Information on EC 2.3.3.9 - malate synthase

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

EC NUMBER
COMMENTARY
2.3.3.9
-
RECOMMENDED NAME
GeneOntology No.
malate synthase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + H2O + glyoxylate = (S)-malate + CoA
show the reaction diagram
mechanism
-
acetyl-CoA + H2O + glyoxylate = (S)-malate + CoA
show the reaction diagram
mechanism
-
acetyl-CoA + H2O + glyoxylate = (S)-malate + CoA
show the reaction diagram
sequential bireactant mechanism
-
acetyl-CoA + H2O + glyoxylate = (S)-malate + CoA
show the reaction diagram
sequencial random mechanism
-
acetyl-CoA + H2O + glyoxylate = (S)-malate + CoA
show the reaction diagram
compulsory-order mechanism, glyoxylate being the first-binding substrate, glyoxylate triggers a conformational change in the enzyme and as a consequence, the correctly shaped binding site for acetyl-CoA is created
-
acetyl-CoA + H2O + glyoxylate = (S)-malate + CoA
show the reaction diagram
mechanism: D631 and R338 act in concert to form the enolate anion of acetyl-CoA in the rate limiting step. C617 is oxidized to cysteine-sulfenic acid
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
aldol condensation
-
-
-
-
Claisen condensation
-
-
Claisen condensation
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
-
-
chitin degradation to ethanol
-
-
citric acid cycle
-
-
glycolate and glyoxylate degradation II
-
-
Glyoxylate and dicarboxylate metabolism
-
-
glyoxylate cycle
-
-
L-arabinose degradation IV
-
-
Metabolic pathways
-
-
methylaspartate cycle
-
-
Microbial metabolism in diverse environments
-
-
Pyruvate metabolism
-
-
TCA cycle IV (2-oxoglutarate decarboxylase)
-
-
TCA cycle V (2-oxoglutarate:ferredoxin oxidoreductase)
-
-
xylose degradation IV
-
-
SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:glyoxylate C-acetyltransferase (thioester-hydrolysing, carboxymethyl-forming)
The enzyme catalyses the irreversible condensation of acetyl-CoA with glyoxylate to form (S)-malate. Among other functions, the enzyme participates in the glyoxylate cycle, a modified version of the TCA cycle that bypasses steps that lead to a loss of CO2.
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
EC 4.1.3.2
-
-
formerly
-
GCE(13-573)
-
N-terminal malate synthase-active domain of glyoxylate cycle enzyme
glcB
Sinorhizobium meliloti Rm5000
-
-
-
glyoxylate cycle enzyme
-
bifunctional enzyme possessing malate synthase and isocitrate lyase activities
glyoxylate transacetase
-
-
-
-
glyoxylic transacetase
-
-
-
-
L-malate glyoxylate-lyase (CoA-acetylating)
-
-
-
-
malate synthase
-
-
malate synthase
Q5YLB8
-
malate synthase
Paracoccidioides brasiliensis Pb01
Q5YLB8
-
-
malate synthase
-
-
malate synthase 1
-
-
-
-
malate synthase A
-
-
malate synthase A
-
-
malate synthase A
D4GTL2
isoform
malate synthase G
-
-
-
-
malate synthase G
Escherichia coli C41
-
-
-
malate synthase G
D4GTL2
isoform
malate synthase G
-
-
malate synthase G
P9WK17
-
malate synthase G
P9WK17
-
-
malate synthase G
-
-
malate synthase H
D4GTL2
isoform
malate synthetase
-
-
-
-
malic synthetase
-
-
-
-
malic-condensing enzyme
-
-
-
-
MSA
D4GTL2
-
MSG
-
-
-
-
MSG
Escherichia coli C41
-
-
-
MSG
D4GTL2
-
MSH
D4GTL2
-
SSO1334
Q97YI7
gene name
CAS REGISTRY NUMBER
COMMENTARY
9013-48-3
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
thermophilic
-
-
Manually annotated by BRENDA team
pathogenic isolates of Candida albicans obtained from HIV/AIDS, diabetic and burn patients
-
-
Manually annotated by BRENDA team
Candida tropicalis pK 233
pK 233
-
-
Manually annotated by BRENDA team
induced by growth on acetate and light
Swissprot
Manually annotated by BRENDA team
formerly Vibrio sp. strain ABE-1
-
-
Manually annotated by BRENDA team
cucumber
-
-
Manually annotated by BRENDA team
Cucurbita sp.
-
-
-
Manually annotated by BRENDA team
isoform G
-
-
Manually annotated by BRENDA team
Escherichia coli C41
-
-
-
Manually annotated by BRENDA team
bifunctional malate synthase/isocitrate lyase, induced by growth on ethanol
Swissprot
Manually annotated by BRENDA team
growth on glucose
-
-
Manually annotated by BRENDA team
Haloferax volcanii DSM 3757
-
-
-
Manually annotated by BRENDA team
sunflower
-
-
Manually annotated by BRENDA team
ssp. indica cv Guangluai 4
-
-
Manually annotated by BRENDA team
Paracoccidioides brasiliensis Pb01
strain Pb01
UniProt
Manually annotated by BRENDA team
castor bean
-
-
Manually annotated by BRENDA team
stains KM10-15
-
-
Manually annotated by BRENDA team
Streptomyces clavuligerus NRRL3585
NRRL3585
SwissProt
Manually annotated by BRENDA team
expression in Escherichia coli
SwissProt
Manually annotated by BRENDA team
expression in Escherichia coli
SwissProt
Manually annotated by BRENDA team
expression with GST-tag in Escherichia coli
Swissprot
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
-
key enzyme of the glyoxylate cycle enzyme
physiological function
Haloferax volcanii DSM 3757
-
key enzyme of the glyoxylate cycle enzyme
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + glyoxylate + H2O
(S)-malate + CoA
show the reaction diagram
-
-
-
-
?
