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Information on EC 1.1.1.37 - malate dehydrogenase and Organism(s) Archaeoglobus fulgidus and UniProt Accession O08349

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EC Tree
     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.37 malate dehydrogenase
IUBMB Comments
There are several forms of malate dehydrogenases that differ by their use of substrate and cofactors. This NAD+-dependent enzyme forms oxaloacetate and unlike EC 1.1.1.38, malate dehydrogenase (oxaloacetate-decarboxylating), is unable to convert it to pyruvate. Also oxidizes some other 2-hydroxydicarboxylic acids. cf. EC 1.1.1.82, malate dehydrogenase (NADP+); EC 1.1.1.299, malate dehydrogenase [NAD(P)+]; and EC 1.1.5.4, malate dehydrogenase (quinone).
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Archaeoglobus fulgidus
UNIPROT: O08349
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The taxonomic range for the selected organisms is: Archaeoglobus fulgidus
The enzyme appears in selected viruses and cellular organisms
Synonyms
malate dehydrogenase, mdh, mitochondrial malate dehydrogenase, malic dehydrogenase, cytosolic malate dehydrogenase, nad-dependent malate dehydrogenase, maldh, mitochondrial mdh, s-mdh, l-malate dehydrogenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
(R)-2-hydroxyacid dehydrogenase
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-
-
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L-malate dehydrogenase
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-
-
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L-malate:NAD oxidoreductase
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malate (NAD) dehydrogenase
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-
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malate dehydrogenase (NAD)
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-
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malic acid dehydrogenase
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-
-
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malic dehydrogenase
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-
-
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mbNAD-MDH
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-
-
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mNAD-MDH
-
-
-
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NAD+-dependent malate dehydrogenase
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NAD-dependent malate dehydrogenase
-
-
-
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NAD-dependent malic dehydrogenase
-
-
-
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NAD-L-malate dehydrogenase
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-
-
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NAD-linked malate dehydrogenase
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-
-
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NAD-malate dehydrogenase
-
-
-
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NAD-malic dehydrogenase
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-
-
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NAD-specific malate dehydrogenase
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-
-
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VEG69
-
-
-
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Vegetative protein 69
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
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reduction
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
(S)-malate:NAD+ oxidoreductase
There are several forms of malate dehydrogenases that differ by their use of substrate and cofactors. This NAD+-dependent enzyme forms oxaloacetate and unlike EC 1.1.1.38, malate dehydrogenase (oxaloacetate-decarboxylating), is unable to convert it to pyruvate. Also oxidizes some other 2-hydroxydicarboxylic acids. cf. EC 1.1.1.82, malate dehydrogenase (NADP+); EC 1.1.1.299, malate dehydrogenase [NAD(P)+]; and EC 1.1.5.4, malate dehydrogenase (quinone).
CAS REGISTRY NUMBER
COMMENTARY hide
9001-64-3
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(S)-malate + NAD+
oxaloacetate + NADH + H+
show the reaction diagram
the reduction of oxaloacetate with NADH is preferred. Malate is oxidized by NAD+ at 10% of the maximal velocity for the reduction of oxaloacetate with NADH. No oxidation of malate with NADP+ as coenzyme
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-
r
oxaloacetate + NADH + H+
(S)-malate + NAD+
show the reaction diagram
the reduction of oxaloacetate with NADH is preferred. Malate is oxidized by NAD+ at 10% of the maximal velocity for the reduction of oxaloacetate with NADH. Maximal activity with NADPH is 10% compared to the activity with NADH
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-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
show the reaction diagram
-
-
-
-
r
oxaloacetate + NADH + H+
(S)-malate + NAD+
show the reaction diagram
-
-
-
-
r
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(S)-malate + NAD+
