Role of heat-shock proteins and cobalamine in maintaining methionine synthase activity. | Zendy

Michał Grabowski | Zendy; Rafał Banasiuk | Zendy; Alicja Węgrzyn | Zendy; Barbara Kędzierska | Zendy; Jan Jakub Lica | Zendy; Zyta Banecka-Majkutewicz | Zendy; Bogdan Banecki | Zendy

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Role of heat-shock proteins and cobalamine in maintaining methionine synthase activity.

Author(s) -

Michał Grabowski,

Rafał Banasiuk,

Alicja Węgrzyn,

Barbara Kędzierska,

Jan Jakub Lica,

Zyta Banecka-Majkutewicz,

Bogdan Banecki

Publication year - 2012

Publication title -

acta biochimica polonica

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.452

H-Index - 78

eISSN - 1734-154X

pISSN - 0001-527X

DOI - 10.18388/abp.2012_2082

Subject(s) - methionine synthase , methionine , meth , homocysteine , heat shock protein , atp synthase , cofactor , chemistry , biochemistry , microbiology and biotechnology , enzyme , pathological , biology , amino acid , medicine , gene , monomer , organic chemistry , acrylate , polymer

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.

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