Cyclic pyranopterin monophosphate synthase
| Cyclic pyranopterin monophosphate synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 4.1.99.18 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Cyclic pyranopterin monophosphate synthase (EC 4.1.99.18, MOCS1A, MoaA, MoaC, molybdenum cofactor biosynthesis protein 1) is an enzyme with systematic name GTP 8,9-lyase (cyclic pyranopterin monophosphate-forming).[1][2][3][4][5][6][7] This enzyme catalyses the following chemical reaction
- GTP cyclic pyranopterin monophosphate + diphosphate
This enzyme catalyses an early step in the biosynthesis of the molybdenum cofactor.
References
- ^ Rieder, C.; Eisenreich, W.; O'Brien, J.; Richter, G.; Götze, E.; Boyle, P.; Blanchard, S.; Bacher, A.; Simon, H. (1998). "Rearrangement reactions in the biosynthesis of molybdopterin - an NMR study with multiply 13C/15N labelled precursors". Eur. J. Biochem. 255 (1): 24–36. doi:10.1046/j.1432-1327.1998.2550024.x. PMID 9692897.
- ^ Wuebbens, M.M.; Rajagopalan, K.V. (1995). "Investigation of the early steps of molybdopterin biosynthesis in Escherichia coli through the use of in vivo labeling studies". J. Biol. Chem. 270 (3): 1082–1087. doi:10.1074/jbc.270.3.1082. PMID 7836363.
{{cite journal}}: CS1 maint: unflagged free DOI (link) - ^ Götze, P.; Hernandez, H.L.; Menzel, C.; Garcia-Serres, R.; Huynh, B.H.; Johnson, M.K.; Mendel, R.R.; Schindelin, H. (2004). "Characterization of MOCS1A, an oxygen-sensitive iron-sulfur protein involved in human molybdenum cofactor biosynthesis". J. Biol. Chem. 279: 34721–34732. doi:10.1074/jbc.M313398200. PMID 15180982.
{{cite journal}}: CS1 maint: unflagged free DOI (link) - ^ Götze, P.; Schindelin, H. (2004). "Crystal structure of the S-adenosylmethionine-dependent enzyme MoaA and its implications for molybdenum cofactor deficiency in humans". Proc. Natl. Acad. Sci. USA. 101: 12870–12875. doi:10.1073/pnas.0404624101. PMID 15317939.
- ^ Sanishvili, R.; Beasley, S.; Skarina, T.; Glesne, D.; Joachimiak, A.; Edwards, A.; Savchenko, A. (2004). "The crystal structure of Escherichia coli MoaB suggests a probable role in molybdenum cofactor synthesis". J. Biol. Chem. 279: 42139–42146. doi:10.1074/jbc.M407694200. PMID 15269205.
{{cite journal}}: CS1 maint: unflagged free DOI (link) - ^ Götze, P.; Schindelin, H. (2006). "Binding of 5′-GTP to the C-terminal FeS cluster of the radical S-adenosylmethionine enzyme MoaA provides insights into its mechanism". Proc. Natl. Acad. Sci. USA. 103: 6829–6834. doi:10.1073/pnas.0510711103. PMID 16632608.
- ^ Lees, N.S.; Götze, P.; Hernandez, H.L.; Subramanian, S.; Schindelin, H.; Johnson, M.K.; Hoffman, B.M. (2009). "ENDOR spectroscopy shows that guanine N1 binds to [4Fe-4S] cluster II of the S-adenosylmethionine-dependent enzyme MoaA: mechanistic implications". J. Am. Chem. Soc. 131: 9184–9185. doi:10.1021/ja903978u. PMID 19566093.
External links
- Cyclic+pyranopterin+monophosphate+synthase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)