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 ACCESSION NO.
LITERATURE
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
-
acetyl-CoA + H2O + glyoxylate = (S)-malate + CoA
show the reaction diagram
mechanism
-
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
-
acetyl-CoA + H2O + glyoxylate = (S)-malate + CoA
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
aldol condensation
-
-
-
-
Claisen condensation
-
-
Claisen condensation
-
-
PATHWAY
KEGG Link
MetaCyc Link
chitin degradation to ethanol
-
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)
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
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
P0A5J4
-
malate synthase G
Mycobacterium tuberculosis Rv1837c
P0A5J4
-
-
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
SEQUENCE CODE
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
Q8LPA6
Swissprot
Manually annotated by BRENDA team
growth on glucose
-
-
Manually annotated by BRENDA team
sunflower
-
-
Manually annotated by BRENDA team
Mycobacterium tuberculosis Rv1837c
-
UniProt
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
Q7BNB5
Swissprot
Manually annotated by BRENDA team
M130
Q7BNB5
SwissProt
Manually annotated by BRENDA team
Streptomyces coelicolor A3(2) M130
M130
Q7BNB5
SwissProt
Manually annotated by BRENDA team
expression with GST-tag in Escherichia coli
Swissprot
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
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
-
-
-
-
?
acetyl-CoA + glyoxylate + H2O
(S)-malate + CoA
show the reaction diagram
-, Q8LPA6
-
-
-
?
acetyl-CoA + glyoxylate + H2O
(S)-malate + CoA
show the reaction diagram
Q7BNB5, -
-
-
-
?
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
Q97YI7, -
-
-
-
?
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
-, P0A5J4
-
-
-
?
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
Q7BNB5
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
Mycobacterium tuberculosis Rv1837c
P0A5J4
-
-
-
?
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
Streptomyces coelicolor A3(2) M130
Q7BNB5
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
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
glyoxylate + propionyl-CoA + H2O
2-oxopentanedioic acid + CoA
show the reaction diagram
-
not
-
-
?
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 ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
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 ACCESSION NO.
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+
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+
Q7BNB5
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+
-, P0A5J4
cofactor
Mg2+
D4GTL2, -
contains one Mg2+ ion in the active site
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 ACCESSION NO.
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
Q7BNB5
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
-
-
dephosphoacetyl-CoA
-
-
dethio-CoA
-, P0A5J4
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
-
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
Q7BNB5
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
-
1 mM, 43% residual activity
oxalate
-
; competitive
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
-
-
pyruvate
-
1 mM, 89% residual activity
pyruvate
B0Q556, -
-
pyruvate
-
; competitive
S-Acetonyl-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 ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
EDTA
-
0.01 mM, 10% activation
Triton X-100
-
activation
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0022
-
acetyl-CoA
-
pH 8.0, 30C
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
-, P0A5J4
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
-
-
0.11
-
acetyl-CoA
-
-
0.11
-
acetyl-CoA
-
mutant R338K, pH 8.0, 37C
0.045
-
glyoxalate
-
pH 8.0, 30C
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
Q7BNB5
-
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
-, P0A5J4
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
-
-
0.104
-
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
Q7BNB5
-
-
additional information
-
additional information
-, Q8LPA6
bifunctional enzyme has specific catalytic features. Isocitrate lyase activity is increased by acetyl-CoA
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
23
-
acetyl-CoA
-, P0A5J4
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
-, P0A5J4
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]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
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
-
-
0.44
-
glycolate
P42450
-
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
-
-
0.6
-
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]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
additional information
-
pyruvate
-
1 mM pyruvate: 40% activity
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.0012
-
Q9ZH77, -
-
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
-
Q7BNB5, -
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
-
Q7BNB5, -
mutant R171L, pH 7.9
69.6
-
-
-
308
-
-
-
25090
-
Q7BNB5, -
wild-type, pH 7.9
additional information
-
-
-
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
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.6
-
-
-
8
-
-
Tris/HCl buffer
8
-
Q97YI7, -
assay at
8.2
-
-
phosphate-citrate-borate buffer or MOPS-KOH buffer
8.6
-
-
-
additional information
-
-
pI 7.5
additional information
-
-
4.6
additional information
-
-
5.0
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.8
8.5
-, P0A5J4
-
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
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
Q7BNB5
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
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
70
-
Q97YI7, -
assay at
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
-
-
15.5% activity
15
-
-
47.1% activity
32.5
40
-
more than 90% of activity
additional information
-
-
Km for glyoxylate increases with decreasing temperature
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
8.45
-
Q5YLB8
calculated
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
of 72-hours dark-grown seedlings
Manually annotated by BRENDA team
-
of dark-germinated seeds
Manually annotated by BRENDA team
Cucurbita sp.