oxaloacetate + NADH + H+
show the reaction diagram
-
-
-
-
r
oxaloacetate + NADH + H+
(S)-malate + NAD+
show the reaction diagram
-
-
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD+
no oxidation of malate with NADP+ as coenzyme
NADH
maximal activity with NADPH is 10% compared to the activity with NADH
NADPH
maximal activity with NADPH is 10% compared to the activity with NADH
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(S)-malate
product inhibitor
NADH
substrate inhibition
oxaloacetate
substrate inhibition
NADH
-
MDH activity is strongly inhibited by excess of oxaloacetate and NADH, over 2 mM
oxaloacetate
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MDH activity is strongly inhibited by excess of oxaloacetate and NADH, overv 2 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.024
NADH
pH 8.0, 65°C, at 0.4 mM oxaloacetate
0.043
oxaloacetate
pH 8.0, 65°C, at 0.4 mM NADH
0.024
NADH
-
pH and temperature not specified in the publication
0.043
oxaloacetate
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pH and temperature not specified in the publication
additional information
additional information
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Michaelis-Menten kinetics
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2
(S)-malate
pH 8.0, 65°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.64
pH 8.0, 65°C, cell extract
4799
pH 8.0, 65°C, purified enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.6 - 8.2
in both 50 mM Tricine-KOH and 50 mM potassium phosphate buffer
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50 - 85
between 50°C and 85°C the activity increases following the Arrhenius equation with a calculated activation energy of 61.6 kJ/mol
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5
isoelectric focusing, pH 3–10
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
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MDH is a ubiquitous enzyme found in prokaryotic and eukaryotic organisms. The enzyme belongs to the superfamily of 2-ketoacid NAD(P)+-dependent dehydrogenases. MDH has diverged into two distinct phylogenetic groups. One group includes cytoplasmic MDH, chloroplast MDH, and MDH from Thermus flavus; the other group includes MDHs that are similar to lactate dehydrogenase (LDH). Structure comparisons, the MDHs are mostly dimeric or tetrameric, overview
physiological function
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regulation of MDH activity, overview
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35000
2 * 35000, SDS-PAGE
70000
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
2 * 35000, SDS-PAGE
dimer
-
crystal structure shows a compact homodimer with one coenzyme bound per subunit. The crystal structure reveals that the association of the dimers to form tetramers is prevented by several deletions, taking place at the level of two loops that are known to be essential for the tetramerization process within the LDH and malDH enzymes
additional information
-
oligomeric states of MDHs, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting drop method, crystal structure in complex with NAD+ solved at 2.9 A resolution. Crystal structure shows a compact homodimer with one coenzyme bound per subunit
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
101
half-life: more than 80 min. Marked stabilizing effect of 1 M K2HPO4 with an increase in thermostability of approximately 40% at 101°C
102
half-life: 30 min
103
half-life: 18 min
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, stable for several months under oxic conditions
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
transcriptional regulation of mdh gene, overview
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Irimia, A.; Vellieux, F.M.; Madern, D.; Zaccai, G.; Karshikoff, A.; Tibbelin, G.; Ladenstein, R.; Lien, T.; Birkeland, N.K.
The 2.9 A resolution crystal structure of malate dehydrogenase from Archaeoglobus fulgidus: mechanisms of oligomerisation and thermal stabilisation
J. Mol. Biol.
335
343-356
2004
Archaeoglobus fulgidus
Manually annotated by BRENDA team
Langelandsvik, A.S.; Steen, I.H.; Birkeland, N.K.; Lien, T.
Properties and primary structure of a thermostable L-malate dehydrogenase from Archaeoglobus fulgidus
Arch. Microbiol.
168
59-67
1997
Archaeoglobus fulgidus (O08349), Archaeoglobus fulgidus
Manually annotated by BRENDA team
Takahashi-Iniguez, T.; Aburto-Rodriguez, N.; Vilchis-Gonzalez, A.; Flores, M.
Function, kinetic properties, crystallization, and regulation of microbial malate dehydrogenase
J. Zhejiang Univ. Sci. B
17
247-261
2016
Aeropyrum pernix, Archaeoglobus fulgidus, Bacillus subtilis, uncultured bacterium, Corynebacterium glutamicum, Escherichia coli, Glaesserella parasuis, Haloarcula marismortui, Helicobacter pylori, Methanothermobacter thermautotrophicus, Methanocaldococcus jannaschii, Nitrosomonas europaea, Pseudomonas stutzeri, Kitasatospora aureofaciens, Streptomyces coelicolor, uncultured bacterium MPOB, Bacillus subtilis B1
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Manually annotated by BRENDA team