|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: 188.8.131.52
Enzymes and Genes:
|Escherichia coli K-12 substr. MG1655:||molybdopterin-synthase adenylyltransferase: 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): -168.60596 [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 184.108.40.206) C-terminal domain.
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
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