Metabolic Modeling Tutorial
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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
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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:
phosphopantetheine adenylyltransferase Inferred from experiment : coaD ( Escherichia coli K-12 substr. MG1655 )
bifunctional coenzyme A synthase Inferred from experiment : COASY ( Homo sapiens )
pantetheine-phosphate adenylyltransferase Inferred from experiment : CAB4 ( Saccharomyces cerevisiae )
4'-phosphopantetheine adenylyltransferase Inferred from experiment : AtCoaD ( Arabidopsis thaliana col )

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, Martin93a, NOVELLI53, HOAGLAND54, Izard99]

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."

Martin93a: 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 18.5 on Thu Dec 18, 2014, BIOCYC14B.