Phosphopantothenoylcysteine Synthetase from Escherichia coli

Phosphopantothenoylcysteine synthase catalyzes the formation of ( R )-4′-phospho- N -pantothenoylcysteine from 4′-phosphopantothenate and l -cysteine: this enzyme, involved in the biosynthesis of coenzyme A (CoA), has not previously been identified. Recently it was shown that the NH 2 -terminal...

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Published in:The Journal of biological chemistry 2001-04, Vol.276 (17), p.13513-13516
Main Authors: Strauss, Erick, Kinsland, Cynthia, Ge, Ying, McLafferty, Fred W., Begley, Tadhg P.
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container_end_page 13516
container_issue 17
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container_title The Journal of biological chemistry
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creator Strauss, Erick
Kinsland, Cynthia
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Begley, Tadhg P.
description Phosphopantothenoylcysteine synthase catalyzes the formation of ( R )-4′-phospho- N -pantothenoylcysteine from 4′-phosphopantothenate and l -cysteine: this enzyme, involved in the biosynthesis of coenzyme A (CoA), has not previously been identified. Recently it was shown that the NH 2 -terminal domain of the Dfp protein from bacteria catalyzes the next step in CoA biosynthesis, the decarboxylation of ( R )-4′-phospho- N -pantothenoylcysteine to form 4′-phosphopantetheine (Kupke, T., Uebele, M., Schmid, D., Jung, G., Blaesse, M., and Steinbacher, S. (2000) J. Biol. Chem. 275, 31838–31846). We have partially purified phosphopantothenoylcysteine decarboxylase from Escherichia coli and demonstrated that the protein encoded by the dfp gene, here renamed coaBC , also has phosphopantothenoylcysteine synthetase activity, using CTP rather than ATP as the activating nucleoside 5′-triphosphate. This discovery completes the identification of all the enzymes involved in the biosynthesis of coenzyme A in bacteria.
doi_str_mv 10.1074/jbc.C100033200
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title Phosphopantothenoylcysteine Synthetase from Escherichia coli
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