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 enzyme, which was characterized from the methanogenic archaeon Methanobacterium thermoautotrophicum, catalyses only the reduction of oxaloacetate, and can use NAD+ and NADP+ with similar specific activity .
Different from EC 1.1.1.37 (malate dehydrogenase (NAD+)), EC 1.1.1.82 (malate dehydrogenase (NADP+)) and EC 1.1.5.4 (malate dehydrogenase (quinone)).
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
MDH II,
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MDH II
-
uses both NADP+ and NAD+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(S)-malate + NAD(P)+ = oxaloacetate + NAD(P)H + H+
(S)-malate + NAD(P)+ = oxaloacetate + NAD(P)H + H+
-
-
-
-
(S)-malate + NAD(P)+ = oxaloacetate + NAD(P)H + H+
ordered bi-bi mechanism
-
(S)-malate + NAD(P)+ = oxaloacetate + NAD(P)H + H+
ordered bi-bi mechanism
-
-
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.
(S)-malate:NAD(P)+ oxidoreductase
This enzyme, which was characterized from the methanogenic archaeon Methanobacterium thermoautotrophicum, catalyses only the reduction of oxaloacetate, and can use NAD+ and NADP+ with similar specific activity [1].
Different from EC 1.1.1.37 (malate dehydrogenase (NAD+)), EC 1.1.1.82 (malate dehydrogenase (NADP+)) and EC 1.1.5.4 (malate dehydrogenase (quinone)).
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
9001-64-3
cf. EC 1.1.1.37
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(S)-malate + NAD+
oxaloacetate + NADH + H+
(S)-malate + NADP+
oxaloacetate + NADPH + H+
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
?
oxaloacetate + NADH + H+
L-malate + NAD+
-
-
-
-
?
oxaloacetate + NADPH
L-malate + NADP+
-
-
-
-
?
additional information
?
-
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
?
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
?
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
?
(S)-malate + NADP+
oxaloacetate + NADPH + H+
-
-
-
-
?
(S)-malate + NADP+
oxaloacetate + NADPH + H+
-
-
-
-
?
(S)-malate + NADP+
oxaloacetate + NADPH + H+
-
-
-
-
?
additional information
?
-
-
enzyme shows pro-R stereospecificity for hydrogen transfer at the C4 position of the nicotinamide moiety of the coenzyme. No substrates are: D-malate, malonate, L-glutamate, L-aspartate, D,L-2-hydroxybutanoate, D,L-3-hydroxybutanoate, citrate, maleate, succinate, L-tartrate, L-threonine, L-serine, L-hydroxymalonate, D-glutamate, 2-oxocaproate, 2-oxoisovalerate, glyoxylate, 2-oxoglutarate, 2-oxobutanoate
-
-
-
additional information
?
-
-
enzyme shows pro-R stereospecificity for hydrogen transfer at the C4 position of the nicotinamide moiety of the coenzyme. No substrates are: D-malate, malonate, L-glutamate, L-aspartate, D,L-2-hydroxybutanoate, D,L-3-hydroxybutanoate, citrate, maleate, succinate, L-tartrate, L-threonine, L-serine, L-hydroxymalonate, D-glutamate, 2-oxocaproate, 2-oxoisovalerate, glyoxylate, 2-oxoglutarate, 2-oxobutanoate
-
-
-
additional information
?
-
-
no substrate: pyruvate
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
additional information
-
no cofactor: NADPH
-
NAD+
-
relative activity of NAD+ to NADP+ is 43.9%
NADH
-
-
NADP+
-
relative activity of NAD+ to NADP+ is 43.9%
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CuCl2
-
1 mM, 10% residual activity
HgCl2
-
1 mM, no residual activity
iodoacetate
-
1 mM, 16.4% residual activity
N-ethylmaleimide
-
1 mM, no residual activity
NADH
-
inhibitory above 0.2 mM
NADPH
-
inhibitory above 0.2 mM
ZnCl2
-
1 mM, 27% residual activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.09
oxaloacetate
-
pH 7.6
0.269
L-malate
-
20°C
0.028
NAD+
-
10°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
41.3
L-malate
-
10°C
41
NAD+
-
10°C
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.
1
-
pH 7.6, oxidation of malate, cosubstrate NAD+; pH 7.6, oxidation of malate, cosubstrate NADP+
52
-
pH 7.6, reduction of oxaloacetate, cosubstrate NADP+
60
-
pH 7.6, reduction of oxaloacetate, cosubstrate NAD+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
10.5
-
oxidation of malate
8
-
reduction of oxaloacetate
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
4 - 10
-
reduction of oxaloacetate
6.5 - 12
-
oxidation of malate
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
40
-
highest initial velocity
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.
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MDH_METKA
Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)
317
0
34609
Swiss-Prot
MDH_METMP
Methanococcus maripaludis (strain S2 / LL)
314
0
34468
Swiss-Prot
MDH_METST
Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3)
317
0
34857
Swiss-Prot
MDH_METTH
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
325
0
35933
Swiss-Prot
MDH_METTM
Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg)
325
0
35860
Swiss-Prot
MDH_AERPE
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
308
0
33490
Swiss-Prot
A0A5J4DRU1_9ARCH
304
0
32730
TrEMBL
A0A5J4DUJ1_9ARCH
269
0
29178
TrEMBL
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
32000
-
4 * 32000, SDS-PAGE
36000
-
x * 36000, SDS-PAGE, x * 36700, calculated
36700
-
x * 36000, SDS-PAGE, x * 36700, calculated
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
?
-
x * 36000, SDS-PAGE, x * 36700, calculated
tetramer
-
4 * 32000, SDS-PAGE
tetramer
-
4 * 32000, SDS-PAGE
-
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.
Oikawa, T.; Yamamoto, N.; Shimoke, K.; Uesato, S.; Ikeuchi, T.; Fujioka, T.
Purification, characterization, and overexpression of psychrophilic and thermolabile malate dehydrogenase of a novel antarctic psychrotolerant, Flavobacterium frigidimaris KUC-1
Biosci. Biotechnol. Biochem.
69
2146-2154
2005
Flavobacterium frigidimaris, Flavobacterium frigidimaris KUC-1
brenda
Thompson, H.; Tersteegen, A.; Thauer, R.; Hedderich, R.
Two malate dehydrogenases in Methanobacterium thermoautotrophicum
Arch. Microbiol.
170
38-42
1998
Methanothermobacter thermautotrophicus
brenda
Select items on the left to see more content.
html completed
HOME
login
history
all enzymes
BRENDA home
History
1.1.1.299 malate dehydrogenase [NAD(P)+]
more
top
Information
