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  Characterization and redox regulation of Plasmodium falciparum methionine adenosyltransferase

Pretzel, J., Gehr, M., Eisenkolb, M., Wang, L., Fritz-Wolf, K., Rahlfs, S., et al. (2016). Characterization and redox regulation of Plasmodium falciparum methionine adenosyltransferase. The Journal of Biochemistry, 160(6), 355-367. doi:10.1093/jb/mvw045.

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Item Permalink: https://hdl.handle.net/11858/00-001M-0000-002C-01A1-D Version Permalink: https://hdl.handle.net/11858/00-001M-0000-002C-AEE6-7
Genre: Journal Article

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 Creators:
Pretzel, Jette, Author
Gehr, Marina, Author
Eisenkolb, Maike, Author
Wang, Lihui, Author
Fritz-Wolf, Karin1, Author           
Rahlfs, Stefan, Author
Becker, Katja, Author
Jortzik, Esther, Author
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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Free keywords: malaria parasites / redox regulation / S-adenosylmethionine / S-glutathionylation / S-nitrosylation
 Abstract: As a methyl group donor for biochemical reactions, S-adenosylmethionine plays a central metabolic role in most organisms. Depletion of S-adenosylmethionine has downstream effects on polyamine metabolism and methylation reactions, and is an effective way to combat pathogenic microorganisms such as malaria parasites. Inhibition of both the methylation cycle and polyamine synthesis strongly affects Plasmodium falciparum growth. Despite its central position in the methylation cycle, not much is currently known about P. falciparum methionine adenosyltransferase (PfalMAT). Notably, however, PfalMAT has been discussed as a target of different redox regulatory modifications. Modulating the redox state of critical cysteine residues is a way to regulate enzyme activity in different pathways in response to changes in the cellular redox state. In the present study, we optimized an assay for detailed characterization of enzymatic activity and redox regulation of PfalMAT. While the presence of reduced thioredoxin increases the activity of the enzyme, it was found to be inhibited upon S-glutathionylation and S-nitrosylation. A homology model and site-directed mutagenesis studies revealed a contribution of the residues Cys52, Cys113 and Cys187 to redox regulation of PfalMAT by influencing its structure and activity. This phenomenon connects cellular S-adenosylmethionine synthesis to the redox state of PfalMAT and therefore to the cellular redox homeostasis.

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Language(s): eng - English
 Dates: 2016-05-242016-06-142016-07-272016-12-01
 Publication Status: Issued
 Pages: 13
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1093/jb/mvw045
URI: https://www.ncbi.nlm.nih.gov/pubmed/27466371
 Degree: -

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Title: The Journal of Biochemistry
Source Genre: Journal
 Creator(s):
Japanese Biochemical Society, Editor              
Affiliations:
-
Publ. Info: Oxford : Oxford Univ. P
Pages: - Volume / Issue: 160 (6) Sequence Number: - Start / End Page: 355 - 367 Identifier: ISSN: 0021-924X
ISSN: 1756-2651