-
-
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
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
abundant in ehtanol-grown cells
Manually annotated by BRENDA team
Cucurbita sp.
-
exclusively localized in
Manually annotated by BRENDA team
-
abundant cells grown on oleic acid; matrix
Manually annotated by BRENDA team
Candida tropicalis pK 233
-
matrix
-
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)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
52000
54000
-
gel filtration, equilibrum sedimentation centrifugation, light scattering, two distinct forms of enzyme
55000
-
-
gel filtration
62000
-
-
gel filtration
62000
-
-
gel filtration
62000
-
-
gel filtration
65000
-
-
gel filtration, enzyme form MSL
80000
-
P42450
gel filtration
81000
-
-
-
110000
-
-
gel filtration
120000
-
Cucurbita sp.
-
sucrose density gradient centrifugation
160000
-
-
gel filtration
160000
-
-
gel filtration
170000
-
-
gel filtration, ultracentrifugation, sucrose density gradient centrifugation
180000
-
-
high speed equilibrium sedimentation
186000
-
-
small-angle X-ray scattering technique
189000
-
Q97YI7, -
-
250000
-
-
gel filtration
250000
-
-
gel filtration
350000
-
-
gel filtation
420000
-
-, Q8LPA6
gel filtration
480000
-
Cucurbita sp.
-
sucrose density gradient centrifugation
510000
-
-
gel filtration
520000
-
-
gel filtration
520000
-
-
gel filtration
575000
-
-
sucrose density gradient centrifugation
630000
-
-
enzyme form MSH; gel filtration
630000
-
-
gel filtration
730000
-
-
gel filtration
750000
-
-
sucrose density gradient centrifugation
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
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 62000, SDS-PAGE, enzyme forms MSL and MSH
?
-
x * 64000, SDS-PAGE
?
-
x * 62000, SDS-PAGE
?
-
x * 63000, SDS-PAGE
?
Q7BNB5, -
x * 86000, GST-enzyme fusion protein, SDS-PAGE
?
Q71JU8, -
x * 60900, calculated
?
-, Q6X898
x * 65000, SDS-PAGE and calculated
?
-
x * 79400, predicted and observed (SDS-PAGE)
?
Q5YLB8
x * 60000, SDS-PAGE
?
Q5YLB8
x * 60000, Western blot analysis
?
-
x * 62000, the 62000 Da N-terminal domain of glyoxylate cycle enzyme provides malate synthase activity, SDS-PAGE
?
-, P0A5J4
x * 80000, His-tagged enzyme, SDS-PAGE
?
Mycobacterium tuberculosis Rv1837c
-
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
-
2 * 61360, calculation from nucleotide sequence
dimer
Cucurbita sp.
-
2 * 60000, enzyme exists as dimer and as octamer, SDS-PAGE
dimer
-
2 * 763000, SDS-PAGE
dodecamer
-
12 * 63000, SDS-PAGE
homodimer
Q97YI7, -
-
monomer
-
1 * 58000, SDS-PAGE
monomer
-
1 * 58000, SDS-PAGE
monomer
-
1 * 56000, SDS-PAGE
monomer
P42450
1* 82362, calculation from nucleotide sequence; 1 * 90000, SDS-PAGE
monomer
-
1 * 82000
monomer
-
1 * 80000
monomer
D4GTL2, -
malate synthase isoforms A and G
monomer
-
1 * 70000, SDS-PAGE
monomer
-
1 * 80000, SDS-PAGE
multimer
-
x * 65000
octamer
-
8 * 63000, predominant form, SDS-PAGE
octamer
Cucurbita sp.
