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Information on EC 2.3.3.9 - malate synthase and Organism(s) Ricinus communis and UniProt Accession P17815

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     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:
Ricinus communis
UNIPROT: P17815
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Word Map
The taxonomic range for the selected organisms is: Ricinus communis
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
malate synthase
-
glyoxylate transacetase
-
-
-
-
glyoxylic transacetase
-
-
-
-
L-malate glyoxylate-lyase (CoA-acetylating)
-
-
-
-
malate synthase 1
-
-
-
-
malate synthase G
-
-
-
-
malate synthetase
-
-
-
-
malic synthetase
-
-
-
-
malic-condensing enzyme
-
-
-
-
MSG
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aldol condensation
-
-
-
-
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
-
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
additional information
?
-
-
enzyme undergoes in vitro phosphorylation
-
-
?
NATURAL SUBSTRATE
NATURAL 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
-
enzyme specifically involved in glyoxalate cycle metabolism
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
required
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ADP
-
5 mM, 46% inhibition
AMP
-
5 mM, 46% inhibition
ATP
-
5 mM, 55% inhibition
glycolate
-
-
oxalate
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.01
acetyl-CoA
-
-
2
glyoxylate
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.15
glycolate
-
-
0.11
oxalate
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
MASY_RICCO
567
0
64263
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
575000
-
sucrose density gradient centrifugation
64000
-
x * 64000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 64000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
side-chain modification
-
posttranslational phosphorylation at a Ser residue
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yang, Y.P.; Randall, D.D.; Trelease, R.N.
Phosphorylation of glyoxysomal malate synthase from castor oil seeds Ricinus communis L.
FEBS Lett.
234
275-279
1988
Ricinus communis
-
Manually annotated by BRENDA team
Bowden, L.; Lord, J.M.
Purification and comparative properties of microsomal and glyoxysomal malate synthase from castor bean endosperm
Plant Physiol.
61
259-265
1978
Ricinus communis
Manually annotated by BRENDA team
Henry, H.; Escher, C.L.; Widmer, F.
Salt-mediated interconversions and purification of malate synthase from germiating soybean cotyledons (Glycine max.)
Plant Sci.
82
21-27
1992
Ricinus communis, Glycine max
-
Manually annotated by BRENDA team
Anand, P.; Kwak, Y.; Simha, R.; Donaldson, R.P.
Hydrogen peroxide induced oxidation of peroxisomal malate synthase and catalase
Arch. Biochem. Biophys.
491
25-31
2009
Ricinus communis (P17815), Ricinus communis
Manually annotated by BRENDA team