acetyl-CoA + glyoxylate + H2O
(S)-malate + CoA
show the reaction diagram
-
-
-
-
?
acetyl-CoA + glyoxylate + H2O
(S)-malate + CoA
show the reaction diagram
-
-
-
-
?
acetyl-CoA + glyoxylate + H2O
(S)-malate + CoA
show the reaction diagram
Q9RKU9
-
-
-
?
acetyl-CoA + glyoxylate + H2O
(S)-malate + CoA
show the reaction diagram
-
-
-
-
?
acetyl-CoA + glyoxylate + H2O
(S)-malate + CoA
show the reaction diagram
Q8LPA6
-
-
-
?
acetyl-CoA + glyoxylate + H2O
(S)-malate + CoA
show the reaction diagram
Q9RKU9
-
-
-
?
acetyl-CoA + glyoxylate + H2O
(S)-malate + CoA
show the reaction diagram
Euglena gracilis SM-ZK
-
-
-
-
?
acetyl-CoA + glyoxylate + H2O
CoA + (S)-malate
show the reaction diagram
-
-
-
-
?
acetyl-CoA + glyoxylate + H2O
CoA + (S)-malate
show the reaction diagram
B0Q556
-
-
-
?
acetyl-CoA + H2O + glyoxylate
(S)-malate + CoA
show the reaction diagram
-
-
-
-
-
acetyl-CoA + H2O + glyoxylate
(S)-malate + CoA
show the reaction diagram
Q97YI7
-
-
-
?
acetyl-CoA + H2O + glyoxylate
(S)-malate + CoA
show the reaction diagram
-
key enzyme of the glyoxylate cycle enzyme
-
-
?
acetyl-CoA + H2O + glyoxylate
(S)-malate + CoA
show the reaction diagram
Haloferax volcanii DSM 3757
-
-
-
-
-
acetyl-CoA + H2O + glyoxylate
(S)-malate + CoA
show the reaction diagram
Haloferax volcanii DSM 3757
-
key enzyme of the glyoxylate cycle enzyme
-
-
?
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
-
-
-
-
?
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
-
-
-
?
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
-
-
-
-
?
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
-
-
-
-
-
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
-
-
-
-
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
-
-
-
-
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
-
-
-
-
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
-
-
-
ir
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
-
-
-
?
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
-
-
-
-
?
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
-
-
-
-
?
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
-
-
-
-
?
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
-
-
-
-
?
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
-
-
-
?
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
-
-
-
-
?
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
-
-
-
-
?
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
-
-
-
ir
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
-
-
-
-
?
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
-
-
-
-
?
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
-
-
-
-
?
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
-
-
-
-
?
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
-
-
-
-
?
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
-
-
-
-
?
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
-
-
-
-
-
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
-
-
-
-
?
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
-
-
-
-
?
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
-
-
-
-
?
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
Cucurbita sp.
-
-
-
-
?
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
-
-
-
-
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
-
-
-
-
-
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
-
-
-
ir
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
-
-
-
-
?
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
-
-
-
-
?
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
-
-
-
-
?
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
-
-
-
-
?
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
-
-
-
-
?
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
P42450
-
-
-
?
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
-
-
-
-
?
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
D4GTL2
-
-
-
?
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
P9WK17
-
-
-
?
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
-
structure of enzyme-substrate complex
-
-
-
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
-
structure of enzyme-substrate complex
-
?
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
Q9RKU9
the optimum concentration of acetyl-CoA 0.0001 mM, the optimum concentration of glyoxylate 0.001 mM
-
-
?
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
Q9ZH77
the optimum concentration of acetyl-CoA 0.0001 mM, the optimum concentration of glyoxylate 0.001 mM
-
-
?
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
-
enzyme specifically involved in glyoxalate cycle metabolism
-
-
-
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
-
enzyme specifically involved in glyoxalate cycle metabolism
-
-
-
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
-
enzyme specifically involved in glyoxalate cycle metabolism
-
-
-
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
-
enzyme specifically involved in glyoxalate cycle metabolism
-
-
-
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
-
enzyme specifically involved in glyoxalate cycle metabolism
-
-
-
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
-
enzyme specifically involved in glyoxalate cycle metabolism
-
-
-
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
-
enzyme specifically involved in glyoxalate cycle metabolism
-
-
-
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
-
enzyme specifically involved in glyoxalate cycle metabolism
-
-
-
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
-
enzyme specifically involved in glyoxalate cycle metabolism
-
-
-
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
-
enzyme specifically involved in glyoxalate cycle metabolism
-
-
-
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
-
enzyme specifically involved in glyoxalate cycle metabolism
-
-
-
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
-
enzyme specifically involved in glyoxalate cycle metabolism
-
-
-
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
-
enzyme specifically involved in glyoxalate cycle metabolism
-
-
-
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
-
enzyme specifically involved in glyoxalate cycle metabolism
-
-
-
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
-
enzyme essential for acetate use in the bacterial cells
-
-
-
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
Q9RKU9
the optimum concentration of acetyl-CoA 0.0001 mM, the optimum concentration of glyoxylate 0.001 mM
-
-
?
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
P9WK17
-
-
-
?
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
Candida tropicalis pK 233
-
-
-
-
?
