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Information on EC 1.1.1.78 - methylglyoxal reductase (NADH) for references in articles please use BRENDA:EC1.1.1.78Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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methylglyoxal reductase (NADH)
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(R)-lactaldehyde + NAD+ = methylglyoxal + NADH + H+
(R)-lactaldehyde + NAD+ = methylglyoxal + NADH + H+
similar enzyme with NADPH-requirement for methylglyoxal reduction, that is inactive with NAD+, NADH and NADP+
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(R)-lactaldehyde + NAD+ = methylglyoxal + NADH + H+
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methylglyoxal degradation VI
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(R)-lactaldehyde:NAD+ oxidoreductase
This mammalian enzyme differs from the yeast enzyme, EC 1.1.1.283, methylglyoxal reductase (NADPH-dependent), by its coenzyme requirement, reaction direction, and enantiomeric preference.
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D-lactaldehyde dehydrogenase
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dehydrogenase, D-lactaldehyde
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methylglyoxal reductase
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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acetaldehyde + NADH + H+
ethanol + NAD+
DL-glyceraldehyde + NAD+
?
glutaraldehyde + NADH
?
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-
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?
glyceraldehyde + NADH
glycerol + NAD+
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-
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?
glyoxal + NADH
glycolaldehyde + NAD+
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?
methylglyoxal + NADH
(R)-lactaldehyde + NAD+
methylglyoxal + NADPH
lactaldehyde + NADP+
methylglyoxal + NADPH + H+
(R)-lactataldehyde + NADP+
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?
phenylglyoxal + NADH
hydroxyphenylacetaldehyde + NAD+
additional information
?
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acetaldehyde + NADH + H+
ethanol + NAD+
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?
acetaldehyde + NADH + H+
ethanol + NAD+
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?
DL-glyceraldehyde + NAD+
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DL-glyceraldehyde + NAD+
?
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methylglyoxal + NADH
(R)-lactaldehyde + NAD+
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ir
methylglyoxal + NADH
(R)-lactaldehyde + NAD+
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?
methylglyoxal + NADH
(R)-lactaldehyde + NAD+
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?
methylglyoxal + NADH
(R)-lactaldehyde + NAD+
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r
methylglyoxal + NADH
(R)-lactaldehyde + NAD+
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?
methylglyoxal + NADPH
lactaldehyde + NADP+
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?
methylglyoxal + NADPH
lactaldehyde + NADP+
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phenylglyoxal + NADH
hydroxyphenylacetaldehyde + NAD+
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?
phenylglyoxal + NADH
hydroxyphenylacetaldehyde + NAD+
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?
additional information
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NADH better substrate than NADPH
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additional information
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enzyme utilizes both: NADH and NADPH
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additional information
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specific for lactaldehyde
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methylglyoxal + NADH
(R)-lactaldehyde + NAD+
methylglyoxal + NADPH
lactaldehyde + NADP+
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?
methylglyoxal + NADH
(R)-lactaldehyde + NAD+
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ir
methylglyoxal + NADH
(R)-lactaldehyde + NAD+
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?
methylglyoxal + NADH
(R)-lactaldehyde + NAD+
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?
methylglyoxal + NADH
(R)-lactaldehyde + NAD+
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r
methylglyoxal + NADH
(R)-lactaldehyde + NAD+
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?
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NADH
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NADH
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NADH better substrate than NADPH
NADH
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utilizes both NADPH and NADH
NADPH
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NADPH
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NADH better substrate than NADPH
NADPH
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utilizes both NADH and NADPH
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5,5'-dithiobis(2-nitrobenzoate)
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iodoacetate
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N-ethylmaleimide
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p-chloromercuribenzoate
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p-chloromercuribenzoate
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p-chloromercuribenzoate
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p-chloromercuribenzoate
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2-mercaptoethanol
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slight activation
dithiothreitol
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slight activation
glutathione
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slight activation
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0.013
DL-lactaldehyde
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additional information
additional information
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7
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similar enzyme with NADPH-requirement for methylglyoxal reduction, that is inactive with NAD+, NADH and NADP+
11
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in the oxidation of D-lactaldehyde, increase of reaction rate up to pH 11
6.5
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reduction of methylglyoxal
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4.5 - 9.5
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pH 4.5 and pH 9.5: about 50% of activity maximum
6 - 8
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pH 6.0 and pH 8.0: about 50% of activity maximum
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25 - 75
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25°C and 75°C: about 50% of activity maximum
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brenda
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brenda
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brenda
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brenda
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highest activity
brenda
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brenda
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brenda
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brenda
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brenda
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35000
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2 * 35000, SDS-PAGE
46000
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2 * 46000, SDS-PAGE
43000
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1 * 43000, SDS-PAGE
43000
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gel filtration, SDS-PAGE
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dimer
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2 * 46000, SDS-PAGE
dimer
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2 * 35000, SDS-PAGE
monomer
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1 * 43000, SDS-PAGE
monomer
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1 * 43000, SDS-PAGE
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4.5
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1 min, 40°C, 50% loss of activity
207971
6
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1 min, 40°C, stable
207971
8
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1 min, 40°C, stable
207971
11
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1 min, 40°C, 50% loss of activity 4
207971
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39
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3 min, 50% loss of activity
44
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80 s, 50% loss of activity
50
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40 s, 50% loss of activity
60
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35 s, 50% loss of activity
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A0A0L1HL75_9PLEO
351
37476
TrEMBL
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Tran-Din, K.; Gottschalk, G.
Formation of D(-)-1,2-propanediol and D(-)-lactate from glucose by Clostridium sphenoides under phosphate limitation
Arch. Microbiol.
142
87-92
1985
Clostridium sphenoides
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Ting, S.M.; Miller, O.N.; Sellinger, O.Z.
The metabolism of lactaldehyde: VII. The oxidation of D-lactaldehyde in rat liver
Biochim. Biophys. Acta
97
407-415
1965
Rattus norvegicus
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Ray, M.; Ray, S.
Purification and partial characterization of a methylglyoxal reductase from goat liver
Biochim. Biophys. Acta
802
119-127
1984
Capra hircus
brenda
Kato, H.; Miyauchi, Y.; Nishimura, T.; Liang, Z.Q.
Purification and partial characterization of NADH-dependent methylglyoxal-reducing enzyme from porcine liver
Agric. Biol. Chem.
52
2641-2642
1988
Sus scrofa
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brenda
Saikusa, T.; Rhee, H.; Watanabe, K.; Murata, K.; Kimura, A.
Metabolism of 2-oxoaldehydes in bacteria: purification and characterization of methylglyoxal reductase from Escherichia coli
Agric. Biol. Chem.
51
1893-1899
1987
Escherichia coli
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Chen, C.N.; Porubleva, L.; Shearer, G.; Svrakic, M.; Holden, L.G.; Dover, J.L.; Johnston, M.; Chitnis, P.R.; Kohl, D.H.
Associating protein activities with their genes: rapid identification of a gene encoding a methylglyoxal reductase in the yeast Saccharomyces cerevisiae
Yeast
20
545-554
2003
Saccharomyces cerevisiae
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