Information on EC 1.1.1.83 - D-malate dehydrogenase (decarboxylating)

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The expected taxonomic range for this enzyme is: Proteobacteria

EC NUMBER
COMMENTARY hide
1.1.1.83
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RECOMMENDED NAME
GeneOntology No.
D-malate dehydrogenase (decarboxylating)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(R)-malate + NAD+ = pyruvate + CO2 + NADH
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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oxidative decarboxylation
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redox reaction
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-
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Butanoate metabolism
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D-malate degradation
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SYSTEMATIC NAME
IUBMB Comments
(R)-malate:NAD+ oxidoreductase (decarboxylating)
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CAS REGISTRY NUMBER
COMMENTARY hide
37250-20-7
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UK-1
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
strain Y
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(R)-malate + NAD+
pyruvate + CO2 + NADH
show the reaction diagram
(R)-malate + NAD+
pyruvate + CO2 + NADH + H+
show the reaction diagram
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-
-
?
D-malate + NAD+
pyruvate + CO2 + NADH
show the reaction diagram
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induced by D-malate
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additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-malate + NAD+
pyruvate + CO2 + NADH
show the reaction diagram
-
induced by D-malate
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
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1 mM, 30% of the activity with Mn2+
K2SO4
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50 mM, 56% of the activity with Mn2+
KCl
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50 mM, 63% of the activity with Mn2+
NaCl
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50 mM, 19% of the activity with Mn2+
Zn2+
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0.1 mM, 14% of the activity with Mn2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,2-Butanedione
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D-lactate
Dihydroxyfumarate
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noncompetitive
iodoacetate
L-Tartrate
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competitive with respect to D-malate
meso-tartrate
N-ethylmaleimide
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1 mM, 18% inactivation
oxaloacetate
p-chloromercuribenzoate
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NH4+
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optimal activity in presence of both Mn2+ and NH4+
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.17 - 2.2
D-malate
0.08 - 0.49
NAD+
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 10.6
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at pH 7.0 and 10.6: about 50% of activity maximum
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
140000
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gel filtration
158000
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gel filtration
162000
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equilibrium sedimentation
175000
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gel filtration, gradient gel electrophoresis
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.5
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30°C, 4 h, stable
389609
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
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half-life: 30 h
50
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half-life: 120 min
55
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half-life: 30 min
60
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half-life: 9 min
65
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2 min, 64% loss of activity
additional information
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NAD+ provides better protection against inactivation than D-malate or beta,beta-dimethyl-DL-malate
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
10-40% loss of activity during repeated freezing and thawing
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NAD+ protects against heat inactivation and trypsinization but not against protein denaturants
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, stable for months
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-70°C, pH 7.2, 1 mM EDTA
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0°C, stable for 30 h, even at protein concentration below 1 mg/ml
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
bifunctional L-(+)-tartrate-D-(+)-malate dehydrogenase
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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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
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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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