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
Streptomyces clavuligerus NRRL3585
Q9ZH77
the optimum concentration of acetyl-CoA 0.0001 mM, the optimum concentration of glyoxylate 0.001 mM
-
-
?
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
Escherichia coli C41
-
-
-
-
?
glyoxylate + butyryl-CoA + H2O
2-oxohexanedioic acid + CoA
show the reaction diagram
-
-
-
-
ir
glyoxylate + fluoroacetyl-CoA + H2O
2-oxo-3-fluoro-butanedioic acid + CoA
show the reaction diagram
-
-
-
-
ir
glyoxylate + propionyl-CoA + H2O
2-oxopentanedioic acid + CoA
show the reaction diagram
-
-
-
-
ir
additional information
?
-
-
enzyme undergoes in vitro phosphorylation
-
-
-
additional information
?
-
-
no substrate: oxaloacetate, pyruvate, 2-oxoglutarate, glyoxal
-
-
-
additional information
?
-
-
characteristic enzymes of the glyoxylate cycle
-
-
-
additional information
?
-
-
glyoxylate cycle enzyme
-
-
-
additional information
?
-
-
key enzymes of the glyoxylate cycle
-
-
-
additional information
?
-
Sinorhizobium meliloti, Sinorhizobium meliloti Rm5000
-
glcB (encoding malate synthase), in the absence of the 240-bp open reading frame SMc00767 is required for acetate metabolism. Malate synthase is not involved in nodulation or nitrogen fixation in the interaction of Sinorhizobium meliloti with alfalfa plants. glcB is dispensable in plant-microbe interactions
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + H2O + glyoxylate
(S)-malate + CoA
show the reaction diagram
Haloferax volcanii, Haloferax volcanii DSM 3757
-
key enzyme of the glyoxylate cycle enzyme
-
-
?
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
-
-
-
-
-
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
-
enzyme specifically involved in glyoxalate cycle metabolism
-
-
-
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
-
enzyme specifically involved in glyoxalate cycle metabolism
-
-
-
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
-
enzyme specifically involved in glyoxalate cycle metabolism
-
-
-
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
-
enzyme specifically involved in glyoxalate cycle metabolism
-
-
-
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
-
enzyme specifically involved in glyoxalate cycle metabolism
-
-
-
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
-
enzyme specifically involved in glyoxalate cycle metabolism
-
-
-
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
-
enzyme specifically involved in glyoxalate cycle metabolism
-
-
-
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
-
enzyme specifically involved in glyoxalate cycle metabolism
-
-
-
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
-
enzyme specifically involved in glyoxalate cycle metabolism
-
-
-
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
-
enzyme specifically involved in glyoxalate cycle metabolism
-
-
-
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
-
enzyme specifically involved in glyoxalate cycle metabolism
-
-
-
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
-
enzyme specifically involved in glyoxalate cycle metabolism
-
-
-
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
-
enzyme specifically involved in glyoxalate cycle metabolism
-
-
-
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
-
enzyme specifically involved in glyoxalate cycle metabolism
-
-
-
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
-
enzyme essential for acetate use in the bacterial cells
-
-
-
additional information
?
-
-
characteristic enzymes of the glyoxylate cycle
-
-
-
additional information
?
-
-
glyoxylate cycle enzyme
-
-
-
additional information
?
-
-
key enzymes of the glyoxylate cycle
-
-
-
additional information
?
-
Sinorhizobium meliloti, Sinorhizobium meliloti Rm5000
-
glcB (encoding malate synthase), in the absence of the 240-bp open reading frame SMc00767 is required for acetate metabolism. Malate synthase is not involved in nodulation or nitrogen fixation in the interaction of Sinorhizobium meliloti with alfalfa plants. glcB is dispensable in plant-microbe interactions
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ba2+
-
about 30% of the activation with Mg2+
Co2+
-
about 30% of the activation with Mg2+
Co2+
P42450
25% of the activation with Mg2+
Co2+
-
about 35% of the activation with Mg2+
KCl
-
salt optimum: 3.0 M KCl
Mg2+
-
optimal concentration 10 mM MgCl2; required
Mg2+
-
Km: 4.7 mM; required
Mg2+
-
absolute requirement for divalent metal ion, best fulfilled by Mg2+; Km: 0.59 mM
Mg2+
-
