Information on EC 1.1.1.38 - malate dehydrogenase (oxaloacetate-decarboxylating)

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY
1.1.1.38
-
RECOMMENDED NAME
GeneOntology No.
malate dehydrogenase (oxaloacetate-decarboxylating)
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
(S)-malate + NAD+ = pyruvate + CO2 + NADH
show the reaction diagram
stepwise reaction mechanism in which hydride transfer preceeds decarboxylation
-
(S)-malate + NAD+ = pyruvate + CO2 + NADH
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
-
-
oxidative decarboxylation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
anaerobic energy metabolism (invertebrates, mitochondrial)
-
C4 photosynthetic carbon assimilation cycle, NAD-ME type
-
C4 photosynthetic carbon assimilation cycle, PEPCK type
-
chitin degradation to ethanol
-
gluconeogenesis I
-
methylgallate degradation
-
protocatechuate degradation I (meta-cleavage pathway)
-
Pyruvate metabolism
-
syringate degradation
-
SYSTEMATIC NAME
IUBMB Comments
(S)-malate:NAD+ oxidoreductase (oxaloacetate-decarboxylating)
Unlike EC 1.1.1.39, malate dehydrogenase (decarboxylating), this enzyme can also decarboxylate oxaloacetate. cf. EC 1.1.1.40, malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+).
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malic enzyme
-
-
-
-
malic enzyme
-
-
malic enzyme
Brevundimonas diminuta IFO13182
-
-
-
mitochondrial malic enzyme ME2
P23368
-
mitochondrial malic enzyme ME2
Q99KE1
-
mitochondrial malic enzyme ME2
-
-
mitochondrial NAD(P) malic enzyme ME2
P23368
-
mitochondrial NAD(P) malic enzyme ME2
Q99KE1
-
mitochondrial NAD(P) malic enzyme ME2
-
-
mitochondrial NAD-malic enzyme
-
-
NAD+-dependent malic enzyme
-
-
NAD-dependent ME
P26616
-
NAD-malic enzyme
-
-
-
-
NAD-malic enzyme
-
-
NAD-malic enzyme
-
-
NAD-ME
-
-
-
-
NAD-ME
P26616
-
NAD-specific malic enzyme
-
-
-
-
pyruvic-malic carboxylase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9080-52-8
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
parasitic roundwurm
-
-
Manually annotated by BRENDA team
strain IFO13182
-
-
Manually annotated by BRENDA team
Brevundimonas diminuta IFO13182
strain IFO13182
-
-
Manually annotated by BRENDA team
Enterobacter aerogenes IFO 3320
-
-
-
Manually annotated by BRENDA team
Eriochloa borumensis
-
-
-
Manually annotated by BRENDA team
Erwinia aroidea
-
-
-
Manually annotated by BRENDA team
Lactobacillus plantarum B38
-
-
-
Manually annotated by BRENDA team
now Sinorhizobium meliloti
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
-
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
-
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
r
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
r
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
-
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
-
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
r
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
r
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
-
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
-
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
-
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
r
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
r
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
r
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
-, r
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
-, r
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
-, r
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
-, r
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
-, r
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
-
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
-
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
-
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
-
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
-
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
-
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
P27443
-
-
-
?
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
r
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
r
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
r
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
r
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
r
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
r
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
r
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
-, r
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
-, r
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
-, r
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
-, r
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
-, r
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
-
r
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
Erwinia aroidea
-
-
-
-, r
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
-, r
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
-, r
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
-
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
-
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
r
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
r
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
-, r
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
-, r
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
-, r
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
-, r
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
-, r
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
Eriochloa borumensis
-
-
-
-, r
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
-
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
-
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
-
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
r
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
r
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
r
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
-, r
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
Enterobacter aerogenes IFO 3320
-
-
-
-, r
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
Lactobacillus plantarum B38
-
-
-
-, r
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
Brevundimonas diminuta IFO13182
-
-
-
-
r
(S)-malate + NAD+
pyruvate + CO2 + NADH
show the reaction diagram
-
-
-
-
?
(S)-malate + NAD+
pyruvate + CO2 + NADH
show the reaction diagram
-
-
-
-
?
