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MetaCyc Reaction: 2.7.7.3

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions
Reactions Classified By Substrate Small-Molecule Reactions

EC Number: 2.7.7.3

Enzymes and Genes:

Arabidopsis thaliana col : 4'-phosphopantetheine adenylyltransferase Inferred from experiment : AtCoaD
Escherichia coli K-12 substr. MG1655 : phosphopantetheine adenylyltransferase Inferred from experiment : coaD
Homo sapiens : bifunctional coenzyme A synthase Inferred from experiment : COASY
Saccharomyces cerevisiae : pantetheine-phosphate adenylyltransferase Inferred from experiment : CAB4

In Pathway: coenzyme A biosynthesis I , coenzyme A biosynthesis II (mammalian)

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 Inferred by computational analysis [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 2.3.1.157, glucosamine-1-phosphate N-acetyltransferase.

Citations: [Geerlof99, Martin93, NOVELLI53, HOAGLAND54, Izard99]

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

Unification Links: KEGG:R03035 , Rhea:19801

Relationship Links: BRENDA:EC:2.7.7.3 , ENZYME:EC:2.7.7.3 , IUBMB-ExplorEnz:EC:2.7.7.3


References

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

HOAGLAND54: 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

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

Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

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

NOVELLI53: NOVELLI GD (1953). "Enzymatic synthesis and structure of CoA." Fed Proc 12(3);675-81. PMID: 13107738


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 19.0 on Tue Aug 4, 2015, BIOCYC14B.