binding of acetyl-CoA to the synthase is independent of Mg2+ but that of glyoxylate is strictly dependent on the presence of Mg2+
Mg2+
-
required
Mg2+
-
causes no structurel effects, suggesting the metal ion to be involved in enzymatic catalysis rather than structural alternations
Mg2+
-
Km: 0.5 mM; required
Mg2+
P42450
absolute requirement for divalent cation, maximal activity with 40 mM Mg2+
Mg2+
-
Km: 0.3 mM; required
Mg2+
-
required
Mg2+
-
enzyme-substrate complex with glyoxylate and Mg2+, Glu427 and Asp455 bind the magnesium ion; required
Mg2+
-
required
Mg2+
Q9ZH77
optimal concentration 0.01 mM MgCl2; required
Mg2+
Q9RKU9
optimal concentration 0.005 mM MgCl2; required
Mg2+
-
absolute requirement for divalent cation, maximal activity with 5 mM Mg2+
Mg2+
-
maximal enzyme activity at 5-10 mM, Km-value 0.4 mM
Mg2+
P37330
enzyme catalyzes the Claisen condensation of glyoxylate and acetyl-CoA to form malate in a magnesium-dependent manner
Mg2+
B0Q556
-
Mg2+
P9WK17
cofactor
Mg2+
D4GTL2
contains one Mg2+ ion in the active site
Mg2+
-
activity is dependent on Mg2+
Mn2+
-
about 30% of the activation with Mg2+
Mn2+
-
can partially replace Mg2+ in activation
Mn2+
P42450
15% of the activation with Mg2+
Mn2+
-
19% of the activation with Mg2+
Ni2+
-
about 98% of the activation with Mg2+
Mn2+
-
40% of the activation with Mg2+
additional information
-
Co2+, Fe2+, Ca2+, Ba2+, Ni2+, Cd2+, Zn2+, Cu2+, Hg2+ are not able to support the activity of enzyme
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,4,5-trioxopyrrolidine-3-carboxamide
-
; competitive
acetaldehyde
-
weak
acetyl-CoA
Q9ZH77
slight reduction of enzyme activity at high concentrations of acety-CoA
acetyl-CoA
Q9RKU9
slight reduction of enzyme activity at high concentrations of acety-CoA
acetyl-CoA
-
above 0.02 mM
ADP
-
5 mM, 46% inhibition
ADP
-
1 mM, 50% residual activity
AMP
-
5 mM, 46% inhibition
AMP
-
1 mM, 54% residual activity
ATP
-
5 mM, 55% inhibition
ATP
-
1 mM, 50% residual activity
Butanedione
-
slight inhibition at high concentrations
Ca2+
-
5 mM, 19% residual activity
Chloroacetyl-CoA
-
-
citrate
-
1 mM, 82% residual activity
coenzyme A
-
0.1 mM, 56% residual activity
D-fructose-1,6-bisphosphate
-
10 mM, 60% residual activity
deamino-acetyl-CoA
-
-
deoxycholate
-
-
dephosphoacetyl-CoA
-
-
dethio-CoA
P9WK17
uncompetitive inhibitor versus glyoxylate and competitive inhibitor versus acetyl-CoA
-
diethyl dicarbonate
-
inhibition prevented by preincubation with acetyl-CoA
EDTA
-
1.0 mM, 30% inhibition
fluoroacetate
-
-
glycolate
-
-
glycolate
-
-
glycolate
-
-
glycolate
-
-
glycolate
P42450
-
glycolate
-
-
glycolate
-
only at fairly high concentration
glycolate
-
1 mM, 77% residual activity
Glyoxal
-
10 mM, 70% residual activity
glyoxylate
Q9ZH77
slight reduction of enzyme activity at high concentrations of glyoxylate
glyoxylate
Q9RKU9
slight reduction of enzyme activity at high concentrations of glyoxylate
iodoacetate
-
5 mM, 6% residual activity
K+
-
5 mM, 5% residual activity
malate
-
1.0 mM, 50% inhibition
methylglyoxal
-
-
Na+
-
5 mM, 10% residual activity
oxalate
-
competiteive with glyoxylate
oxalate
-
-
oxalate
-
-
oxalate
-
1 mM, 43% residual activity
oxalate
-
; competitive
oxaloacetate
-
-
oxaloacetate
-
1 mM, 92% residual activity
p-chloromercuribenzoate
-
0.05 mM, 9% residual activity
parabanic acid
-
; competitive
phosphoenolpyruvate
-
-
phosphoenolpyruvate
P42450
not
phosphoenolpyruvate
-
-
phosphoenolpyruvate
-
1 mM, 66% residual activity
pyridoxal-5'-phosphate
-
preincubation with glyoxylate but not acetyl-CoA prevents inhibition
pyruvate
-
weak
pyruvate
-
-
pyruvate
P42450
not
pyruvate
-
-
pyruvate
-
1 mM, 89% residual activity
pyruvate
-
-
pyruvate
B0Q556
-
pyruvate
-
; competitive
S-Acetonyl-CoA
-
-
S-Ethyl-CoA
-
-
Mn2+
-
5 mM, 16% residual activity
additional information
P42450
acetyl-phosphate; not: fructose 1,6-bisphosphate
-
additional information
-
3-phosphoglycerate, 6-phosphogluconate, malonic acid; not: fructose 1,6-bisphosphate
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
EDTA
-
0.01 mM, 10% activation
Triton X-100
-
activation
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00012
acetyl-CoA
-
pH 8.0, 40C
0.0022
acetyl-CoA
-
pH 8.0, 30C
0.008
acetyl-CoA
-
-
0.008
acetyl-CoA
-
-
0.009
acetyl-CoA
-
wild-type, pH 8.0, 37C
0.009
acetyl-CoA
-
wild-type protein
0.01
acetyl-CoA
-
-
0.01
acetyl-CoA
-
-
0.01
acetyl-CoA
P9WK17
wild type enzyme, at pH 7.5 and 25C
0.011
acetyl-CoA
-
-
0.012
acetyl-CoA
P42450
-
0.012
acetyl-CoA
-
-
0.02
acetyl-CoA
-
-
0.022
acetyl-CoA
-
wild-type protein
