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
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
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MetaCyc Reaction: 2.7.7.80

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions Protein-Modification Reactions
Reactions Classified By Substrate Macromolecule Reactions Protein-Reactions Protein-Modification Reactions

EC Number: 2.7.7.80

Enzymes and Genes:
molybdopterin-synthase adenylyltransferase Inferred from experiment : moeB ( Escherichia coli K-12 substr. MG1655 )
MOCS3 adenylyltransferase/sulfurtransferase : MOCS3 ( Homo sapiens )

In Pathway: molybdenum cofactor biosynthesis

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

Mass balance status: The left side is missing: H: 1

Enzyme Commission Primary Name: molybdopterin-synthase adenylyltransferase

Enzyme Commission Synonyms: MoeB, adenylyltransferase and sulfurtransferase MOCS3

Standard Gibbs Free Energy (ΔrG in kcal/mol): -168.17688 Inferred by computational analysis [Latendresse13]

Enzyme Commission Summary:
Adenylates the C-terminus of the small subunit of the molybdopterin synthase. This activation is required to form the thiocarboxylated C-terminus of the active molybdopterin synthase. The reaction occurs in prokaryotes and eukaryotes. The reaction occurs in prokaryotes and eukaryotes. In the human, the reaction is catalysed by the N-terminal domain of the protein MOCS3, which also includes a molybdopterin-synthase sulfurtransferase (EC 2.8.1.11) C-terminal domain.

Citations: [Leimkuhler01a, Matthies05]

Gene-Reaction Schematic: ?

Relationship Links: BRENDA:EC:2.7.7.80 , ENZYME:EC:2.7.7.80 , IUBMB-ExplorEnz:EC:2.7.7.80

Credits:
Created 05-Apr-2010 by Caspi R , SRI International


References

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

Leimkuhler01a: Leimkuhler S, Wuebbens MM, Rajagopalan KV (2001). "Characterization of Escherichia coli MoeB and its involvement in the activation of molybdopterin synthase for the biosynthesis of the molybdenum cofactor." J Biol Chem 276(37);34695-701. PMID: 11463785

Matthies05: Matthies A, Nimtz M, Leimkuhler S (2005). "Molybdenum cofactor biosynthesis in humans: identification of a persulfide group in the rhodanese-like domain of MOCS3 by mass spectrometry." Biochemistry 44(21);7912-20. PMID: 15910006


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 Nov 27, 2014, BIOCYC14B.