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Information on EC 2.3.3.9 - malate synthase and Organism(s) Escherichia coli and UniProt Accession P37330

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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:
Escherichia coli
UNIPROT: P37330
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The taxonomic range for the selected organisms is: Escherichia coli
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 G
-
glyoxylate transacetase
-
-
-
-
glyoxylic transacetase
-
-
-
-
L-malate glyoxylate-lyase (CoA-acetylating)
-
-
-
-
malate synthase 1
-
-
-
-
malate synthase A
-
-
malate synthase G
malate synthetase
-
-
-
-
malic synthetase
-
-
-
-
malic-condensing enzyme
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + glyoxylate + H2O = (S)-malate + CoA
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aldol condensation
-
-
-
-
Claisen 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
acetyl-CoA + glyoxylate + H2O
(S)-malate + CoA
show the reaction diagram
-
-
-
-
?
acetyl-CoA + glyoxylate + H2O
CoA + (S)-malate
show the reaction diagram
-
-
-
-
?
acetyl-CoA + H2O + glyoxylate
(S)-malate + CoA
show the reaction diagram
-
-
-
-
?
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
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
acetyl-CoA + H2O + glyoxylate
(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
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
enzyme catalyzes the Claisen condensation of glyoxylate and acetyl-CoA to form malate in a magnesium-dependent manner
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,4,5-trioxopyrrolidine-3-carboxamide
oxalate
parabanic acid
pyruvate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.009 - 0.11
acetyl-CoA
0.021 - 0.058
glyoxylate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.19 - 48.1
glyoxylate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.04 - 0.113
2,4,5-trioxopyrrolidine-3-carboxamide
0.023 - 0.037
oxalate
0.37 - 0.55
parabanic acid
0.6 - 1.6
pyruvate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.39
-
mutant R338K, pH 8.0, 37°C
31.8
-
mutant C617S, pH 8.0, 37°C
36.1
-
wild-type, pH 8.0, 37°C
additional information
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
82000
1 * 82000
52000 - 54000
-
gel filtration, equilibrum sedimentation centrifugation, light scattering, two distinct forms of enzyme
55000
-
gel filtration
56000
-
1 * 56000, SDS-PAGE
65000
-
x * 65000
70000
-
1 * 70000, SDS-PAGE
80000
-
1 * 80000
82000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 82000
monomer
multimer
-
x * 65000
additional information
-
enzyme monomeric in procaryotes but multimeric in eucaryotes
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
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C438S
-
residue in the acetyl-CoA binding pocket
C617S
D631N
R338K
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45
-
50 mM Tris-HCl, pH 8.0, without KCl or with 0.2 M KCl, half-life: 25 min
50
-
50 mM Tris-HCL, pH 8.0, without KCl or with 0.2 M KCl, half-life: 3 min
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
HiTrap column chromatography
-
Ni-NTA agarose column chromatography and Superdex 200 gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
-
expression in Escherichia coli
-
His-tag version expressed in Escherichia coli
-
His-tagged version expressed in Escherichia coli
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
in 20 mM Tris, 300 mM NaCl, 10 mM MgSO4, 1 mM TCEP HCl, 10% (v/v) glycerol buffer, pH 7.9
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sundaram, T.K.; Chell, R.M.; Wilkinson, A.E.
Monomeric malate synthase from a thermophilic Bacillus
Arch. Biochem. Biophys.
199
515-525
1980
Bacillus sp. (in: Bacteria), Escherichia coli, Neurospora crassa
Manually annotated by BRENDA team
Chell, R.M.; Sundaram, T.K.
Structural basis of the thermostability of monomeric malate synthase from a thermophilic Bacillus
J. Bacteriol.
135
334-341
1978
Bacillus licheniformis, Bacillus sp. (in: Bacteria), Escherichia coli, Vogesella indigofera
Manually annotated by BRENDA team
Falmagne, P.; Wiame, J.M.
Purification et caracterisation partielle des deux malate synthases d` Escherichia coli
Eur. J. Biochem.
37
415-424
1973
Escherichia coli
-
Manually annotated by BRENDA team
Howard, B.R.; Endrizzi, J.A.; Remington, S.J.
Crystal structure of Escherichia coli malate synthase G complexed with magnesium and glyoxylate at 2.0 ANG resolution: Mechanistic implications
Biochemistry
39
3156-3168
2000
Escherichia coli
Manually annotated by BRENDA team
Anstrom, D.M.; Kallio, K.; Remington, S.J.
Structure of the Escherichia coli malate synthase G:pyruvate:acetyl-coenzyme A abortive ternary complex at 1.95 A resolution
Protein Sci.
12
1822-1832
2003
Escherichia coli
Manually annotated by BRENDA team
Maheshwari, A.; Verma, V.K.; Chaudhuri, T.K.
Equilibrium and kinetics of the unfolding and refolding of Escherichia coli Malate Synthase G monitored by circular dichroism and fluorescence spectroscopy
Biochimie
92
491-498
2010
Escherichia coli
Manually annotated by BRENDA team
Grishaev, A.; Tugarinov, V.; Kay, L.; Trewhella, J.; Bax, A.
Refined solution structure of the 82-kDa enzyme malate synthase G from joint NMR and synchrotron SAXS restraints
J. Biomol. NMR
40
95-106
2008
Escherichia coli (P37330)
Manually annotated by BRENDA team
Dunn, M.F.; Ramirez-Trujillo, J.A.; Hernandez-Lucas, I.
Major roles of isocitrate lyase and malate synthase in bacterial and fungal pathogenesis
Microbiology
155
3166-3175
2009
Bradyrhizobium japonicum, Candida albicans, Escherichia coli, Mycobacterium tuberculosis, Paracoccidioides brasiliensis, Parastagonospora nodorum, Rhizobium leguminosarum, Rhodococcus fascians, Sinorhizobium meliloti, Xanthomonas campestris, Yersinia enterocolitica, Yersinia pestis, Yersinia pseudotuberculosis
Manually annotated by BRENDA team
Lohman, J.R.; Olson, A.C.; Remington, S.J.
Atomic resolution structures of Escherichia coli and Bacillus anthracis malate synthase A: comparison with isoform G and implications for structure-based drug discovery
Protein Sci.
17
1935-1945
2008
Escherichia coli, Bacillus anthracis (A0A0F7RL08), Bacillus anthracis
Manually annotated by BRENDA team
Kumar, R.; Bhakuni, V.
Comparative analysis of malate synthase G from Mycobacterium tuberculosis and E. coli: role of ionic interaction in modulation of structural and functional properties
Int. J. Biol. Macromol.
49
917-922
2011
Escherichia coli, Mycobacterium tuberculosis, Escherichia coli C41
Manually annotated by BRENDA team
Dahiya, V.; Chaudhuri, T.K.
Functional intermediate in the refolding pathway of a large and multidomain protein malate synthase G
Biochemistry
52
4517-4530
2013
Escherichia coli
Manually annotated by BRENDA team