Entry
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
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
Genes
PMUD : NCTC8068_03333(odh)
ARJ : DOM24_00265 DOM24_03895
COM : CMT41_09325 CMT41_09330
PSY : PCNPT3_02670 PCNPT3_07190
RSC : RCFBP_20774 RCFBP_20776
AXX : ERS451415_04062(odh)
PIG : EGT29_20880 EGT29_21235
ACRA : BSY15_2487 BSY15_2488
VAP : Vapar_0420 Vapar_1485 Vapar_6050
VPD : VAPA_1c05000 VAPA_1c15770
VAM : C4F17_10965 C4F17_16570
AAK : AA2016_2193 AA2016_5625 AA2016_6453
AMIH : CO731_00337(odh_1) CO731_05356(odh_2) CO731_05401(odh_3)
AMIS : Amn_41390 Amn_pa01290
ANJ : AMD1_PA0045(odh) AMD1_PA0327(odh)
PHT : BLM14_16170 BLM14_27490
NKI : KW403_06385 KW403_18915
NRH : T8J41_07675 T8J41_22035
SMK : Sinme_3886 Sinme_6865
RHI : NGR_a00740 NGR_b03550
SINO : SS05631_a45530 SS05631_b51320
ESJ : SJ05684_a40760 SJ05684_b45290
ALF : CFBP5473_15110 CFBP5473_23920
NEN : NCHU2750_46460(odh) NCHU2750_55530(odh)
ABAW : D5400_06845 D5400_08020
BRO : BRAD285_5026 BRAD285_6496
BXN : I3J27_26410 I3J27_32565
AALM : LUX29_04765 LUX29_20630
YPAC : CEW88_03990 CEW88_18790
AHT : ANTHELSMS3_01768(odh)
DALK : DSCA_25840 DSCA_56040
SDP : NCTC12225_00601(odh)
SPIC : SAMEA4384060_0733(odh)
SSH : NCTC13712_02248(odh)
SSIM : SAMEA4384339_2129(odh)
SSTE : SAMEA4384403_2425(odh)
SHV : AAT16_01855 AAT16_04580 AAT16_10350
JEA : JEM45_08205 JEM45_09165
PKU : AUO94_08225 AUO94_14135
PFAE : AJGP001_03050 AJGP001_16835
PDEC : H1Q58_08115 H1Q58_12350
PANC : E2636_12305 E2636_15760
LCB : LCABL_04530(AGR_pAT_610)
JDA : BW727_101397(odh_1) BW727_101917(odh_2)
CRS : FQB35_01385 FQB35_02255 FQB35_03370 FQB35_03395 FQB35_14565
CPRF : K7H06_04865 K7H06_06220 K7H06_10295 K7H06_15035 K7H06_15900
RGV : NQ502_13845 NQ502_13935
ACOL : K5I23_05245 K5I23_13220
PETR : QKW49_07000 QKW49_20780
FWA : DCMF_01875 DCMF_04045 DCMF_26680
PROM : QO263_04525 QO263_18800
GFE : Gferi_04555 Gferi_15455
TEB : T8CH_0355(odh) T8CH_2851
GEK : kuro4_08130 kuro4_26110 kuro4_28280
KME : H0A61_00159(odh_1) H0A61_00204(odh_2)
PED : ING2D1G_0149 ING2D1G_1090 ING2D1G_1417
KPAR : JL105_06980 JL105_09105
NFR : ERS450000_02063(odh)
BRT : J4N02_07430 J4N02_09890
NAQU : ENKNEFLB_02180(odh)
ACO : Amico_1250 Amico_1803
TLI : Tlie_1504 Tlie_1506 Tlie_1711
PPIO : CE91St28_22620 CE91St28_22770
PYY : RAH42_11990 RAH42_12060
MPG : Theba_0163 Theba_0170
BARC : AOA65_0109 AOA65_0338
LOKI : Lokiarch_08200(odh)
» show all
Taxonomy
Reference
Authors
Asano Y, Yamaguchi K, Kondo K.
Title
A new NAD+-dependent opine dehydrogenase from Arthrobacter sp. strain 1C.
Journal
Reference
Authors
Dairi T, Asano Y
Title
Cloning, nucleotide sequencing, and expression of an opine dehydrogenase gene from Arthrobacter sp. strain 1C.
Journal
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 1:151-160 (1996)
Other DBs
ExplorEnz - The Enzyme Database: 1.5.1.28
ExPASy - ENZYME nomenclature database: 1.5.1.28
LinkDB
All DBs