PTHR42739

MALATE SYNTHASE G

PANTHER entry
Member databasePANTHER
PANTHER typefamily

Description
Imported from IPR006253

Malate synthase G (MSG, 723 residues) is an enzyme of the glyoxylate pathway, that catalyses the Claisen condensation and subsequent hydrolysis of acetyl-coenzyme A (acetyl-CoA) and glyoxylate to form malate and CoA
[1, 8]
. This biochemical bypass is used by microorganisms (bacteria, yeast, and fungi) for biosynthesis under anaerobic conditions
[2]
. Enzymes of the glyoxylate bypass have been implicated as virulence factors in several pathogens, including Mycobacterium tuberculosis
[3, 4, 5]
.

The X-ray structure of the ternary abortive complex of MSG with pyruvate (glyoxylate mimic) and acetyl-CoA has been determined
[1]
and shown to have the same structure as in the complex with glyoxylate
[6]
. MSG is composed of four domains: an N-terminal α-helical clasp, a central TIM barrel α/β core, an α/β domain which may have a regulatory function, and a C-terminal five α-helical bundle
[8]
. The cleft between the TIM β/α-barrel fold and the C-terminal helical domain forms the active site of malate synthases
[7, 1, 6]
.

References
Imported from IPR006253

1.Structure of the Escherichia coli malate synthase G:pyruvate:acetyl-coenzyme A abortive ternary complex at 1.95 A resolution. Anstrom DM, Kallio K, Remington SJ. Protein Sci. 12, 1822-32, (2003). View articlePMID: 12930982

2.Synthesis of cell constituents from C2-units by a modified tricarboxylic acid cycle. KORNBERG HL, KREBS HA. Nature 179, 988-91, (1957). PMID: 13430766

3.Lipid lunch for persistent pathogen. Bishai W. Nature 406, 683-5, (2000). View articlePMID: 10963578

4.Persistence of Mycobacterium tuberculosis in macrophages and mice requires the glyoxylate shunt enzyme isocitrate lyase. McKinney JD, Honer zu Bentrup K, Munoz-Elias EJ, Miczak A, Chen B, Chan WT, Swenson D, Sacchettini JC, Jacobs WR Jr, Russell DG. Nature 406, 735-8, (2000). View articlePMID: 10963599

5.The glyoxylate cycle is required for fungal virulence. Lorenz MC, Fink GR. Nature 412, 83-6, (2001). View articlePMID: 11452311

6.Crystal structure of Escherichia coli malate synthase G complexed with magnesium and glyoxylate at 2.0 A resolution: mechanistic implications. Howard BR, Endrizzi JA, Remington SJ. Biochemistry 39, 3156-68, (2000). View articlePMID: 10715138

7.Atomic resolution structures of Escherichia coli and Bacillus anthracis malate synthase A: comparison with isoform G and implications for structure-based drug discovery. Lohman JR, Olson AC, Remington SJ. Protein Sci. 17, 1935-45, (2008). View articlePMID: 18714089

8.Refined solution structure of the 82-kDa enzyme malate synthase G from joint NMR and synchrotron SAXS restraints. Grishaev A, Tugarinov V, Kay LE, Trewhella J, Bax A. J. Biomol. NMR 40, 95-106, (2008). View articlePMID: 18008171

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