The Enzyme Database

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EC 2.7.7.3     
Accepted name: pantetheine-phosphate adenylyltransferase
Reaction: ATP + pantetheine 4′-phosphate = diphosphate + 3′-dephospho-CoA
For diagram of the late stages of CoA biosynthesis, click here
Other name(s): dephospho-CoA pyrophosphorylase; pantetheine phosphate adenylyltransferase; dephospho-coenzyme A pyrophosphorylase; 3′-dephospho-CoA pyrophosphorylase
Systematic name: ATP:pantetheine-4′-phosphate adenylyltransferase
Comments: The enzyme from several bacteria (e.g. Escherichia coli, Bacillus subtilis and Haemophilus influenzae) has been shown to be bifunctional and also to possess the activity of EC 2.3.1.157, glucosamine-1-phosphate N-acetyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9026-99-7
References:
1.  Hoagland, M.B. and Novelli, G.D. Biosynthesis of coenzyme A from phosphopantetheine and pantetheine from pantothenate. J. Biol. Chem. 207 (1954) 767–773. [PMID: 13163064]
2.  Novelli, G.D. Enzymatic synthesis and structure of CoA. Fed. Proc. 12 (1953) 675–682. [PMID: 13107738]
3.  Martin, D.P. and Drueckhammer, D.G. Separate enzymes catalyze the final two steps of coenzyme A biosynthesis in Brevibacterium ammoniagenes: purification of pantetheine phosphate adenylyltransferase. Biochem. Biophys. Res. Commun. 192 (1993) 1155–1161. [PMID: 8389542]
4.  Geerlof, A., Lewendon, A. and Shaw, W.V. Purification and characterization of phosphopantetheine adenylyltransferase from Escherichia coli. J. Biol. Chem. 274 (1999) 27105–27111. [PMID: 10480925]
5.  Izard, T., Geerlof, A., Lewendon, A. and Barker, J.J. Cubic crystals of phosphopantetheine adenylyltransferase from Escherichia coli. Acta Crystallogr. D Biol. Crystallogr. 55 (1999) 1226–1228. [PMID: 10329792]
[EC 2.7.7.3 created 1961, modified 2002]
 
 


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