(S)-malate + NAD+
pyruvate + CO2 + NADH
show the reaction diagram
-
-
-
-
?
(S)-malate + NAD+
pyruvate + CO2 + NADH
show the reaction diagram
P23368
-
-
-
?
(S)-malate + NAD+
pyruvate + CO2 + NADH
show the reaction diagram
Q99KE1
-
-
-
?
(S)-malate + NAD+
pyruvate + CO2 + NADH
show the reaction diagram
P26616
-
-
-
?
(S)-malate + NAD+
pyruvate + CO2 + NADH
show the reaction diagram
-
enzyme is involved in carbon fixation and metabolism, regulation of the pathways, overview
-
-
?
(S)-malate + NAD+
pyruvate + CO2 + NADH
show the reaction diagram
-
regulation of the pathway, metabolic flux and source-sink study, C4 photosynthetic metabolism in response to changes in the source-sink balance, modeling of a system of single-rooted leaves without petioles, overview
-
-
?
(S)-malate + NAD+
pyruvate + CO2 + NADH
show the reaction diagram
-
via decarboxylation of oxaloacetate
-
-
?
(S)-malate + NADP+
CO2 + pyruvate + NADPH
show the reaction diagram
-
-
-
-
-
(S)-malate + NADP+
CO2 + pyruvate + NADPH
show the reaction diagram
-
20% activity compared to cofactor NAD+
-
?
Oxaloacetate
CO2 + pyruvate
show the reaction diagram
-
-
-
ir
Oxaloacetate
CO2 + pyruvate
show the reaction diagram
-
-
-
ir
Oxaloacetate
CO2 + pyruvate
show the reaction diagram
-
-
-
ir
Oxaloacetate
CO2 + pyruvate
show the reaction diagram
-
-
-
ir
Oxaloacetate
CO2 + pyruvate
show the reaction diagram
-
-
-
ir
Oxaloacetate
CO2 + pyruvate
show the reaction diagram
-
-
-
ir
Oxaloacetate
CO2 + pyruvate
show the reaction diagram
-
-
-
ir
Oxaloacetate
CO2 + pyruvate
show the reaction diagram
-
-
-
ir
Oxaloacetate
CO2 + pyruvate
show the reaction diagram
-
-
-
ir
Oxaloacetate
CO2 + pyruvate
show the reaction diagram
-
-
-
ir
Oxaloacetate
CO2 + pyruvate
show the reaction diagram
-
-
-
ir
Oxaloacetate
CO2 + pyruvate
show the reaction diagram
-
-
-
ir
Oxaloacetate
CO2 + pyruvate
show the reaction diagram
-
-
-
ir
Oxaloacetate
CO2 + pyruvate
show the reaction diagram
-
-
-
ir
Oxaloacetate
CO2 + pyruvate
show the reaction diagram
-
-
-
ir
Oxaloacetate
CO2 + pyruvate
show the reaction diagram
-
-
-
ir
Oxaloacetate
CO2 + pyruvate
show the reaction diagram
-
-
-
ir
Oxaloacetate
CO2 + pyruvate
show the reaction diagram
-
-
-
ir
Oxaloacetate
CO2 + pyruvate
show the reaction diagram
-
-
-
ir
Oxaloacetate
CO2 + pyruvate
show the reaction diagram
-
-
-
ir
Oxaloacetate
CO2 + pyruvate
show the reaction diagram
-
-
-
ir
Oxaloacetate
CO2 + pyruvate
show the reaction diagram
-
-
-
ir
Oxaloacetate
CO2 + pyruvate
show the reaction diagram
-
-
-
ir
Oxaloacetate
CO2 + pyruvate
show the reaction diagram
-
-
-
ir
Oxaloacetate
CO2 + pyruvate
show the reaction diagram
-
-
-
ir
Oxaloacetate
CO2 + pyruvate
show the reaction diagram
-
-
-
ir
Oxaloacetate
CO2 + pyruvate
show the reaction diagram
-
-
-
ir
Oxaloacetate
CO2 + pyruvate
show the reaction diagram
Eleusine indica, Eriochloa borumensis
-
-
-
ir
Oxaloacetate
CO2 + pyruvate
show the reaction diagram
-
-
-
ir
Oxaloacetate
CO2 + pyruvate
show the reaction diagram
-
-
-
ir
Oxaloacetate
CO2 + pyruvate
show the reaction diagram
-
-
-
ir
Oxaloacetate
CO2 + pyruvate
show the reaction diagram
-
-
-
ir
Oxaloacetate
CO2 + pyruvate
show the reaction diagram
-
Mg2+ or Mn2+ are required
-
ir
Oxaloacetate
CO2 + pyruvate
show the reaction diagram
-
NAD+ inhibits oxaloacetate decarboxylation activity
-
ir
Oxaloacetate
CO2 + pyruvate
show the reaction diagram
Enterobacter aerogenes IFO 3320
-
-
-
ir
Oxaloacetate
CO2 + pyruvate
show the reaction diagram
Lactobacillus plantarum B38
-
-
-
ir
oxaloacetate + NADH
L-malate + NAD+
show the reaction diagram
-
-
-
?
