We're sorry, but BRENDA doesn't work properly without JavaScript. Please make sure you have JavaScript enabled in your browser settings.
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments 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.
The enzyme appears in viruses and cellular organisms
Synonyms
mgr, methylglyoxal reductase, mgr ii, mgr i,
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
D-lactaldehyde dehydrogenase
-
-
-
dehydrogenase, D-lactaldehyde
-
-
-
methylglyoxal reductase
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(R)-lactaldehyde + NAD+ = 2-oxopropanal + NADH + H+
(R)-lactaldehyde + NAD+ = 2-oxopropanal + NADH + H+
similar enzyme with NADPH-requirement for methylglyoxal reduction, that is inactive with NAD+, NADH and NADP+
-
(R)-lactaldehyde + NAD+ = 2-oxopropanal + NADH + H+
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
acetaldehyde + NADH + H+
ethanol + NAD+
DL-glyceraldehyde + NAD+
?
glutaraldehyde + NADH
?
-
-
-
?
glyceraldehyde + NADH
glycerol + NAD+
-
-
-
?
glyoxal + NADH
glycolaldehyde + NAD+
-
-
-
?
methylglyoxal + NADH
(R)-lactaldehyde + NAD+
methylglyoxal + NADPH
lactaldehyde + NADP+
methylglyoxal + NADPH + H+
(R)-lactataldehyde + NADP+
-
-
-
?
phenylglyoxal + NADH
hydroxyphenylacetaldehyde + NAD+
additional information
?
-
acetaldehyde + NADH + H+
ethanol + NAD+
-
-
-
?
acetaldehyde + NADH + H+
ethanol + NAD+
-
-
-
?
DL-glyceraldehyde + NAD+
?
-
-
-
?
DL-glyceraldehyde + NAD+
?
-
-
-
?
methylglyoxal + NADH
(R)-lactaldehyde + NAD+
-
-
-
ir
methylglyoxal + NADH
(R)-lactaldehyde + NAD+
-
-
-
?
methylglyoxal + NADH
(R)-lactaldehyde + NAD+
-
-
-
?
methylglyoxal + NADH
(R)-lactaldehyde + NAD+
-
-
-
r
methylglyoxal + NADH
(R)-lactaldehyde + NAD+
-
-
-
?
methylglyoxal + NADPH
lactaldehyde + NADP+
-
-
-
?
methylglyoxal + NADPH
lactaldehyde + NADP+
-
-
-
?
phenylglyoxal + NADH
hydroxyphenylacetaldehyde + NAD+
-
-
-
?
phenylglyoxal + NADH
hydroxyphenylacetaldehyde + NAD+
-
-
-
?
additional information
?
-
-
NADH better substrate than NADPH
-
?
additional information
?
-
-
enzyme utilizes both: NADH and NADPH
-
?
additional information
?
-
-
specific for lactaldehyde
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
methylglyoxal + NADH
(R)-lactaldehyde + NAD+
methylglyoxal + NADPH
lactaldehyde + NADP+
-
-
-
?
methylglyoxal + NADH
(R)-lactaldehyde + NAD+
-
-
-
ir
methylglyoxal + NADH
(R)-lactaldehyde + NAD+
-
-
-
?
methylglyoxal + NADH
(R)-lactaldehyde + NAD+
-
-
-
?
methylglyoxal + NADH
(R)-lactaldehyde + NAD+
-
-
-
r
methylglyoxal + NADH
(R)-lactaldehyde + NAD+
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NADH
-
-
NADH
-
utilizes both NADPH and NADH
NADH
-
NADH better substrate than NADPH
NADPH
-
-
NADPH
-
NADH better substrate than NADPH
NADPH
-
utilizes both NADH and NADPH
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
5,5'-dithiobis(2-nitrobenzoate)
-
-
iodoacetate
-
-
N-ethylmaleimide
-
-
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2-mercaptoethanol
-
slight activation
dithiothreitol
-
slight activation
glutathione
-
slight activation
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.013
DL-lactaldehyde
-
-
additional information
additional information
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
11
-
in the oxidation of D-lactaldehyde, increase of reaction rate up to pH 11
7
-
similar enzyme with NADPH-requirement for methylglyoxal reduction, that is inactive with NAD+, NADH and NADP+
6.5
-
reduction of methylglyoxal
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
4.5 - 9.5
-
pH 4.5 and pH 9.5: about 50% of activity maximum
6 - 8
-
pH 6.0 and pH 8.0: about 50% of activity maximum
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
25 - 75
-
25°C and 75°C: about 50% of activity maximum
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
highest activity
brenda
-
-
brenda
-
-
brenda
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
A0A364N0B2_9PLEO
351
0
37476
TrEMBL
other Location (Reliability: 1 )
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
35000
-
2 * 35000, SDS-PAGE
46000
-
2 * 46000, SDS-PAGE
43000
-
gel filtration, SDS-PAGE
43000
-
1 * 43000, SDS-PAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
dimer
-
2 * 46000, SDS-PAGE
dimer
-
2 * 35000, SDS-PAGE
monomer
-
1 * 43000, SDS-PAGE
monomer
-
1 * 43000, SDS-PAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
11
-
1 min, 40°C, 50% loss of activity 4
207971
4.5
-
1 min, 40°C, 50% loss of activity
207971
6
-
1 min, 40°C, stable
207971
8
-
1 min, 40°C, stable
207971
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
39
-
3 min, 50% loss of activity
44
-
80 s, 50% loss of activity
50
-
40 s, 50% loss of activity
60
-
35 s, 50% loss of activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Lacrimispora sphenoides
-
brenda
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
brenda
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
-
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
-
brenda
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
brenda
Select items on the left to see more content.
html completed
HOME
login
history
all enzymes
BRENDA home
History
1.1.1.78 methylglyoxal reductase (NADH)
more
top
Information
