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
1.1.1.83
-
RECOMMENDED NAME
GeneOntology No.
D-malate dehydrogenase (decarboxylating)
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
(R)-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
Butanoate metabolism
-
D-malate degradation
-
SYSTEMATIC NAME
IUBMB Comments
(R)-malate:NAD+ oxidoreductase (decarboxylating)
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
D-malate dehydrogenase
-
-
-
-
D-malic enzyme
-
-
-
-
dehydrogenase, D-malate (decarboxylating)
-
-
-
-
dmlA
P76251
-
CAS REGISTRY NUMBER
COMMENTARY
37250-20-7
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Pseudomonas fluorescens UK-1
UK-1
-
-
Manually annotated by BRENDA team
bifunctional L(+)-tartrate dehydrogenase-D(+)-malate dehydrogenase,decarboxylating, EC 1.1.1.93/EC 1.1.1.83
-
-
Manually annotated by BRENDA team
Rhodobacter sphaeroides Y
strain Y
-
-
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
(R)-malate + NAD+
pyruvate + CO2 + NADH
show the reaction diagram
-
-
-
-
?
(R)-malate + NAD+
pyruvate + CO2 + NADH
show the reaction diagram
-
-
-
-
?
(R)-malate + NAD+
pyruvate + CO2 + NADH
show the reaction diagram
-
-
-
-
?
(R)-malate + NAD+
pyruvate + CO2 + NADH
show the reaction diagram
-
-
-
-
?
(R)-malate + NAD+
pyruvate + CO2 + NADH
show the reaction diagram
-
-
-
-
?
(R)-malate + NAD+
pyruvate + CO2 + NADH
show the reaction diagram
Rhodobacter sphaeroides Y
-
-
-
-
?
(R)-malate + NAD+
pyruvate + CO2 + NADH
show the reaction diagram
Pseudomonas fluorescens UK-1
-
-
-
-
?
(R)-malate + NAD+
pyruvate + CO2 + NADH + H+
show the reaction diagram
P76251
-
-
-
?
D-malate + NAD+
pyruvate + CO2 + NADH
show the reaction diagram
-
induced by D-malate
-
-
-
additional information
?
-
-
bifunctional L(+)-tartrate dehydrogenase (decarboxylating) EC 1.1.1.93/EC 1.1.1.83 also catalyzes nonoxidative decarboxylation of L-tartrate
-
-
-
additional information
?
-
Rhodobacter sphaeroides Y
-
bifunctional L(+)-tartrate dehydrogenase (decarboxylating) EC 1.1.1.93/EC 1.1.1.83 also catalyzes nonoxidative decarboxylation of L-tartrate
-
-
-
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
D-malate + NAD+
pyruvate + CO2 + NADH
show the reaction diagram
-
induced by D-malate
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Co2+
-
1 mM, 30% of the activity with Mn2+
K2SO4
-
50 mM, 56% of the activity with Mn2+
KCl
-
50 mM, 63% of the activity with Mn2+
Mg2+
-
Mn2+ or Mg2+ required
Mg2+
-
5 mM, 59% of the activity with Mn2+
Mg2+
P76251
divalent cation required
Mn2+
-
Mn2+ or Mg2+ required
Mn2+
-
Km: 0.016 mM, optimal activity in presence of both Mn2+ and NH4+
NaCl
-
50 mM, 19% of the activity with Mn2+
Zn2+
-
0.1 mM, 14% of the activity with Mn2+
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Dihydroxyfumarate
-
noncompetitive
iodoacetate
-
5 mM, 24% inhibition
L-Tartrate
-
competitive with respect to D-malate
meso-tartrate
-
competitive
N-ethylmaleimide
-
1 mM, 18% inactivation
oxaloacetate
-
competitive
p-chloromercuribenzoate
-
0.2 mM, 10% inactivation
p-chloromercuribenzoate
-
0.5 mM, 45% inactivation
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
NH4+
-
optimal activity in presence of both Mn2+ and NH4+
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.6
-
P76251
assay at
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7
10.6
-
at pH 7.0 and 10.6: about 50% of activity maximum
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
37
-
P76251
assay at
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
140000
-
-
gel filtration
158000
-
-
gel filtration
162000
-
-
equilibrium sedimentation
175000
-
-
gel filtration, gradient gel electrophoresis
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
tetramer
-
4 * 34000, SDS-PAGE
tetramer
-
4 * 38500, SDS-PAGE
tetramer
Pseudomonas fluorescens UK-1
-
4 * 34000, SDS-PAGE; 4 * 34000, SDS-PAGE
-
tetramer
Rhodobacter sphaeroides Y
-
4 * 38500, SDS-PAGE
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
8.5
-
-
30C, 4 h, stable
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
-
half-life: 30 h
50
-
-
half-life: 120 min
55
-
-
half-life: 30 min
60
-
-
half-life: 9 min
65
-
-
2 min, 64% loss of activity
additional information
-
-
NAD+ provides better protection against inactivation than D-malate or beta,beta-dimethyl-DL-malate
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
NAD+ protects against heat inactivation and trypsinization but not against protein denaturants
-
10-40% loss of activity during repeated freezing and thawing
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-70C, pH 7.2, 1 mM EDTA
-
-20C, stable for months
-
0C, stable for 30 h, even at protein concentration below 1 mg/ml
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
bifunctional L-(+)-tartrate-D-(+)-malate dehydrogenase
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
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)
P76251
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
P76251
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
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