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MetaCyc Reaction:

Superclasses: Reactions Classified By Conversion TypeSimple ReactionsChemical ReactionsProtein-Modification Reactions
Reactions Classified By SubstrateMacromolecule ReactionsProtein-ReactionsProtein-Modification Reactions

EC Number:

Enzymes and Genes:

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

In Pathway: molybdenum cofactor biosynthesis

The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the Enzyme Commission system.

Most BioCyc compounds have been protonated to a reference pH value of 7.3. 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): -168.60596Inferred 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 C-terminal domain.

Citations: [Leimkuhler01a, Matthies05]

Gene-Reaction Schematic

Gene-Reaction Schematic

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

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


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 Pathway Tools version 19.5 (software by SRI International) on Sun May 1, 2016, biocyc14.