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- W46757834 abstract "Proteins contain a limited range of functional groups that can be used for enzymatic catalysis. These include acids, bases, simple nucleophiles, and electrophiles. Redox chemistry is limited, with rare exceptions, to the thiol group of cysteine. These functional groups are inadequate for the efficient catalysis of many reactions in living systems and cells have evolved a set of small molecules, called cofactors, that bind at the active site and augment the catalytic potential of the enzyme. Many of these cofactors are biosynthesized from vitamins, so called because of the essential roles that they play in the human diet. This article will provide a summary of the biosynthesis of the major cofactors in bacteria. We will divide these into three groups: (1) carrier cofactors (coenzyme A, biotin, lipoic acid, and folate), (2) metabolite-activating cofactors (thiamin, PLP, and adenosyl cobalamin), and (3) redox cofactors (NAD, menaquinone, ubiquinone, flavin, molybdopterin, and heme). For each cofactor, we will give a brief description of its biochemical function followed by a schematic description of the biosynthesis pathway. Where possible, we include the KEGG reference and indicate when a comprehensive analysis of the comparative genomics of the cofactor is available in ‘The SEED’ database." @default.
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- W46757834 date "2009-01-01" @default.
- W46757834 modified "2023-09-26" @default.
- W46757834 title "Coenzyme and Prosthetic Group Biosynthesis" @default.
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- W46757834 doi "https://doi.org/10.1016/b978-012373944-5.00069-9" @default.
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