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
| 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 | ||||||||
| |||||||||
This enzyme catalyses an early step in the biosynthesis of molybdopterin.
References edit
- ^ Rieder C, Eisenreich W, O'Brien J, Richter G, Götze E, Boyle P, Blanchard S, Bacher A, Simon H (July 1998). "Rearrangement reactions in the biosynthesis of molybdopterin--an NMR study with multiply 13C/15N labelled precursors". European Journal of Biochemistry. 255 (1): 24–36. doi:10.1046/j.1432-1327.1998.2550024.x. PMID 9692897.
- ^ Wuebbens MM, Rajagopalan KV (January 1995). "Investigation of the early steps of molybdopterin biosynthesis in Escherichia coli through the use of in vivo labeling studies". The Journal of Biological Chemistry. 270 (3): 1082–7. doi:10.1074/jbc.270.3.1082. PMID 7836363.
- ^ Hänzelmann P, Hernández HL, Menzel C, García-Serres R, Huynh BH, Johnson MK, Mendel RR, Schindelin H (August 2004). "Characterization of MOCS1A, an oxygen-sensitive iron-sulfur protein involved in human molybdenum cofactor biosynthesis". The Journal of Biological Chemistry. 279 (33): 34721–32. doi:10.1074/jbc.M313398200. PMID 15180982.
- ^ Hänzelmann P, Schindelin H (August 2004). "Crystal structure of the S-adenosylmethionine-dependent enzyme MoaA and its implications for molybdenum cofactor deficiency in humans". Proceedings of the National Academy of Sciences of the United States of America. 101 (35): 12870–5. doi:10.1073/pnas.0404624101. PMC 516487. PMID 15317939.
- ^ Sanishvili R, Beasley S, Skarina T, Glesne D, Joachimiak A, Edwards A, Savchenko A (October 2004). "The crystal structure of Escherichia coli MoaB suggests a probable role in molybdenum cofactor synthesis". The Journal of Biological Chemistry. 279 (40): 42139–46. doi:10.1074/jbc.M407694200. PMC 3366512. PMID 15269205.
- ^ Hänzelmann P, Schindelin H (May 2006). "Binding of 5'-GTP to the C-terminal FeS cluster of the radical S-adenosylmethionine enzyme MoaA provides insights into its mechanism". Proceedings of the National Academy of Sciences of the United States of America. 103 (18): 6829–34. doi:10.1073/pnas.0510711103. PMC 1458979. PMID 16632608.
- ^ Lees NS, Hänzelmann P, Hernandez HL, Subramanian S, Schindelin H, Johnson MK, Hoffman BM (July 2009). "ENDOR spectroscopy shows that guanine N1 binds to [4Fe-4S] cluster II of the S-adenosylmethionine-dependent enzyme MoaA: mechanistic implications". Journal of the American Chemical Society. 131 (26): 9184–5. doi:10.1021/ja903978u. PMC 2757093. PMID 19566093.
External links edit
- Cyclic+pyranopterin+monophosphate+synthase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
