KEGG   ENZYME: 1.1.1.283Help
Entry
EC 1.1.1.283                Enzyme                                 

Name
methylglyoxal reductase (NADPH);
lactaldehyde dehydrogenase (NADP+);
GRE2 (gene name);
methylglyoxal reductase (NADPH-dependent);
lactaldehyde:NADP+ oxidoreductase
Class
Oxidoreductases;
Acting on the CH-OH group of donors;
With NAD+ or NADP+ as acceptor
BRITE hierarchy
Sysname
(S)-lactaldehyde:NADP+ oxidoreductase
Reaction(IUBMB)
(S)-lactaldehyde + NADP+ = 2-oxopropanal + NADPH + H+ [RN:R02260]
Reaction(KEGG)
Substrate
(S)-lactaldehyde [CPD:C00424];
NADP+ [CPD:C00006]
Product
2-oxopropanal [CPD:C00546];
NADPH [CPD:C00005];
H+ [CPD:C00080]
Comment
The enzyme from the yeast Saccharomyces cerevisiae catalyses the reduction of a keto group in a number of compounds, forming enantiopure products. Among the substrates are methylglyoxal (which is reduced to (S)-lactaldehyde) [1,2], 3-methylbutanal [3], hexane-2,5-dione [4] and 3-chloro-1-phenylpropan-1-one [5]. The enzyme differs from EC 1.1.1.78, methylglyoxal reductase (NADH), which is found in mammals, by its coenzyme requirement, reaction direction, and enantiomeric preference.
History
EC 1.1.1.283 created 2005, modified 2013
Pathway
Pyruvate metabolism
Propanoate metabolism
Orthology
K17741  
NADPH-dependent methylglyoxal reductase
Genes
SCE: 
YOL151W(GRE2)
LTH: 
VPO: 
ZRO: 
CGR: 
NCS: 
NCAS_0A03090(NCAS0A03090) NCAS_0A07210(NCAS0A07210) NCAS_0C05270(NCAS0C05270) NCAS_0C05980(NCAS0C05980) NCAS_0D02420(NCAS0D02420) NCAS_0D04850(NCAS0D04850) NCAS_0G03820(NCAS0G03820) NCAS_0H00790(NCAS0H00790)
NDI: 
NDAI_0D00910(NDAI0D00910) NDAI_0D05090(NDAI0D05090) NDAI_0F01560(NDAI0F01560) NDAI_0I02450(NDAI0I02450)
TPF: 
TPHA_0A00590(TPHA0A00590) TPHA_0F03690(TPHA0F03690) TPHA_0M01160(TPHA0M01160) TPHA_0N01940(TPHA0N01940) TPHA_0O00640(TPHA0O00640)
TBL: 
TBLA_0A01590(TBLA0A01590) TBLA_0C00270(TBLA0C00270) TBLA_0C00280(TBLA0C00280) TBLA_0C03420(TBLA0C03420) TBLA_0C03430(TBLA0C03430) TBLA_0D00750(TBLA0D00750)
TDL: 
TDEL_0C00230(TDEL0C00230) TDEL_0C02800(TDEL0C02800) TDEL_0D00270(TDEL0D00270)
KAF: 
KAFR_0A08710(KAFR0A08710) KAFR_0A08720(KAFR0A08720) KAFR_0C00150(KAFR0C00150)
PPA: 
DHA: 
PIC: 
PGU: 
SPAA: 
LEL: 
CAL: 
CaO19.11785(GRE22) CaO19.13054(GRE21) CaO19.4309(GRE22) CaO19.5611(GRE21)
CTP: 
COT: 
CDU: 
CTEN: 
CLU: 
 » show all
Taxonomy
Reference
1  [PMID:3896793]
  Authors
Murata K, Fukuda Y, Simosaka M, Watanabe K, Saikusa T, Kimura A.
  Title
Metabolism of 2-oxoaldehyde in yeasts. Purification and characterization of NADPH-dependent methylglyoxal-reducing enzyme from Saccharomyces cerevisiae.
  Journal
Eur. J. Biochem. 151 (1985) 631-6.
  Sequence
[sce:YOL151W]
Reference
2  [PMID:12722185]
  Authors
Chen CN, Porubleva L, Shearer G, Svrakic M, Holden LG, Dover JL, Johnston M, Chitnis PR, Kohl DH.
  Title
Associating protein activities with their genes: rapid identification of a gene encoding a methylglyoxal reductase in the yeast Saccharomyces cerevisiae.
  Journal
Yeast. 20 (2003) 545-54.
  Sequence
[sce:YOL151W]
Reference
3  [PMID:16999827]
  Authors
Hauser M, Horn P, Tournu H, Hauser NC, Hoheisel JD, Brown AJ, Dickinson JR
  Title
A transcriptome analysis of isoamyl alcohol-induced filamentation in yeast reveals a novel role for Gre2p as isovaleraldehyde reductase.
  Journal
FEMS. Yeast. Res. 7 (2007) 84-92.
  Sequence
[sce:YOL151W]
Reference
4  [PMID:20237665]
  Authors
Muller M, Katzberg M, Bertau M, Hummel W
  Title
Highly efficient and stereoselective biosynthesis of (2S,5S)-hexanediol with a dehydrogenase from Saccharomyces cerevisiae.
  Journal
Org. Biomol. Chem. 8 (2010) 1540-50.
  Sequence
[sce:YOL151W]
Reference
5  [PMID:20111861]
  Authors
Choi YH, Choi HJ, Kim D, Uhm KN, Kim HK
  Title
Asymmetric synthesis of (S)-3-chloro-1-phenyl-1-propanol using Saccharomyces cerevisiae reductase with high enantioselectivity.
  Journal
Appl. Microbiol. Biotechnol. 87 (2010) 185-93.
  Sequence
[sce:YOL151W]
Reference
6  [PMID:20606287]
  Authors
Breicha K, Muller M, Hummel W, Niefind K
  Title
Crystallization and preliminary crystallographic analysis of Gre2p, an NADP(+)-dependent alcohol dehydrogenase from Saccharomyces cerevisiae.
  Journal
Acta. Crystallogr. Sect. F. Struct. Biol. Cryst. Commun. 66 (2010) 838-41.
  Sequence
[sce:YOL151W]
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
78310-66-4

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