oxaloacetate + NADH
(S)-malate + NAD+
show the reaction diagram
-
divalent metal ions are required
-
?
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
-
-
?
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
-
-
r
pyruvate + NADH + H+
L-lactate + NAD+
show the reaction diagram
-
-
-
?
pyruvate + NADH + H+
L-lactate + NAD+
show the reaction diagram
-
-
-
r
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
-
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
-
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
-
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
-
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
-
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
-
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
-
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
-
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
-
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
-
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
-
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
-
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
-
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
-
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
-
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
-
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
-
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
r
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
-
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
-
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
-
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
-
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
-
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
-
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
-
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
-
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
-
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
Eleusine indica, Eriochloa borumensis
-
-
-
-
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
-
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
-
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
-
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
-
-
-
-
(S)-malate + NAD+
pyruvate + CO2 + NADH
show the reaction diagram
P26616
-
-
-
?
(S)-malate + NAD+
pyruvate + CO2 + NADH
show the reaction diagram
-
enzyme is involved in carbon fixation and metabolism, regulation of the pathways, overview
-
-
?
(S)-malate + NAD+
pyruvate + CO2 + NADH
show the reaction diagram
-
regulation of the pathway, metabolic flux and source-sink study, C4 photosynthetic metabolism in response to changes in the source-sink balance, modeling of a system of single-rooted leaves without petioles, overview
-
-
?
(S)-malate + NAD+
pyruvate + CO2 + NADH
show the reaction diagram
-
via decarboxylation of oxaloacetate
-
-
?
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
Enterobacter aerogenes IFO 3320
-
-
-
-
(S)-malate + NAD+
CO2 + pyruvate + NADH
show the reaction diagram
Lactobacillus plantarum B38
-
-
-
-
(S)-malate + NADP+
CO2 + pyruvate + NADPH
show the reaction diagram
-
20% activity compared to cofactor NAD+
-
?
Oxaloacetate
CO2 + pyruvate
show the reaction diagram
-
-
-
ir
Oxaloacetate
CO2 + pyruvate
show the reaction diagram
-
-
-
ir
Oxaloacetate
CO2 + pyruvate
show the reaction diagram
-
-
-
ir
Oxaloacetate
CO2 + pyruvate