0.0228
acetyl-CoA
-
-
0.023
acetyl-CoA
B0Q556
-
0.025
acetyl-CoA
Q8LPA6
30C, pH 8.0
0.03
acetyl-CoA
-
recombinant enzyme
0.046
acetyl-CoA
-
mutant C617S, pH 8.0, 37C
0.046
acetyl-CoA
-
C617 mutant protein
0.05
acetyl-CoA
Q97YI7
pH 8.0, 70C, native enzyme from xylose-grown cell extract
0.052
acetyl-CoA
-
-
0.056
acetyl-CoA
-
C438S mutant protein
0.06
acetyl-CoA
Q97YI7
pH 8.0, 70C, recombinant enzyme
0.08
acetyl-CoA
-
-
0.08
acetyl-CoA
-
-
0.083
acetyl-CoA
-
-
0.088
acetyl-CoA
-
-
0.11
acetyl-CoA
-
-
0.11
acetyl-CoA
-
mutant R338K, pH 8.0, 37C
0.045
glyoxalate
-
pH 8.0, 30C
0.00011
glyoxylate
-
pH 8.0, 40C
0.00059
glyoxylate
Q9ZH77
-
0.002
glyoxylate
Q97YI7
pH 8.0, 70C, native enzyme from xylose-grown cell extract; pH 8.0, 70C, recombinant enzyme
0.00349
glyoxylate
Q9RKU9
-
0.0198
glyoxylate
-
-
0.021
glyoxylate
-
wild-type, pH 8.0, 37C
0.021
glyoxylate
-
wild-type protein
0.027
glyoxylate
-
mutant R338K, pH 8.0, 37C
0.03
glyoxylate
P42450
-
0.03
glyoxylate
P9WK17
wild type enzyme, at pH 7.5 and 25C
0.04
glyoxylate
Q8LPA6
30C, pH 8.0
0.05
glyoxylate
-
-
0.05
glyoxylate
-
mutant C617S, pH 8.0, 37C
0.05
glyoxylate
-
C617 mutant protein
0.052
glyoxylate
-
-
0.055
glyoxylate
-
wild-type protein
0.057
glyoxylate
-
recombinant enzyme
0.058
glyoxylate
-
-
0.058
glyoxylate
-
C438S mutant protein
0.06
glyoxylate
-
-
0.063
glyoxylate
-
-
0.065
glyoxylate
-
wild type full-length glyoxylate cycle enzyme, at 25C, pH not specified in the publication
0.07
glyoxylate
-
-
0.073
glyoxylate
-
N-terminal malate synthase-active domain GCE(13-573) of glyoxylate cycle enzyme, at 25C, pH not specified in the publication
0.076
glyoxylate
-
-
0.085
glyoxylate
B0Q556
-
0.093
glyoxylate
-
-
0.098
glyoxylate
-
-
0.1
glyoxylate
-
-
0.104
glyoxylate
-
-
0.14
glyoxylate
-
-
1
glyoxylate
-
-
1.25
glyoxylate
-
-
2
glyoxylate
-
-
additional information
additional information
-
thermal dependencies of Km, Gossypium hirsutum has a minimum value of 0.0083 mM at 27.5C and higher values at temperatures above or below, the Km of Helianthus annuus enzyme increases with temperature
-
additional information
additional information
Q9ZH77
-
-
additional information
additional information
Q9RKU9
-
-
additional information
additional information
Q8LPA6
bifunctional enzyme has specific catalytic features. Isocitrate lyase activity is increased by acetyl-CoA
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
23
acetyl-CoA
P9WK17
wild type enzyme, at pH 7.5 and 25C
27.8
acetyl-CoA
-
-
60.7
acetyl-CoA
-
at 20C
161
acetyl-CoA
-
at 45C
3.19
glyoxylate
-
mutant R338K, pH 8.0, 37C
14
glyoxylate
-
N-terminal malate synthase-active domain GCE(13-573) of glyoxylate cycle enzyme, at 25C, pH not specified in the publication
17
glyoxylate
-
wild type full-length glyoxylate cycle enzyme, at 25C, pH not specified in the publication
23
glyoxylate
P9WK17
wild type enzyme, at pH 7.5 and 25C
42.4
glyoxylate
-
mutant C617S, pH 8.0, 37C
48.1
glyoxylate
-
wild-type, pH 8.0, 37C
additional information
additional information
-
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.04
2,4,5-trioxopyrrolidine-3-carboxamide
-
C438S mutant protein
0.113
2,4,5-trioxopyrrolidine-3-carboxamide
-
C617 mutant protein
0.01
ATP
-
enzyme form MSH
0.2
ATP
-
enzyme form MSL
0.06
Bromopyruvate
-
-
0.07
glycolate
-
-
0.15
glycolate
-
-
0.31
glycolate
-
-
0.44
glycolate
P42450
-
0.019
oxalate
-
-
0.023
oxalate
-
wild-type protein
0.037
oxalate
-
wild-type protein
0.09
oxalate
-
-
0.11
oxalate
-
-
0.27
oxalate
P42450
-
1.2
oxalate
-
enzyme form MSH
1.5
oxalate
-
enzyme form MSL
1.5
oxaloacetate
-
-
0.37
parabanic acid
-
C438S mutant protein
0.55
parabanic acid
-
C617 mutant protein
0.2
phosphoenolpyruvate
-
-
0.54
pyruvate
-
-
0.6
pyruvate
-
C438S mutant protein
0.65
pyruvate
-
wild-type protein
0.75
pyruvate
B0Q556
-
1
pyruvate
-
mutant C617S, pH 8.0, 37C; wild-type, pH 8.0, 37C
1
pyruvate
-
C617 mutant protein; wild-type protein
1.6
pyruvate
-
mutant R338K, pH 8.0, 37C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
pyruvate
-
1 mM pyruvate: 40% activity
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2.39
-
mutant R338K, pH 8.0, 37C
3.73
Q5YLB8
cells grown in the presence of potassium acetate
5.19
Q8LPA6
30C, pH 8.0
6
-
recombinant enzyme
15.6
Q9RKU9
mutant D453A, pH 7.9
24.5
-
-
26.9
-
wild-type enzyme
27
-
mutant enzyme PC2 NG35
31.8
-
mutant C617S, pH 8.0, 37C
36.1
-
wild-type, pH 8.0, 37C
44.2
Q9RKU9
mutant R171L, pH 7.9
25090
Q9RKU9
wild-type, pH 7.9
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
Cucurbita sp.
