Molybdopterin-synthase adenylyltransferase
| Molybdopterin-synthase adenylyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.7.7.80 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Molybdopterin-synthase adenylyltransferase (EC 2.7.7.80, MoeB, adenylyltransferase and sulfurtransferase MOCS3) is an enzyme with systematic name ATP:molybdopterin-synthase adenylyltransferase.[1][2] This enzyme catalyses the following chemical reaction
- ATP + [molybdopterin-synthase sulfur-carrier protein]-Gly-Gly diphosphate + [molybdopterin-synthase sulfur-carrier protein]-Gly-Gly-AMP
This enzyme adenylates the C-terminus of the small subunit of the molybdopterin synthase.
References
- ^ Leimkühler S, Wuebbens MM, Rajagopalan KV (September 2001). "Characterization of Escherichia coli MoeB and its involvement in the activation of molybdopterin synthase for the biosynthesis of the molybdenum cofactor". The Journal of Biological Chemistry. 276 (37): 34695–701. doi:10.1074/jbc.M102787200. PMID 11463785.
- ^ Matthies A, Nimtz M, Leimkühler S (May 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. doi:10.1021/bi0503448. PMID 15910006.
External links
- Molybdopterin-synthase+adenylyltransferase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
