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EC Tree
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.
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,
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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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malate synthetase
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malic-condensing enzyme
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malate synthase G
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MSG
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acetyl-CoA + glyoxylate + H2O = (S)-malate + CoA
acetyl-CoA + glyoxylate + H2O = (S)-malate + CoA
mechanism
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acetyl-CoA + glyoxylate + H2O = (S)-malate + CoA
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
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aldol condensation
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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.
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acetyl-CoA + glyoxylate + H2O
(S)-malate + CoA
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?
acetyl-CoA + glyoxylate + H2O
CoA + (S)-malate
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?
acetyl-CoA + H2O + glyoxylate
(S)-malate + CoA
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glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
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glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
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glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
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glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
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enzyme specifically involved in glyoxalate cycle metabolism
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acetyl-CoA + H2O + glyoxylate
(S)-malate + CoA
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?
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
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enzyme specifically involved in glyoxalate cycle metabolism
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?
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Mg2+
enzyme catalyzes the Claisen condensation of glyoxylate and acetyl-CoA to form malate in a magnesium-dependent manner
Mg2+
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Mg2+
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enzyme-substrate complex with glyoxylate and Mg2+, Glu427 and Asp455 bind the magnesium ion
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2,4,5-trioxopyrrolidine-3-carboxamide
2,4,5-trioxopyrrolidine-3-carboxamide
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2,4,5-trioxopyrrolidine-3-carboxamide
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competitive
oxalate
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parabanic acid
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parabanic acid
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competitive
pyruvate
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0.009
acetyl-CoA
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wild-type, pH 8.0, 37°C
0.009
acetyl-CoA
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wild-type protein
0.022
acetyl-CoA
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wild-type protein
0.046
acetyl-CoA
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mutant C617S, pH 8.0, 37°C
0.046
acetyl-CoA
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C617 mutant protein
0.056
acetyl-CoA
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C438S mutant protein
0.11
acetyl-CoA
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mutant R338K, pH 8.0, 37°C
0.021
glyoxylate
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wild-type, pH 8.0, 37°C
0.021
glyoxylate
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wild-type protein
0.027
glyoxylate
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mutant R338K, pH 8.0, 37°C
0.05
glyoxylate
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mutant C617S, pH 8.0, 37°C
0.05
glyoxylate
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C617 mutant protein
0.055
glyoxylate
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wild-type protein
0.058
glyoxylate
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C438S mutant protein
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3.19
glyoxylate
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mutant R338K, pH 8.0, 37°C
42.4
glyoxylate
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mutant C617S, pH 8.0, 37°C
48.1
glyoxylate
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wild-type, pH 8.0, 37°C
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0.04 - 0.113
2,4,5-trioxopyrrolidine-3-carboxamide
0.37 - 0.55
parabanic acid
0.04
2,4,5-trioxopyrrolidine-3-carboxamide
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C438S mutant protein
0.113
2,4,5-trioxopyrrolidine-3-carboxamide
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C617 mutant protein
0.023
oxalate
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wild-type protein
0.037
oxalate
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wild-type protein
0.37
parabanic acid
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C438S mutant protein
0.55
parabanic acid
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C617 mutant protein
0.6
pyruvate
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C438S mutant protein
0.65
pyruvate
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wild-type protein
1
pyruvate
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mutant C617S, pH 8.0, 37°C
1
pyruvate
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wild-type, pH 8.0, 37°C
1
pyruvate
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C617 mutant protein
1
pyruvate
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wild-type protein
1.6
pyruvate
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mutant R338K, pH 8.0, 37°C
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2.39
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mutant R338K, pH 8.0, 37°C
31.8
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mutant C617S, pH 8.0, 37°C
36.1
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wild-type, pH 8.0, 37°C
additional information
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C438S mutant protein has 74% of wild-type acitvity
additional information
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C617S mutant protein has 88% of wild-type acitvity
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Uniprot
brenda
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52000 - 54000
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gel filtration, equilibrum sedimentation centrifugation, light scattering, two distinct forms of enzyme
56000
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1 * 56000, SDS-PAGE
70000
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1 * 70000, SDS-PAGE
82000
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1 * 82000, SDS-PAGE
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additional information
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enzyme monomeric in procaryotes but multimeric in eucaryotes
monomer
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monomer
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1 * 56000, SDS-PAGE
monomer
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1 * 70000, SDS-PAGE
monomer
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1 * 82000, SDS-PAGE
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isoform G in complex with Mg2+, pyruvate, and acetyl-CoA
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structure of enzyme based on a beta8/alpha8 barrel fold
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C438S
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residue in the acetyl-CoA binding pocket
C617S
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88.1% of wild-type activity
C617S
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residue in the acetyl-CoA binding pocket
D631N
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no activity
D631N
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no enzymic activity
R338K
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6% of wild-type activity
R338K
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6.6% of wild-type activity
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45
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50 mM Tris-HCl, pH 8.0, without KCl or with 0.2 M KCl, half-life: 25 min
50
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50 mM Tris-HCL, pH 8.0, without KCl or with 0.2 M KCl, half-life: 3 min
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HiTrap column chromatography
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Ni-NTA agarose column chromatography and Superdex 200 gel filtration
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expressed in Escherichia coli BL21(DE3) cells
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expression in Escherichia coli
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His-tag version expressed in Escherichia coli
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His-tagged version expressed in Escherichia coli
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in 20 mM Tris, 300 mM NaCl, 10 mM MgSO4, 1 mM TCEP HCl, 10% (v/v) glycerol buffer, pH 7.9
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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
brenda
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
brenda
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
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brenda
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
brenda
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
brenda
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
brenda
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)
brenda
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
brenda
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
brenda
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
brenda
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
brenda