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
C438S mutant protein has 74% of wild-type acitvity; C617S mutant protein has 88% of wild-type acitvity
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.6
-
-
8
-
Tris/HCl buffer
8
Q97YI7
assay at
8
-
assay at
8.2
-
phosphate-citrate-borate buffer or MOPS-KOH buffer
additional information
-
pI 7.5
additional information
-
4.6
additional information
-
5.0
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.8 - 8.5
P9WK17
-
5 - 9.5
-
pH 5.0: about 35% of maximal activity, pH 9.5: about 70% of maximal activity
6.8 - 9.7
-
pH 6.8 and 9.7: about 50% of maximal activity, phosphate-citrate-borate buffer
7 - 10
-
pH 7.0: about 40% of maximal activity, pH 10.0: about 45% of maximal activity
7 - 8.5
-
pH 7.0: about 80% of maximal activity, pH 8.7: about 60% of maximal activity, enzyme form MSL and MSH
7
-
87% activity
7.5 - 10.5
-
pH 7.5: about 55% of maximal activity, pH 10.5: about 25% of maximal activity, enzyme form MSL and MSH
7.5 - 8.5
Q8LPA6
malate synthase reaction
8 - 10
Q9ZH77
significant reduction of specific activity at pH 7.0 and below
8 - 10
Q9RKU9
significant reduction of specific activity at pH 7.0 and below
10
-
85% activity
additional information
-
below pH 6: no activity remains, outside pH 7-10 the activity decreases rapidly
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
-
assay at
70
Q97YI7
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5
-
15.5% activity
15
-
47.1% activity
20 - 45
Q9RKU9
-
25 - 80
-
25C: about 45% of maximal activity, 80C: about 45% of maximal activity
32.5 - 40
-
more than 90% of activity
additional information
-
Km for glyoxylate increases with decreasing temperature
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.45
Q5YLB8
calculated
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Cucurbita sp.
-
-
Manually annotated by BRENDA team
-
of 72-hours dark-grown seedlings
Manually annotated by BRENDA team
-
of dark-germinated seeds
Manually annotated by BRENDA team
-
no activity can be detected when lactate is the carbon source, but high activity is measured when acetate is
Manually annotated by BRENDA team
Haloferax volcanii DSM 3757
-
no activity can be detected when lactate is the carbon source, but high activity is measured when acetate is
-
Manually annotated by BRENDA team
-
grown both in light and in dark
Manually annotated by BRENDA team
-
the enzyme is consistently active in the seedlings submerged from 12 h to 72 h
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)
Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)
Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)
Mycobacterium leprae (strain Br4923)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
52000 - 54000
-
gel filtration, equilibrum sedimentation centrifugation, light scattering, two distinct forms of enzyme
638488
55000
-
gel filtration
638481
56000
-
gel filtration
638481
62000
-
gel filtration
33133
62000
-
gel filtration
638480
62000
-
gel filtration
638481
65000
-
gel filtration, enzyme form MSL
638472
80000
P42450
gel filtration
638495
81000
-
-
638502
110000
-
gel filtration
638491
120000
Cucurbita sp.
-
sucrose density gradient centrifugation
638493
160000
-
gel filtration
638480
160000
-
gel filtration
638504
170000
-
gel filtration, ultracentrifugation, sucrose density gradient centrifugation
638487
180000
-
high speed equilibrium sedimentation
638479
186000
-
small-angle X-ray scattering technique
638485
189000
Q97YI7
-
715548
200000
-
gel filtration
727500
250000
-
gel filtration
638474
250000
-
gel filtration
638496
350000
-
gel filtation
638482
420000
Q8LPA6
gel filtration
658479
480000
Cucurbita sp.
-
sucrose density gradient centrifugation
638493
510000
-
gel filtration
638497
520000
-
gel filtration
638492
520000
-
gel filtration
658296
575000
-
sucrose density gradient centrifugation
638483
630000
-
enzyme form MSH; gel filtration
638472
630000
-
gel filtration
638494
730000
-
gel filtration
638478
750000
-
sucrose density gradient centrifugation
638471, 638478
additional information
-
by incubation with 5 mM ATP the high molecular weight enzyme form MSH is converted to the low molecular weight enzyme form MSL
638472
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 62000, SDS-PAGE
?
Q5YLB8
x * 60000, SDS-PAGE
?
-
x * 63000, SDS-PAGE
?
-
x * 64000, SDS-PAGE
?
-
x * 62000, SDS-PAGE, enzyme forms MSL and MSH
?
Q71JU8
x * 60900, calculated
?
Q6X898
x * 65000, SDS-PAGE and calculated
?
Q9RKU9
x * 86000, GST-enzyme fusion protein, SDS-PAGE
?
Q5YLB8
x * 60000, Western blot analysis
?
-
x * 79400, predicted and observed (SDS-PAGE)
?
-
x * 62000, the 62000 Da N-terminal domain of glyoxylate cycle enzyme provides malate synthase activity, SDS-PAGE
?
P9WK17
x * 80000, His-tagged enzyme, SDS-PAGE
?
-
x * 86000, GST-enzyme fusion protein, SDS-PAGE
-
?
-
x * 80000, His-tagged enzyme, SDS-PAGE
-
?
