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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: Archaea, Bacteria
Synonyms
MDH II,
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MDH II
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uses both NADP+ and NAD+
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(S)-malate + NAD(P)+ = oxaloacetate + NAD(P)H + H+
(S)-malate + NAD(P)+ = oxaloacetate + NAD(P)H + H+
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(S)-malate + NAD(P)+ = oxaloacetate + NAD(P)H + H+
ordered bi-bi mechanism
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(S)-malate + NAD(P)+ = oxaloacetate + NAD(P)H + H+
ordered bi-bi mechanism
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(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)).
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9001-64-3
cf. EC 1.1.1.37
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(S)-malate + NAD+
oxaloacetate + NADH + H+
(S)-malate + NADP+
oxaloacetate + NADPH + H+
oxaloacetate + NADH
L-malate + NAD+
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-
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-
?
oxaloacetate + NADH + H+
L-malate + NAD+
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?
oxaloacetate + NADPH
L-malate + NADP+
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-
?
additional information
?
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(S)-malate + NAD+
oxaloacetate + NADH + H+
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-
?
(S)-malate + NAD+
oxaloacetate + NADH + H+
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-
-
-
?
(S)-malate + NAD+
oxaloacetate + NADH + H+
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-
-
-
?
(S)-malate + NADP+
oxaloacetate + NADPH + H+
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?
(S)-malate + NADP+
oxaloacetate + NADPH + H+
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?
(S)-malate + NADP+
oxaloacetate + NADPH + H+
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-
-
-
?
additional information
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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
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?
additional information
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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
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?
additional information
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no substrate: pyruvate
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?
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additional information
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no cofactor: NADPH
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NAD+
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NAD+
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relative activity of NAD+ to NADP+ is 43.9%
NADH
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NADP+
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NADP+
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relative activity of NAD+ to NADP+ is 43.9%
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CuCl2
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1 mM, 10% residual activity
HgCl2
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1 mM, no residual activity
iodoacetate
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1 mM, 16.4% residual activity
N-ethylmaleimide
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1 mM, no residual activity
NADH
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inhibitory above 0.2 mM
NADPH
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inhibitory above 0.2 mM
ZnCl2
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1 mM, 27% residual activity
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0.09
oxaloacetate
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pH 7.6
0.269
L-malate
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20°C
0.4
malate
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pH 7.6
0.4
malate
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at pH 7.6 and 60°C
0.028
NAD+
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10°C
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41.3
L-malate
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10°C
41
NAD+
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10°C
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52
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pH 7.6, reduction of oxaloacetate, cosubstrate NADP+
60
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pH 7.6, reduction of oxaloacetate, cosubstrate NAD+
1
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pH 7.6, oxidation of malate, cosubstrate NAD+
1
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pH 7.6, oxidation of malate, cosubstrate NADP+
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10.5
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oxidation of malate
8
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reduction of oxaloacetate
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4 - 10
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reduction of oxaloacetate
6.5 - 12
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oxidation of malate
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40
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highest initial velocity
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brenda
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brenda
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brenda
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MDH_AERPE
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
308
0
33490
Swiss-Prot
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MDH_METST
Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3)
317
0
34857
Swiss-Prot
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MDH_METTH
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
325
0
35933
Swiss-Prot
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MDH_METTM
Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg)
325
0
35860
Swiss-Prot
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MDH_METKA
Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)
317
0
34609
Swiss-Prot
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MDH_METMP
Methanococcus maripaludis (strain S2 / LL)
314
0
34468
Swiss-Prot
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A0A5J4DUJ1_9ARCH
269
0
29178
TrEMBL
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A0A5J4DRU1_9ARCH
304
0
32730
TrEMBL
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32000
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4 * 32000, SDS-PAGE
36000
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x * 36000, SDS-PAGE, x * 36700, calculated
36700
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x * 36000, SDS-PAGE, x * 36700, calculated
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?
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x * 36000, SDS-PAGE, x * 36700, calculated
tetramer
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4 * 32000, SDS-PAGE
tetramer
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4 * 32000, SDS-PAGE
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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
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1.1.1.299 malate dehydrogenase [NAD(P)+]
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