show the reaction diagram
-
-
-
ir
Oxaloacetate
CO2 + pyruvate
show the reaction diagram
-
-
-
ir
Oxaloacetate
CO2 + pyruvate
show the reaction diagram
-
-
-
ir
Oxaloacetate
CO2 + pyruvate
show the reaction diagram
-
-
-
ir
Oxaloacetate
CO2 + pyruvate
show the reaction diagram
-
-
-
ir
Oxaloacetate
CO2 + pyruvate
show the reaction diagram
-
-
-
ir
Oxaloacetate
CO2 + pyruvate
show the reaction diagram
-
-
-
ir
Oxaloacetate
CO2 + pyruvate
show the reaction diagram
-
-
-
ir
Oxaloacetate
CO2 + pyruvate
show the reaction diagram
-
-
-
ir
Oxaloacetate
CO2 + pyruvate
show the reaction diagram
-
-
-
ir
Oxaloacetate
CO2 + pyruvate
show the reaction diagram
-
-
-
ir
Oxaloacetate
CO2 + pyruvate
show the reaction diagram
-
-
-
ir
Oxaloacetate
CO2 + pyruvate
show the reaction diagram
-
-
-
ir
Oxaloacetate
CO2 + pyruvate
show the reaction diagram
-
-
-
ir
Oxaloacetate
CO2 + pyruvate
show the reaction diagram
-
-
-
ir
Oxaloacetate
CO2 + pyruvate
show the reaction diagram
-
-
-
ir
Oxaloacetate
CO2 + pyruvate
show the reaction diagram
-
-
-
ir
Oxaloacetate
CO2 + pyruvate
show the reaction diagram
-
-
-
ir
Oxaloacetate
CO2 + pyruvate
show the reaction diagram
-
-
-
ir
Oxaloacetate
CO2 + pyruvate
show the reaction diagram
-
-
-
ir
Oxaloacetate
CO2 + pyruvate
show the reaction diagram
-
-
-
ir
Oxaloacetate
CO2 + pyruvate
show the reaction diagram
-
-
-
ir
Oxaloacetate
CO2 + pyruvate
show the reaction diagram
-
-
-
ir
Oxaloacetate
CO2 + pyruvate
show the reaction diagram
-
-
-
ir
Oxaloacetate
CO2 + pyruvate
show the reaction diagram
Eleusine indica, Eriochloa borumensis
-
-
-
ir
Oxaloacetate
CO2 + pyruvate
show the reaction diagram
-
-
-
ir
Oxaloacetate
CO2 + pyruvate
show the reaction diagram
-
-
-
ir
Oxaloacetate
CO2 + pyruvate
show the reaction diagram
-
-
-
ir
Oxaloacetate
CO2 + pyruvate
show the reaction diagram
Escherichia coli B, Enterobacter aerogenes IFO 3320
-
-
-
ir
Oxaloacetate
CO2 + pyruvate
show the reaction diagram
Lactobacillus plantarum B38
-
-
-
ir
oxaloacetate + NADH
L-malate + NAD+
show the reaction diagram
-
-
-
?
pyruvate + NADH + H+
L-lactate + NAD+
show the reaction diagram
-
-
-
?
pyruvate + NADH + H+
L-lactate + NAD+
show the reaction diagram
-
-
-
r
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
NAD+
-
dependent on
NAD+
P23368
dual cofactor specificity for NAD+ and NADP+, but shows higher affinity for NAD+, mitochondrial malic enzyme ME2 activity is one-third to one-half as active in the presence of a saturating concentration of NADP+ compared to a saturating concentration of NAD+
NAD+
Q99KE1
dual cofactor specificity for NAD+ and NADP+, but shows higher affinity for NAD+, mitochondrial malic enzyme ME2 activity is one-third to one-half as active in the presence of a saturating concentration of NADP+ compared to a saturating concentration of NAD+
NAD+
-
dual cofactor specificity for NAD+ and NADP+, but shows higher affinity for NAD+, mitochondrial malic enzyme ME2 activity is one-third to one-half as active in the presence of a saturating concentration of NADP+ compared to a saturating concentration of NAD+
NADP+
-
2% activity
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Co2+
-
at 0.002 mM MgCl2 enzyme activity is reduced to 25% without additional divalent cations, activity is restored with 0.5 or 5.0 mM CoCl2
Cs+
-
30 mM Na+L-malate instead of K+L-malate reduces enzyme activity to 18% in the presence of 3 mM MnCl2, activity is restored with 5 or 50 mM CsCl