Paracoccidioides brasiliensis Pb01
-
x * 60000, Western blot analysis
-
decamer
-
10 * 62000, SDS-PAGE
dimer
-
2 * 175000, SDS-PAGE
dimer
Cucurbita sp.
-
2 * 60000, enzyme exists as dimer and as octamer, SDS-PAGE
dimer
-
2 * 61360, calculation from nucleotide sequence
dimer
-
2 * 763000, SDS-PAGE
dodecamer
-
12 * 63000, SDS-PAGE
homodimer
Q97YI7
-
homotrimer
-
3 * 67000, SDS-PAGE
homotrimer
Haloferax volcanii DSM 3757
-
3 * 67000, SDS-PAGE
-
monomer
-
1 * 58000, SDS-PAGE
monomer
-
1 * 58000, SDS-PAGE
monomer
-
1 * 80000, SDS-PAGE
monomer
-
1 * 56000, SDS-PAGE
monomer
P42450
1 * 90000, SDS-PAGE
monomer
-
1 * 70000, SDS-PAGE
monomer
-
1 * 80000
monomer
P42450
1* 82362, calculation from nucleotide sequence
monomer
-
1 * 82000
monomer
D4GTL2
malate synthase isoforms A and G
multimer
-
x * 65000
octamer
-
8 * 65000, SDS-PAGE
octamer
Cucurbita sp.
-
8 * 60000, enzyme exists as dimer and as octamer, SDS-PAGE
octamer
-
8 * 22000, SDS-PAGE
octamer
-
8 * 63000, predominant form, SDS-PAGE
tetramer
Q8LPA6
4 * 110000, SDS-PAGE
tetramer
-
4 * 70000, SDS-PAGE
tetramer
-
4 * 62000, SDS-PAGE
tetramer
-
4 * 61000, SDS-PAGE
tetramer
Candida tropicalis pK 233
-
4 * 61000, SDS-PAGE
-
tetramer
Euglena gracilis SM-ZK
-
4 * 110000, SDS-PAGE
-
trimer
-
3 * 66000, SDS-PAGE
trimer or hexamer
D4GTL2
malate synthase isoform H is found in the native state as a trimer/hexamer equilibrium
monomer
Escherichia coli C41
-
1 * 70000, SDS-PAGE
-
additional information
-
enzyme monomeric in procaryotes but multimeric in eucaryotes
additional information
Q8LPA6
enzyme consists of N-terminal malate synthase domain fused to C-terminal isocitrate lyase domain
additional information
Euglena gracilis SM-ZK
-
enzyme consists of N-terminal malate synthase domain fused to C-terminal isocitrate lyase domain
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
side-chain modification
-
enzyme contains phospholipid
side-chain modification
-
enzyme synthesized as a monomeric precursor in the cytoplasm, processing which is a prerequisite for oligomerization takes place rapidly in the glyoxysomes
no modification
-
no glycoprotein
side-chain modification
-
posttranslational phosphorylation at a Ser residue
no modification
-
contains no covalent linked carbohydrate residues
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
isoform G in complex with Mg2+, pyruvate, and acetyl-CoA
-
structure of enzyme based on a beta8/alpha8 barrel fold
-
malate synthase isoform H in complex with glyoxylate and also as a ternary complex with acetyl-coenzyme A and pyruvate, sitting drop vapor diffusion method, using 0.17 M ammonium acetate, 24.5-27% (w/v) PEG 4500, 15% (v/v) glycerol, and 0.085 M sodium acetate trihydrate at a pH of 4.4-5.0
D4GTL2
mixed alpha/beta structure
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1 - 2
-
1 h preincubation: about 5% activity
702873
5
-
1 h preincubation: about 5% activity
702873
5.5
-
4C, 12 h, about 60% loss of activity, enzyme form MSH
638472
6 - 7
-
1 h preincubation: 100% activity
702873
6
-
4C, 12 h, about 90% loss of activity, enzyme form MSH
638472
7 - 8
-
4C, 12 h, stable, enzyme forms MSL and MSH
638472
7
-
inactive at pH 7.0 and below
638491
9
-
4C, 12 h, about 50% loss of activity, enzyme form MSL, about 40% loss of activity of enzyme form MSH
638472
11
-
1 h preincubation: 90% activity
702873
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
-
pH 7.6, 5 min, enzyme form MSL is stable up to
638472
40
-
pH 7.6, 5 min, about 30% loss of activity of enzyme form MSL
638472
40
-
1 h preincubation: 100% activity
702873
41
-
1 h, little effect
638491
44
-
1 h, complete inactivation
638491
45
-
pH 7.6, 5 min, about 60% loss of activity of enzyme form MSL, enzyme form MSH is stable up to
638472
45
-
pH 7.5-9.5, completely stable for at least 2 h
638481
45
-
50 mM Tris-HCl, pH 8.0, without KCl or with 0.2 M KCl, half-life: 25 min
638481
50
-
pH 7.6, 5 min, complete loss of activity of enzyme form MSL
638472
50
-
50 mM Tris-HCL, pH 8.0, without KCl or with 0.2 M KCl, half-life: 3 min
638481
55
-
pH 7.6, 5 min, complete loss of activity of enzyme form MSH
638472
55
Q71JU8
20 min, 80% residual activity, in presence of 0.2 M guanidine HCl, 10 min, 50% residual activity
659630
55
-
1 h preincubation: 47% activity
702873
60
-
less than 10% loss of activity after 2 h at pH 8
33133
60
-
25 mM Tris-HCl, pH 7.0, without KCl, half-life: 168 min, 25 mM Tris-HCL, pH 7.0, with KCl, half-life: 30 min, 25 mM glycine-NaOH buffer, pH 8.5, without KCl, half-life: 750 min, 25 mM glycine-NaOH buffer, pH 8.5, with 0.2 KCl, half-life: 50 min, 25 mM glycine-NaOH buffer, pH 9.0, without KCl, half-life: 522 min, 25 mM glycine-NaOH buffer, pH 9.0, with 0.2 KCl, half-life: 12 min, 25 mM Tris-HCL, pH 6.86, with 0.2 M KCl, half-life: 2 min
638481
65
-
2 min, 84% loss of activity
638478
70
-
1 h preincubation: complete loss of activity
702873
additional information
-
