Abstract
The final two enzymes in the CoA biosynthetic pathway, phosphopantetheine adenylyltransferase (PPAT; EC 2.7.7.3) and dephospho-CoA kinase (DPCK; EC 2.7.1.24), are separate proteins in prokaryotes, but exist as a bifunctional enzyme in pig liver. In the present study we have obtained sequence information from purified pig-liver enzyme, and identified the corresponding cDNA in a number of species. The human gene localizes to chromosome 17q12-21 and contains regions with sequence similarity to the monofunctional Escherichia coli DPCK and PPAT. The recombinant 564-amino-acid human protein confirmed the associated transferase and kinase activities, and gave similar kinetic properties to the wild-type pig enzyme.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Base Sequence
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Chromosome Mapping
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Chromosomes, Human, Pair 17 / genetics
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Cloning, Molecular
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DNA, Complementary / genetics
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Escherichia coli / enzymology
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Escherichia coli / genetics
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Gene Expression
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Humans
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Kinetics
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Liver / enzymology
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Molecular Sequence Data
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Nucleotidyltransferases / genetics*
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Nucleotidyltransferases / metabolism
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Phosphotransferases (Alcohol Group Acceptor) / genetics*
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Phosphotransferases (Alcohol Group Acceptor) / metabolism
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Recombinant Proteins / genetics
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Recombinant Proteins / metabolism
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Sequence Homology, Amino Acid
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Swine
Substances
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DNA, Complementary
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Recombinant Proteins
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Phosphotransferases (Alcohol Group Acceptor)
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dephospho-CoA kinase
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Nucleotidyltransferases
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pantetheine-phosphate adenylyltransferase
Associated data
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GENBANK/AY094602
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GENBANK/AY094603