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Information on EC 1.1.1.83 - D-malate dehydrogenase (decarboxylating)
for references in articles please use BRENDA:EC1.1.1.83
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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
1.1.1.83 D-malate dehydrogenase (decarboxylating)
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
- 1.1.1.83
- fluorescens
- oxaloacetate
- dehydrogenases
-
isomerization
- maleylpyruvate
-
nadp-linked
- alcaligenes
-
nadp-dependent
- gentisate
- aerogenes
-
l-malic
- analysis
showSynonyms
d-malate dehydrogenase, d-malic enzyme, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D-malate dehydrogenase
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-
-
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D-malic enzyme
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-
-
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dehydrogenase, D-malate (decarboxylating)
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-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(R)-malate + NAD+ = pyruvate + CO2 + NADH + H+
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-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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-
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oxidative decarboxylation
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-
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redox reaction
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-
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reduction
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-
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-
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SYSTEMATIC NAME
IUBMB Comments
(R)-malate:NAD+ oxidoreductase (decarboxylating)
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CAS REGISTRY NUMBER
COMMENTARY
37250-20-7
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-malate + NAD+
pyruvate + CO2 + NADH
-
Substrates: induced by D-malate
Products: -
Products: -
?
(R)-malate + NAD+
pyruvate + CO2 + NADH
-
Substrates: -
Products: -
Products: -
?
(R)-malate + NAD+
pyruvate + CO2 + NADH
-
Substrates: -
Products: -
Products: -
?
(R)-malate + NAD+
pyruvate + CO2 + NADH
-
Substrates: -
Products: -
Products: -
?
(R)-malate + NAD+
pyruvate + CO2 + NADH
-
Substrates: -
Products: -
Products: -
?
(R)-malate + NAD+
pyruvate + CO2 + NADH
-
Substrates: -
Products: -
Products: -
?
(R)-malate + NAD+
pyruvate + CO2 + NADH
-
Substrates: -
Products: -
Products: -
?
(R)-malate + NAD+
pyruvate + CO2 + NADH + H+
Substrates: -
Products: -
Products: -
?
(R)-malate + NAD+
pyruvate + CO2 + NADH + H+
-
Substrates: -
Products: -
Products: -
r
additional information
?
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Substrates: bifunctional L(+)-tartrate dehydrogenase (decarboxylating) EC 1.1.1.93/EC 1.1.1.83 also catalyzes nonoxidative decarboxylation of L-tartrate
Products: -
Products: -
?
additional information
?
-
-
Substrates: bifunctional L(+)-tartrate dehydrogenase (decarboxylating) EC 1.1.1.93/EC 1.1.1.83 also catalyzes nonoxidative decarboxylation of L-tartrate
Products: -
Products: -
?
additional information
?
-
-
Substrates: bifunctional L(+)-tartrate dehydrogenase (decarboxylating) EC 1.1.1.93/EC 1.1.1.83 also catalyzes nonoxidative decarboxylation of L-tartrate
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-malate + NAD+
pyruvate + CO2 + NADH
-
Substrates: induced by D-malate
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mn2+
Mn2+
-
Km: 0.016 mM, optimal activity in presence of both Mn2+ and NH4+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
bifunctional L(+)-tartrate dehydrogenase-D(+)-malate dehydrogenase,decarboxylating, EC 1.1.1.93/EC 1.1.1.83
-
-
brenda
Highest Expressing Human Cell Lines
Cell Line Links Show AA Sequence and Transmembrane Helices (10241 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
NAD+ provides better protection against inactivation than D-malate or beta,beta-dimethyl-DL-malate
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
NAD+ protects against heat inactivation and trypsinization but not against protein denaturants
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
addition of nitrate during anaerobic growth represses the expression of dmlA-lacZ about 2.2fold, but the expression is still higher than the expression under aerobic conditions. The presence of glucose during anaerobic growth represses dmlA expression to levels similar to those observed after nitrate addition, suggesting that there is some glucose repression (2.4fold)
in a wild-type background, D-malate and meso- and L-tartrate cause high levels of induction of dmlA-lacZ expression (up to 12.3fold). With L-malate, succinate, and D-tartrate there is only weak induction. Induction of dmlA encoding DmlA requires an intact dmlR gene, which encodes DmlR, a LysR-type transcriptional regulator
the expression of dmlA-lacZ at high levels is induced under anaerobic conditions in the presence of D-malate and is more than 5fold greater than the expression under aerobic conditions
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
sequential fluorometric quantification of malic acid enantiomers in a single line flow-injection system using immobilized-enzyme reactors. An immobilized D-malate dehydrogenase (EC 1.1.1.83) reactor and an immobilized L-malate dehydrogenase (EC 1.1.1.40) reactor are introduced into the flowline in series. Sample and coenzyme (NAD+ or NADP+) are injected into the flow line by an open sandwich method. D-Malate is selectively oxidized by EC 1.1.1.83 when NAD+ is injected with a sample. When NADP+ is injected with a sample, L -malate is oxidized only by 1.1.1.40. NADH or NADPH produced by the immobilized-enzyme reactors is monitored fluorometrically at 455 nm
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lhdesmki, M.; Mntsl, P.
Comparison of D-malate and beta, beta-dimethylmalate dehydrogenases from Pseudomonas fluorescens UK-1
Biochim. Biophys. Acta
613
266-274
1980
Pseudomonas fluorescens, Pseudomonas fluorescens UK-1
brenda
Ebbighausen, H.; Giffhorn, F.
A novel mechanism involved in the metabolism of the tartaric acid stereoisomers in Rhodopseudomonas sphaeroides: enzymatic conversion of meso-tartaric acid to D(-)-glyceric acid and CO2
Arch. Microbiol.
138
338-344
1984
Cereibacter sphaeroides
-
brenda
Stern, J.R.; O'Brien, R.W.
Oxidation D-malic and beta-alkylmalic acids wild-type and mutant strains of Salmonella typhimurium and by Aerobacter aerogenes
J. Bacteriol.
98
147-151
1969
Klebsiella aerogenes, Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Knichel, W.; Radler, F.
D-Malic enzyme of Pseudomonas fluorescens
Eur. J. Biochem.
123
547-552
1982
Klebsiella aerogenes, Pseudomonas aeruginosa, Pseudomonas fluorescens, Pseudomonas putida
brenda
Laehdesmaeki, M.; Maentsaelae, P.
D-Malate dehydrogenase from pseudomonas fluorescens UK-1
Acta Chem. Scand. B
34
423-427
1980
Pseudomonas fluorescens, Pseudomonas fluorescens UK-1
brenda
Giffhorn, F.; Kuhn, A.
Purification and characterization of a bifunctional L-(+)-tartrate dehydrogenase-D-(+)-malate dehydrogenase (decarboxylating) from Rhodopseudomonas sphaeroides Y
J. Bacteriol.
155
281-290
1983
Cereibacter sphaeroides, Cereibacter sphaeroides Y
brenda
Tsukatani, T.; Matsumoto, K.
Sequential fluorometric quantification of malic acid enantiomers by a single line flow-injection system using immobilized-enzyme reactors
Talanta
65
396-401
2005
Escherichia coli
brenda
Lukas, H.; Reimann, J.; Kim, O.B.; Grimpo, J.; Unden, G.
Regulation of aerobic and anaerobic D-malate metabolism of Escherichia coli by the LysR-type regulator DmlR (YeaT)
J. Bacteriol.
192
2503-2511
2010
Escherichia coli (P76251), Escherichia coli
brenda
EXTERNAL LINKS (specific for EC-Number 1.1.1.83)
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