heating for 3 min, complete inactivation of enzyme form MSL and 65% loss of activity of enzyme form MSH, slight increase of heat stability in presence of glyoxylate and/or Mg2+
638472
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
freezing and thawing inactivates
-
DTT and glycerol stabilize
-
DTT stabilizes
-
salt does not stabilize
-
trypsin, treatment for 10 min, about 50% loss of activity of enzyme form MSH, 92% loss of activity of enzyme form MSL
-
freezing and thawing inactivates
-
Mg2+ stabilizes
-
inactivation in air-saturated aqueous solution by X-irradiation, inactivation is mainly due to the action of OH radicals, to a minor extent to O2 radicals and H2O2
-
Mg2+ stabilizes
-
limited proteolysis with trypsin results in cleavage of malate synthase into two framents of respectively 45000 Da and 19000 Da
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0-4C, stable for at least 2 weeks
-
-20C, stable for more than one month
-
4C, stable for more than 3 weeks
P42450
-70C, stable for at least 3 months
-
2C, stable for at least a month
-
-70C, 200 mM Hepes buffer, containing 6 mM MgCl2, 2 mM 2-mercaptoethanol, pH 7.6, stable for several months
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
-
Cucurbita sp.
-
Ni-NTA agarose column chromatography and Superdex 200 gel filtration
-
DEAE Sepharose column chromatography, HisTrap HP column chromatography, and Superdex 200 pg gel filtration
-
reverse phase chromatography, anion-exchange column chromatography, and gel filtration
D4GTL2
Ni-NTA agarose column chromatography and Superdex 200 gel filtration
-
recombinant enzyme
-
Ni-chelate affinity chromatography, His-, Trx-, and S-tag removed by cleavage with enterokinase
Q5YLB8
glutathione affinity chromatography, proteolytic removal of the GST tag, anion exchange chromatography
-
recombinant enzymes
Q9ZH77
recombinant enzymes
Q9RKU9
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
His-tagged version, gene synthesized commercially, expressed in Escherichia coli
B0Q556
expression in Escherichia coli and Corynebacterium glutamicum
P42450
overexpressed in Ashbya gossypii
-
expression in Escherichia coli
-
His-tag version expressed in Escherichia coli
-
His-tagged version expressed in Escherichia coli
-
wild type enzyme is expressed in Escherichia coli BL21(DE3) cells, mutant enzymes are expressed in Escherichia coli ArcticExpress(DE3) RP cells
-
expressed in Escherichia coli T7 Express cells
P9WK17
His-tagged version expressed in Escherichia coli
Q5YLB8
GST-tagged version expressed in Escherichia coli
-
expression in Escherichia coli
-
expression in Escherichia coli
Q9ZH77
expression in Escherichia coli
Q9RKU9
expression in Escherichia coli
Q97YI7
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
in the presence of macrophages
-
regulation by carbon and nitrogen sources, highly induced by oxalurate in the presence of glucose and by proline
Q5YLB8
in the presence of macrophages
-
regulation by carbon and nitrogen sources, highly induced by oxalurate in the presence of glucose and by proline
Paracoccidioides brasiliensis Pb01
-
-
decrease in transcription after germination, increase of activity after germination
-
during infection of tomato plants
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C438S
-
residue in the acetyl-CoA binding pocket
C617S
-
88.1% of wild-type activity
C617S
-
residue in the acetyl-CoA binding pocket
D631N
-
no activity
D631N
-
no enzymic activty
R338K
-
6% of wild-type activity
R338K
-
6.6% of wild-type activity
R187K
-
the glyoxylate cycle enzyme mutant completely loses malate synthase activity but retains isocitrate lyase activity
C619S
P9WK17
the mutant exhibits kinetics comparable to those of the wild type enzyme
D453A
Q9RKU9
0.06% of wild-type activity
P186R
-
more thermostable and thermoactive than wild-type
R171L
Q9RKU9
0.2% of wild-type activity, reduced expression at room temperature, expression of soluble protein at 15C
T8P/L9P
-
more thermostable than wild-type
T8P/L9P/P186R
-
more thermostable and thermoactive than wild-type
D453A
-
0.06% of wild-type activity
-
R171L
-
0.2% of wild-type activity, reduced expression at room temperature, expression of soluble protein at 15C
-
D475N
-
the glyoxylate cycle enzyme mutant completely loses malate synthase activity but retains isocitrate lyase activity
additional information
-
the C-terminal domain of the glyoxylate cycle enzyme, when expressed alone (GCE(566-1165)), does not show any enzyme activity
C619S
-
the mutant exhibits kinetics comparable to those of the wild type enzyme
-
additional information
-
enzyme disruption mutant, in absence of any supplied carbon source, spores are unable to germinate and therefore non-pathogenic. Germination and pathogenicity can be restored by addition of glucose or sucrose. In mutants, lipid mobilization and peroxisomal beta-oxidation is delayed or inhibited
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
-
enzyme is required for pathogenicity of the fungal phytopathogen