K+
-
30 mM Na+L-malate instead of K+L-malate reduces enzyme activity to 18% in the presence of 3 mM MnCl2, activity is restored with 50 mM KCl
Mg2+
-
at 0.002 mM MgCl2 enzyme activity is reduced to 25% without additional divalent cations, activity is restored with 0.5 or 5.0 mM MgCl2
Mg2+
-
stabilizes two distinct conformational states of the enzyme, which differ in response to various substrate and effector concentrations
Mg2+
-
complex sigmoidal saturation curve of free malate concentration in the presence of 5 mM Mg2+
Mn2+
-
at 0.002 mM MgCl2 enzyme activity is reduced to 25% without additional divalent cations, activity is restored with 0.5 or 5.0 mM MnCl2
Mn2+
-
stabilizes two distinct conformational states of the enzyme, which differ in response to various substrate and effector concentrations
Mn2+
-
hyperbolic saturation curve of free malate concentration in the presence of 0.3 mM Mn2+
Mn2+
-
Mn2+ protects enzyme against heat denaturation
Mn2+
-
required
Ni2+
-
requirement for divalent cation
Zn2+
-
requirement for divalent cation
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1,10-phenanthroline
-
0.025 mM, 70% activity lost after 5 min
1-(5-O-phosphono-beta-D-ribofuranosyl)-4-[2-(trifluoromethyl)phenyl]-1H-1,2,3-triazole
P26616
-
2-methylbutanoate
-
5.22 mM, competitive inhibitor, 60% inhibition at pH 7.5, 54% inhibition at pH 7.0
2-methylpentanoate
-
5.22 mM, competitive inhibitor, 45% inhibition at pH 7.5, 40% inhibition at pH 7.0
4,4'-dithiodipyridine
-
sulfhydryl reagent, rapid and complete loss of activity, presence of Mg2+ or Mn2+ enhances inactivation rate
4-(2-aminophenyl)-1-(5-O-phosphono-beta-D-ribofuranosyl)-1H-1,2,3-triazole
P26616
-
4-(2-fluorophenyl)-1-(5-O-phosphono-beta-D-ribofuranosyl)-1H-1,2,3-triazole
P26616
-
4-(2-hydroxyethyl)-1-(5-O-phosphono-beta-D-ribofuranosyl)-1H-1,2,3-triazole
P26616
-
4-(2-methylphenyl)-1-(5-O-phosphono-beta-D-ribofuranosyl)-1H-1,2,3-triazole
P26616
-
4-(4-fluorophenyl)-1-(5-O-phosphono-beta-D-ribofuranosyl)-1H-1,2,3-triazole
P26616
-
4-(4-methoxyphenyl)-1-(5-O-phosphono-beta-D-ribofuranosyl)-1H-1,2,3-triazole
P26616
-
4-(naphthalen-1-yl)-1-(5-O-phosphono-beta-D-ribofuranosyl)-1H-1,2,3-triazole
P26616
-
4-phenyl-1-(5-O-phosphono-beta-D-ribofuranosyl)-1H-1,2,3-triazole
P26616
-
5,5'-dithiobis(2-nitrobenzoic acid)
-
sulfhydryl reagent, rapid and complete loss of activity, presence of Mg2+ or Mn2+ enhances inactivation rate
5,5'-dithiobis(2-nitrobenzoic acid)
-
inhibition of decarboxylation activity
acetyl-CoA
-
0.005 mM, 18% inhibition, 0.01 mM, 42% inhibition, 0.1 mM, 68% inhibition
acetyl-CoA
-
allosteric inhibition
ADP
-
57% inhibition, 2 mM ADP, 0.01 mM CoA, 1 mM malate, 2 mM NAD+, 4 mM Mn2+
ADP
-
26% inhibition,2 mM ADP, 0.005 mM CoA, 5 mM malate, 2 mM NAD+, 4 mM Mn2+
AgNO3
-
inhibition with 20 mM, complete inhibition with 300 mM
AMP
-
50% inhibition, 2 mM AMP, 0.01 mM CoA, 1 mM malate, 2 mM NAD+, 4 mM Mn2+
AMP
-
39% inhibition, 2 mM AMP, 0.005 mM CoA, 5 mM malate, 2 mM NAD+, 4 mM Mn2+
ATP
-
72% inhibition, 2 mM ATP, 0.01 mM CoA, 1 mM malate, 2 mM NAD+, 4 mM Mn2+
ATP
-
allosteric inhibition
ATP
-
more effective in the presence of Mn2+ than in the presence of Mg2+, 50% inhibition with 1.6 mM Mn2+ and 3.9 mM in the presence of Mg2+ respectively
ATP
-
competitive inhibition
Cl-
-
competitive vs. malate and NAD+
