Stereochemical studies on phosphopantothenoylcysteine decarboxylase from Escherichia coli. Academic Article

abstract

• Phosphopantothenoylcysteine decarboxylase catalyzes the decarboxylation of 4'-phosphopantothenoylcysteine (2) to form 4'-phosphopanthetheine (3), an intermediate in the biosynthesis of Coenzyme A. In this study we investigated the stereochemistry of this reaction. Our results show that the decarboxylation proceeds with retention of stereochemistry, and that the pro-R proton at C(beta) of the cysteine moiety of 2 is removed during a reversible oxidation of the thiol to a thioaldehyde intermediate.

authors

• Begley, Tadhg

published proceedings

• Bioorg Med Chem Lett

author list (cited authors)

• Strauss, E., & Begley, T. P.

citation count

• 17

complete list of authors

• Strauss, Erick||Begley, Tadhg P

publication date

• January 2003

publisher

• Elsevier  Publisher

published in

• Bioorganic and Medicinal Chemistry Letters  Journal

keywords

• Binding Sites
• Carboxy-Lyases
• Coenzyme A
• Escherichia Coli
• Magnetic Resonance Spectroscopy
• Oxidation-Reduction
• Protein Conformation
• Stereoisomerism

PubMed Central ID

• 12565925

Digital Object Identifier (DOI)

• 10.1016/s0960-894x(02)01018-1

start page

• 339

end page

• 342

volume

• 13

issue

• 3

URL

• http%3A%2F%2Fdx.doi.org%2F10.1016%2Fs0960-894x%2802%2901018-1