Cyclic pyranopterin monophosphate synthase

Cyclic pyranopterin monophosphate synthase
Identifiers
EC number	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
Search PMC articles PubMed articles NCBI proteins

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 $\rightleftharpoons$ cyclic pyranopterin monophosphate + diphosphate

This enzyme catalyses an early step in the biosynthesis of the molybdenum cofactor.

References

1. 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.
2. 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.
3. 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.
4. 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.
5. 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.
6. 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.
7. 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 US National Library of Medicine Medical Subject Headings (MeSH)