CoA
-
allosteric inhibition
CoA
-
50% inhibition with 0.75 mM CoA in the presence of Mg2+ and 3.4 mM in the presence of Mn2+
CoA
-
in the absence of L-aspartate 50% inhibition with 0.22 mM CoA, in the presence of 2 mM L-aspartate 50% inhibition with 1.1 mM
Cu2+
-
0.025 mM, 70% activity lost after 5 min
D-malate
-
competitive inhibition
diethyldicarbonate
-
80% inactivation after treatment with 5 mM diethyldicarbonate for 25 min, biphasic inactivation, 40-50% inactivation in first phase, 1-2 histidine residues are acylated by diethyldicarbonate, 250 mM malate provides complete protection, 50% protection with 50 mM MgSO4, 55% enzyme activity is restored with 0.5 M hydroxylamine
iodoacetate
-
complete inactivation
iodoacetate
-
inhibition of decarboxylation activity
N-acetyl-1-(5-O-phosphono-beta-D-ribofuranosyl)-1H-1,2,3-triazol-4-amine
P26616
-
N-benzoyl-1-(5-O-phosphono-beta-D-ribofuranosyl)-1H-1,2,3-triazol-4-amine
P26616
-
N-ethylmaleimide
-
sulfhydryl reagent, rapid and complete loss of activity, presence of Mg2+ or Mn2+ enhances inactivation rate
N-ethylmaleimide
-
L-malate and tartronate strongly protect the enzyme in the presence of MnCl2 and NAD+, 80% inhibition of decarboxylation activity, 10fold increase in reduction activity
oxaloacetate
-
1 mM, 80% inhibition at pH 7.5, 50% inhibition at pH 7.0
oxaloacetate
-
50% inhibition with 0.09 mM
p-(chloromercuri)benzoate
-
complete inactivation
p-(chloromercuri)benzoate
-
-
p-(chloromercuri)benzoate
-
0.0025 mM, 80% inhibition within 2 min
Tartronate
-
competitive inhibition vs. malate, noncompetitve vs. NAD+
tiglic acid
-
5.22 mM, competitive inhibitor, 58% inhibition at pH 7.5, 52% inhibition at pH 7.0
UTP
-
25% inhibition, 0.01 mM CoA, 1 mM malate, 2 mM NAD+, 4 mM Mn2+
malonate
-
competitive inhibition
additional information
-
in vivo inhibition of the enzyme by oxidation, activity in leaves held under continuous light is reduced by 20-40%
-
additional information
-
water stress reduces the enzyme activity in vivo
-
additional information
P26616
synthesis and inhibitor potencies of triazole moiety-containing nucleotide analogues, overview. The synthesis involves two key steps, the lipase-mediated selective deacylation of 1-azido-2,3,5-tri-O-acetyl-beta-D-ribofuranoside and the Huisgen 1,3-dipolar cycloaddition between terminal alkynes and the 1-azido ribofuranoside derivative
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
5,5'-dithiobis(2-nitrobenzoic acid)
-
0.5 mM, 2.7fold increase in oxaloacetate reduction activity
alpha-methyl-DL-aspartate
-
1.35fold activation
aspartate
-
0.005 mM, 18% activation
aspartate
-
0.005 mM, 20% activation
aspartate
-
0.005 mM, 15% activation
aspartate
-
0.005 mM, 35% activation
ATP
-
68% activation, 2 mM ATP, 0.005 mM CoA, 5 mM malate, 2 mM NAD+, 4 mM Mn2+
beta-methyl-DL-aspartate
-
1.34fold activation
CoA
-
sigmoidal response to CoA concentration
D-Aspartate
-
2 mM, 1.27fold activation
fumarate
-
0.7 mM, 2.1fold activation
fumarate
P23368
-
fumarate
Q99KE1
-
L-aspartate
-
2 mM, 1.35fold activation
N-ethylmaleimide
-
1 mM, 8.9fold increase in oxaloacetate reduction activity
NH4+
-
30 mM Na+L-malate instead of K+L-malate reduces enzyme activity to 18% in the presence of 3 mM MnCl2, activity is restored with 5 or 50 mM NH4Cl
p-chloromercuribenzoate
-
0.02 mM, 2.5fold increase in oxaloacetate reduction activity
phosphoenolpyruvate