-
8 * 60000, enzyme exists as dimer and as octamer, SDS-PAGE
octamer
-
8 * 22000, SDS-PAGE
octamer
-
8 * 65000, SDS-PAGE
tetramer
-
4 * 61000, SDS-PAGE
tetramer
-
4 * 70000, SDS-PAGE
tetramer
-
4 * 62000, SDS-PAGE
tetramer
-, Q8LPA6
4 * 110000, 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 ACCESSION NO.
COMMENTARY
LITERATURE
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
side-chain modification
-
enzyme contains phospholipid
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 ACCESSION NO.
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
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
1
2
-
1 h preincubation: about 5% activity
5
-
-
1 h preincubation: about 5% activity
5.5
-
-
4C, 12 h, about 60% loss of activity, enzyme form MSH
6
7
-
1 h preincubation: 100% activity
6
-
-
4C, 12 h, about 90% loss of activity, enzyme form MSH
7
8
-
4C, 12 h, stable, enzyme forms MSL and MSH
7
-
-
inactive at pH 7.0 and below
9
-
-
4C, 12 h, about 50% loss of activity, enzyme form MSL, about 40% loss of activity of enzyme form MSH
11
-
-
1 h preincubation: 90% activity
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
-
pH 7.6, 5 min, enzyme form MSL is stable up to
40
-
-
pH 7.6, 5 min, about 30% loss of activity of enzyme form MSL
40
-
-
1 h preincubation: 100% activity
41
-
-
1 h, little effect
44
-
-
1 h, complete inactivation
45
-
-
pH 7.6, 5 min, about 60% loss of activity of enzyme form MSL, enzyme form MSH is stable up to
45
-
-
pH 7.5-9.5, completely stable for at least 2 h
45
-
-
50 mM Tris-HCl, pH 8.0, without KCl or with 0.2 M KCl, half-life: 25 min
50
-
-
pH 7.6, 5 min, complete loss of activity of enzyme form MSL
50
-
-
50 mM Tris-HCL, pH 8.0, without KCl or with 0.2 M KCl, half-life: 3 min
55
-
-
pH 7.6, 5 min, complete loss of activity of enzyme form MSH
55
-
Q71JU8, -
20 min, 80% residual activity, in presence of 0.2 M guanidine HCl, 10 min, 50% residual activity
55
-
-
1 h preincubation: 47% activity
60
-
-
less than 10% loss of activity after 2 h at pH 8
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
65
-
-
2 min, 84% loss of activity
70
-
-
1 h preincubation: complete loss of activity
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+
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
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 ACCESSION NO.
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 ACCESSION NO.
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
Q7BNB5
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
-, P0A5J4
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
Q7BNB5
expression in Escherichia coli
Q97YI7, -
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
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 ACCESSION NO.
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 enzymic activty
D631N
-
no activity
R338K
-
6.6% of wild-type activity
R338K
-
6% of wild-type activity
R187K
-
the glyoxylate cycle enzyme mutant completely loses malate synthase activity but retains isocitrate lyase activity
C619S
-, P0A5J4
the mutant exhibits kinetics comparable to those of the wild type enzyme
D453A
Q7BNB5, -
0.06% of wild-type activity
P186R
-
more thermostable and thermoactive than wild-type
R171L
Q7BNB5, -
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
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
Mycobacterium tuberculosis Rv1837c
-
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 ACCESSION NO.
COMMENTARY
LITERATURE
agriculture
-
enzyme is required for pathogenicity of the fungal phytopathogen