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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:

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

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.

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: molybdopterin-synthase adenylyltransferase

Enzyme Commission Synonyms: MoeB, adenylyltransferase and sulfurtransferase MOCS3

Standard Gibbs Free Energy (ΔrG in kcal/mol): -168.60596 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: [Leimkuhler01, Matthies05]

Gene-Reaction Schematic: ?

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."

Leimkuhler01: 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 19.0 on Fri Jul 3, 2015, biocyc11.