|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions|
|Reactions Classified By Substrate → Small-Molecule Reactions|
EC Number: 18.104.22.168
Enzymes and Genes:
|Arabidopsis thaliana col :||4'-phosphopantetheine adenylyltransferase
|Escherichia coli K-12 substr. MG1655 :||phosphopantetheine adenylyltransferase
|Homo sapiens :||bifunctional coenzyme A synthase
|Saccharomyces cerevisiae :||pantetheine-phosphate adenylyltransferase
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.
Most BioCyc compounds have been protonated to a reference pH value of 7.3, and some reactions have been computationally balanced for hydrogen by adding free protons. Please see the PGDB Concepts Guide for more information.
Mass balance status: Balanced.
Enzyme Commission Primary Name: pantetheine-phosphate adenylyltransferase
Enzyme Commission Synonyms: dephospho-CoA pyrophosphorylase, pantetheine phosphate adenylyltransferase, dephospho-coenzyme A pyrophosphorylase, 3'-dephospho-CoA pyrophosphorylase
Standard Gibbs Free Energy (ΔrG'° in kcal/mol): -54.05249 [Latendresse13]
Enzyme Commission Summary:
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 22.214.171.124, glucosamine-1-phosphate N-acetyltransferase.
Geerlof99: Geerlof A, Lewendon A, Shaw WV (1999). "Purification and characterization of phosphopantetheine adenylyltransferase from Escherichia coli." J Biol Chem 1999;274(38);27105-11. PMID: 10480925
Izard99: Izard T, Geerlof A, Lewendon A, Barker JJ (1999). "Cubic crystals of phosphopantetheine adenylyltransferase from Escherichia coli." Acta Crystallogr D Biol Crystallogr 1999;55 ( Pt 6);1226-8. PMID: 10329792
Martin93: 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. PMID: 8389542
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