Cloning, expression, and characterization of a human 4'-phosphopantetheinyl transferase with broad substrate specificity.

摘要: A single candidate 4′-phosphopantetheine transferase, identified by BLAST searches of the human genome sequence data base, has been cloned, expressed, and characterized. The enzyme, which is expressed mainly in cytosolic compartment a wide range tissues, 329-residue, monomeric protein. enzyme capable transferring moiety coenzyme to conserved serine residue both acyl carrier protein domain multifunctional fatty acid synthase associated independently with mitochondria. transferase also phosphopantetheinylation peptidyl proteins from prokaryotes. same recently implicated α-aminoadipate semialdehyde dehydrogenase involved lysine catabolism (Praphanphoj, V., Sacksteder, K. A., Gould, S. J., Thomas, G. H., Geraghty, M. T. (2001) Mol. Genet. Metab. 72, 336–342). Thus, contrast yeast, utilizes separate transferases service each three different substrates, humans appear utilize single, broad specificity for all posttranslational 4′-phosphopantetheinylation reactions.