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PMID:23251906

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Citation

Grabowski, M, Banasiuk, R, Węgrzyn, A, Kędzierska, B, Lica, J, Banecka-Majkutewicz, Z and Banecki, B (2012) Role of heat-shock proteins and cobalamine in maintaining methionine synthase activity. Acta Biochim. Pol. 59:489-93

Abstract

Atheromatous plaque is one of the most common cardiovascular-related diseases. Reports show a connection between its development and the levels of homocysteine. In pathological states high levels of homocysteine in the organism can be caused by the malfunction of the methionine synthase pathway. Bacterial methionine synthase (MetH) is a homologue of the human methionine syntase (MS). In this study we aimed to investigate the functional relations between MetH and its cofactor--cobalamine--under stress conditions. We have demonstrated that heat shock proteins (Hsp 70/100 system or HtpG) can protect MetH activity under stress conditions. Moreover, in the presence of cobalamine they can restore the activity of partially denatured methionine synthase.

Links

PubMed

Keywords

5-Methyltetrahydrofolate-Homocysteine S-Methyltransferase/chemistry; 5-Methyltetrahydrofolate-Homocysteine S-Methyltransferase/metabolism; Heat-Shock Proteins/chemistry; Heat-Shock Proteins/metabolism; Homocysteine/chemistry; Homocysteine/metabolism; Humans; Kinetics; Metabolic Networks and Pathways; Methionine/biosynthesis; Methylation; Plaque, Atherosclerotic/enzymology; Plaque, Atherosclerotic/metabolism; Vitamin B 12/metabolism

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

ECOLI:METH

enables

GO:0031419: cobalamin binding

ECO:0000314: direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

ECOLI:METH

enables

GO:0008705: methionine synthase activity

ECO:0000314: direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

Notes

See also

References

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