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Information on EC 2.3.3.9 - malate synthase and Organism(s) Streptomyces clavuligerus and UniProt Accession Q9ZH77

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EC Tree
     2 Transferases
         2.3 Acyltransferases
             2.3.3 Acyl groups converted into alkyl groups on transfer
                2.3.3.9 malate synthase
IUBMB Comments
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.
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This record set is specific for:
Streptomyces clavuligerus
UNIPROT: Q9ZH77
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Word Map
The taxonomic range for the selected organisms is: Streptomyces clavuligerus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
malate synthase, malate synthase g, glyoxylate cycle enzyme, malate synthetase, malate synthase a, malate synthase 1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glyoxylate transacetase
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-
-
-
glyoxylic transacetase
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-
-
-
L-malate glyoxylate-lyase (CoA-acetylating)
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-
-
-
malate synthase 1
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-
-
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malate synthase G
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-
-
-
malate synthetase
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-
-
-
malic synthetase
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-
-
-
malic-condensing enzyme
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-
-
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MSG
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aldol condensation
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-
-
-
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.
CAS REGISTRY NUMBER
COMMENTARY hide
9013-48-3
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
the optimum concentration of acetyl-CoA 0.0001 mM, the optimum concentration of glyoxylate 0.001 mM
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-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acetyl-CoA
slight reduction of enzyme activity at high concentrations of acety-CoA
glyoxylate
slight reduction of enzyme activity at high concentrations of glyoxylate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00059
glyoxylate
-
additional information
additional information
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8 - 10
significant reduction of specific activity at pH 7.0 and below
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
NRRL3585
SwissProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
MASY_STRCL
541
0
60012
Swiss-Prot
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Loke, P.; Goh, L.L.; Soh, B.S.; Yeow, P.; Sim, T.S.
Purification and characterization of recombinant malate synthase enzymes from Streptomyces coelicolor A3(2) and S. clavuligerus NRRL3585
J. Ind. Microbiol. Biotechnol.
28
239-243
2002
Streptomyces clavuligerus (Q9ZH77), Streptomyces clavuligerus, Streptomyces clavuligerus NRRL 3585 (Q9ZH77), Streptomyces coelicolor (Q9RKU9), Streptomyces coelicolor, Streptomyces coelicolor A3(2) (Q9RKU9), Streptomyces coelicolor A3(2)
Manually annotated by BRENDA team