期刊
MOLECULAR BIOSYSTEMS
卷 7, 期 1, 页码 29-37出版社
ROYAL SOC CHEMISTRY
DOI: 10.1039/c005311b
关键词
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资金
- NIH [GM41574]
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R37GM041574, R01GM041574] Funding Source: NIH RePORTER
Redox enzymes which catalyze the oxidation and reduction of substrates are ubiquitous in nature. These enzymes typically possess exogenous cofactors to allow them to perform catalytic functions which cannot be accomplished using only amino acid residues. It is now evident that nature also employs an alternative strategy of generating catalytic and redox-active sites in proteins by posttranslational modification of amino acid residues. This review describes the structures and functions of several of these protein-derived cofactors and the diverse mechanisms of posttranslational modification through which they are generated.
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