant enzymes.
  Journal
J. Mol. Catal., B Enzym. 1 (1996) 151-160.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
108281-02-3

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