|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: 184.108.40.206
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 [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 220.127.116.11) C-terminal domain.
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
©2014 SRI International, 333 Ravenswood Avenue, Menlo Park, CA 94025-3493