-
0.5 mM
UTP
-
35% activation, 2 mM UTP, 0.005 mM CoA, 5 mM malate, 2 mM NAD+, 4 mM Mn2+
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.42
-
(S)-malate
-
pH 7.2, 25C, recombinant enzyme
0.19
-
L-Malate
-
in the presence of 1 mM L-aspartate, pH 7.9
0.22
-
L-Malate
-
in the presence of 2 mM L-aspartate, pH 5.5
0.26
-
L-Malate
-
in the absence of L-aspartate, pH 5.5
0.4
-
L-Malate
-
-
0.4
-
L-Malate
-
in the absence of L-aspartate, pH 7.9
0.4
-
L-Malate
-
-
0.45
-
L-Malate
-
decarboxylation of L-malate
0.5
-
L-Malate
Erwinia aroidea
-
-
0.58
-
L-Malate
-
in the presence of 2 mM L-aspartate, pH 8.5
0.7
-
L-Malate
-
-
0.8
-
L-Malate
-
-
1
-
L-Malate
-
native enzyme
1.1
-
L-Malate
-
recombinant enzyme
1.1
-
L-Malate
-
-
1.18
-
L-Malate
-
pH 7.3
1.2
-
L-Malate
-
-
1.34
-
L-Malate
-
-
1.4
-
L-Malate
-
in the absence of L-aspartate, pH 8.5
1.63
-
L-Malate
-
-
1.76
-
L-Malate
-
-
1.96
-
L-Malate
-
-
2.15
-
L-Malate
-
-
2.21
-
L-Malate
-
-
3.1
-
L-Malate
-
in the presence of 0.5 mM ATP
5.2
-
L-Malate
-
pH 9.0
7.3
-
L-Malate
-
in the presence of 1.0 mM ATP
0.004
-
NAD+
-
pH 9.0
0.011
-
NAD+
-
native enzyme
0.011
-
NAD+
-
pH 7.3
0.015
-
NAD+
-
recombinant enzyme
0.046
-
NAD+
-
in the presence of 5 mM L-aspartate
0.058
-
NAD+
-
in the presence of 0.5 mM L-aspartate
0.06
-
NAD+
-
at pH 6.5, 7.0 and 7.5
0.063
-
NAD+
-
decarboxylation of L-malate
0.071
-
NAD+
-
nearly hyperbolic NAD+ saturation curve
0.097
-
NAD+
-
pH 7.2, 25C, recombinant enzyme
0.39
-
NAD+
-
-
0.48
-
NAD+
-
-
0.51
-
NAD+
Eriochloa borumensis
-
-
0.025
-
NADH
-
reduction of oxaloacetate
2.1
-
oxaloacetate
-
reduction of oxaloacetate
4.8
-
oxaloacetate
-
decarboxylation of oxaloacetate
5
-
oxaloacetate
-
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
134.4
-
(S)-malate
-
pH 7.2, 25C, recombinant enzyme
130
-
L-Malate
-
native and recombinant enzyme
28
-
oxaloacetate
-
in the absence of NAD+, 20 mM Mn2+
30
-
oxaloacetate
-
in the presence of NAD+, 20 mM Mn2+
0.06
-
pyruvate
-
in the presence of NAD+, 20 mM Mn2+
0.09
-
pyruvate
-
in the absence of NAD+, 20 mM Mn2+
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.017
-
-
water stress plants at daytime or at nighttime
0.036
-
-
control plants at daytime
0.07
-
-
pyruvate reduction
0.107
-
-
control plants at nighttime
0.46
-
-
below, extract from leaves under continuous light conditions
0.58
-
-
below, leaf extract
1.7
-
-
oxaloacetate reduction
30
-
Erwinia aroidea
-
-
32
-
-
-
35
-
-
-
38.5
-
-
recombinant enzyme
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
-
-
oxaloacetate reduction
5
-
-
pyruvate reduction
7
-
P26616
assay at
7.2
-
-
0.3 mM L-malate
7.2
-
-
with increasing substrate concentrations pH optimum is shifted towards higher pH values
7.2
-
-
recombinant His6-tagged enzyme
7.3
-
-
assay at
7.6
-
-
0.3 mM L-malate, in the presence of 2 mM L-aspartate
7.6
-
-
assay at
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.9
8
-
over 70% of maximal activity within this range
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-
assay at
25
-
-
assay at
30
-
-
assay at
37
-
P26616
assay at
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
no activity in chloroplasts and nuclei
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
65000
-
-
monomeric recombinant His6-tagged enzyme, native PAGE
84000
-
-
gel filtration
140000
-
-
gel filtration
180000
-
-
gel filtration
190000
-
-
