The biosynthesis of coenzyme A in bacteria. Academic Article

abstract

• Coenzyme A (I) and enzyme-bound phosphopantetheine (II) function as acyl carriers and as carbonyl activating groups for Claisen reactions as well as for amide-, ester-, and thioester-forming reactions in the cell. In so doing, these cofactors play a key role in the biosynthesis and breakdown of fatty acids and in the biosynthesis of polyketides and nonribosomal peptides. Coenzyme A is biosynthesized in bacteria in nine steps. The biosynthesis begins with the decarboxylation of aspartate to give beta-alanine. Pantoic acid is formed by the hydroxymethylation of alpha-ketoisovalerate followed by reduction. These intermediates are then condensed to give pantothenic acid. Phosphorylation of pantothenic acid followed by condensation with cysteine and decarboxylation gives 4'-phosphopantetheine. Adenylation and phosphorylation of 4'-phosphopantetheine completes the biosynthesis of coenzyme A. This review will focus on the mechanistic enzymology of coenzyme A biosynthesis in bacteria.

authors

• Begley, Tadhg

published proceedings

• Vitam Horm

altmetric score

• 3

author list (cited authors)

• Begley, T. P., Kinsland, C., & Strauss, E.

citation count

• 158

complete list of authors

• Begley, TP||Kinsland, C||Strauss, E

publication date

• January 2001

publisher

• Elsevier  Publisher

published in

• Vitamins and Hormones: Advances in Research and Applications  Journal

keywords

• Coenzyme A
• Decarboxylation
• Escherichia Coli
• Humans
• Oxidation-Reduction
• Pantothenic Acid
• Saccharomyces Cerevisiae

PubMed Central ID

• 11153265

Digital Object Identifier (DOI)

• 10.1016/s0083-6729(01)61005-7

start page

• 157

end page

• 171

volume

• 61

URL

• http%3A%2F%2Fdx.doi.org%2F10.1016%2Fs0083-6729%2801%2961005-7