Global InformationMolybdopterin molybdotransferase information
| Molybdopterin molybdotransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.10.1.1 | ||||||||
| 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 molybdotransferase (EC 2.10.1.1, MoeA, Cnx1) is an enzyme with systematic name adenylyl-molybdopterin:molybdate molybdate transferase (AMP-forming).[1][2][3] This enzyme catalyses the following chemical reaction
- adenylyl-molybdopterin + molybdate molybdenum cofactor + AMP
Catalyses the insertion of molybdenum into the ene-dithiol group of molybdopterin.
- ^ Nichols JD, Rajagopalan KV (March 2005). "In vitro molybdenum ligation to molybdopterin using purified components". The Journal of Biological Chemistry. 280 (9): 7817–22. doi:10.1074/jbc.M413783200. PMID 15632135.
- ^ Nichols JD, Xiang S, Schindelin H, Rajagopalan KV (January 2007). "Mutational analysis of Escherichia coli MoeA: two functional activities map to the active site cleft". Biochemistry. 46 (1): 78–86. doi:10.1021/bi061551q. PMC 1868504. PMID 17198377.
- ^ Llamas A, Otte T, Multhaup G, Mendel RR, Schwarz G (July 2006). "The Mechanism of nucleotide-assisted molybdenum insertion into molybdopterin. A novel route toward metal cofactor assembly". The Journal of Biological Chemistry. 281 (27): 18343–50. doi:10.1074/jbc.M601415200. PMID 16636046.