Pantetheine-phosphate_adenylyltransferase

Pantetheine-phosphate adenylyltransferase

Pantetheine-phosphate adenylyltransferase

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In enzymology, a pantetheine-phosphate adenylyltransferase (EC 2.7.7.3) is an enzyme that catalyzes the chemical reaction

ATP + 4'-Phosphopantetheine diphosphate + 3'-dephospho-CoA
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Thus, the two substrates of this enzyme are ATP and 4'-Phosphopantetheine, whereas its two products are diphosphate and 3'-dephospho-CoA.

This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is ATP:pantetheine-4'-phosphate adenylyltransferase. Other names in common use include dephospho-CoA pyrophosphorylase, pantetheine phosphate adenylyltransferase, dephospho-coenzyme A pyrophosphorylase, and 3'-dephospho-CoA pyrophosphorylase. This enzyme participates in pantothenate and coa biosynthesis.

Structural studies

As of late 2007, 8 structures have been solved for this class of enzymes, with PDB accession codes 1B6T, 1GN8, 1H1T, 1O6B, 1OD6, 1QJC, 1TFU, and 1VLH.


References

    • HOAGLAND MB, NOVELLI GD (1954). "Biosynthesis of coenzyme A from phospho-pantetheine and of pantetheine from pantothenate". J. Biol. Chem. 207 (2): 767–73. PMID 13163064.
    • NOVELLI GD (1953). "Enzymatic synthesis and structure of CoA". Fed. Proc. 12 (3): 675–81. PMID 13107738.
    • Martin DP, Drueckhammer DG (1993). "Separate enzymes catalyze the final two steps of coenzyme A biosynthesis in Brevibacterium ammoniagenes: purification of pantetheine phosphate adenylyltransferase". Biochem. Biophys. Res. Commun. 192 (3): 1155–61. doi:10.1006/bbrc.1993.1537. PMID 8389542.
    • Geerlof A, Lewendon A, Shaw WV (1999). "Purification and characterization of phosphopantetheine adenylyltransferase from Escherichia coli". J. Biol. Chem. 274 (38): 27105–11. doi:10.1074/jbc.274.38.27105. PMID 10480925.
    • Izard T, Geerlof A, Lewendon A, Barker JJ (1999). "Cubic crystals of phosphopantetheine adenylyltransferase from Escherichia coli". Acta Crystallogr. D. 55 (Pt 6): 1226–8. doi:10.1107/S0907444999004394. PMID 10329792.



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