Strauss E, Kinsland C, Ge Y, McLafferty F W, Begley T P
Department of Chemistry and Chemical Biology, Baker Laboratory, Cornell University, Ithaca, New York, 14853, USA.
J Biol Chem. 2001 Apr 27;276(17):13513-6. doi: 10.1074/jbc.C100033200. Epub 2001 Mar 13.
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.
磷酸泛酰巯基乙胺半胱氨酸合酶催化由4'-磷酸泛酰巯基乙胺和L-半胱氨酸形成（R）-4'-磷酸-N-泛酰巯基乙胺：这种参与辅酶A（CoA）生物合成的酶此前尚未被鉴定出来。最近研究表明，细菌中Dfp蛋白的NH2末端结构域催化CoA生物合成的下一步反应，即（R）-4'-磷酸-N-泛酰巯基乙胺脱羧形成4'-磷酸泛酰巯基乙胺（Kupke, T., Uebele, M., Schmid, D., Jung, G., Blaesse, M., and Steinbacher, S. (2000) J. Biol. Chem. 275, 31838 - 31846）。我们已经从大肠杆菌中部分纯化了磷酸泛酰巯基乙胺脱羧酶，并证明dfp基因（此处重新命名为coaBC）编码的蛋白质也具有磷酸泛酰巯基乙胺半胱氨酸合酶活性，使用CTP而非ATP作为活化核苷5'-三磷酸。这一发现完成了对细菌中参与辅酶A生物合成的所有酶的鉴定。