gel filtration
198000
-
-
low speed sedimentation equilibrium
200000
-
Erwinia aroidea, Escherichia coli B
-
gel filtration
203000
-
-
sucrose density gradient centrifugation
220000
-
-
gel filtration
220000
-
-
-
240000
-
-
gel filtration
260000
-
-
tetrameric recombinant His6-tagged enzyme, native PAGE
500000
-
-
octameric recombinant His6-tagged enzyme, native PAGE
580000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oligomer
-
x * 65000, recombinant His6-tagged enzyme, SDS-PAGE, monomer, homotetramer, and homooctamer enzyme fomrs exist in solution
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
50
-
-
22% activity left after 4 min, 80% activity left in the presence of 10 mM L-aspartate and 1 mM MnCl2, 78% activity left in the presence of 0.7 mM CoA
OXIDATION STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
enzyme is reversibly inhibited by air oxidation, activity is completely restored in 30 min by the addition of 2 mM dithiotreitol
-
286697
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, 15 mM triethanolamine-maleate, pH 7.5, 1 mM EDTA, 10 mM dithiotreitol, 5% glycerol, several months, no loss of activity
-
4C, 50 mM Tris-HCl, pH 7.4, 1 mM EDTA, 10 mM 2-mercaptoethanol, 10 mM MgCl2, 5 mM L-aspartate, 2 months, 10% activity lost
-
4C, 50 mM Tris-HCl, pH 7.4, 1 mM EDTA, 10 mM 2-mercaptoethanol, 2 months, 15% activity lost
-
4C, 50 mM Tris-HCl, pH 7.4, 1 month, 90% activity lost
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ammonium sulfate, DEAE-cellulose, Blue-B agarose, Orange-A agarose
-
streptomycin sulfate ammonium sulfate, Phenyl-sepharose, Orange-A-Sepharose
-
DEAE Sepharose CL-6B column chromatography, and Q Sepharose column chromatography
-
recombinant His6-tagged enzyme from strain BL21(DE3) by nickel affinity chromatography and ultrafiltration to 95% purity
-
streptomycin, ammonium sulfate, heat treatment, acid treatment, calcium phosphate gel, DEAE-sephadex, hydroxylapatite, Sepharose 6B
-
38-40c treatment, ammonium sulfate, protamine sulfate precipitation, calcium phosphate gel, ammonium sulfate
-
MnCl2 precipitation, protaminsulfate precipitation, Sephadex G-25, Sephadex G-200, hydroxylapatite
-
MnCl2 precipitation, protaminsulfate precipitation, Sephadex G-25, hydroxylapatite
-
protamine sulfate precipitation, ammonium sulfate precipitation, DEAE-cellulose
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in Escherichia coli
-
expression of His6-tagged enzyme in strain BL21(DE3) as mainly soluble protein
-
overexpressed in Escherichia coli
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
N434A
P27443
with N434A, the interaction of the residue with malate is lost, causing the malate to reorient itself, leading to a slower decarboxylation step
N479Q
P27443
the Kmalate value for the N479Q mutant enzyme increases by 2.2fold compared to the wild type enzyme, the KNAD value for the N479Q mutant enzyme increases by 1.1fold compared to the wild type enzyme
N479S
P27443
the Kmalate value for the N479Q mutant enzyme increases by 2.1fold compared to the wild type enzyme, the KNAD value for the N479Q mutant enzyme increases by 1.8fold compared to the wild type enzyme
S433A
P27443
the KNAD value for the S433A mutant enzyme increases by 80fold compared to the wild type enzyme, indicating that this residue provides significant binding affinity for the dinucleotide
G444A
-
inactive enzyme