| EC |
2.7.7.80 |
| Accepted name: |
molybdopterin-synthase adenylyltransferase |
| Reaction: |
ATP + [molybdopterin-synthase sulfur-carrier protein]-Gly-Gly = diphosphate + [molybdopterin-synthase sulfur-carrier protein]-Gly-Gly-AMP |
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For diagram of MoCo biosynthesis, click here |
| Glossary: |
small subunit of the molybdopterin synthase = molybdopterin-synthase sulfur-carrier protein = MoaD |
| Other name(s): |
MoeB; adenylyltransferase and sulfurtransferase MOCS3 |
| Systematic name: |
ATP:molybdopterin-synthase adenylyltransferase |
| Comments: |
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 small subunit. 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. |
| Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB |
| References: |
| 1. |
Leimkuhler, S., Wuebbens, M.M. and Rajagopalan, K.V. 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 (2001) 34695–34701. [DOI] [PMID: 11463785] |
| 2. |
Matthies, A., Nimtz, M. and Leimkuhler, S. Molybdenum cofactor biosynthesis in humans: identification of a persulfide group in the rhodanese-like domain of MOCS3 by mass spectrometry. Biochemistry 44 (2005) 7912–7920. [DOI] [PMID: 15910006] |
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| [EC 2.7.7.80 created 2011] |
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