Biology:Cyclic pyranopterin monophosphate synthase

From HandWiki
Cyclic pyranopterin monophosphate synthase
Identifiers
EC number4.1.99.18
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB 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 [math]\displaystyle{ \rightleftharpoons }[/math] cyclic pyranopterin monophosphate + diphosphate

This enzyme catalyses an early step in the biosynthesis of molybdopterin.

References

  1. "Rearrangement reactions in the biosynthesis of molybdopterin--an NMR study with multiply 13C/15N labelled precursors". European Journal of Biochemistry 255 (1): 24–36. July 1998. doi:10.1046/j.1432-1327.1998.2550024.x. PMID 9692897. 
  2. "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. January 1995. doi:10.1074/jbc.270.3.1082. PMID 7836363. 
  3. "Characterization of MOCS1A, an oxygen-sensitive iron-sulfur protein involved in human molybdenum cofactor biosynthesis". The Journal of Biological Chemistry 279 (33): 34721–32. August 2004. doi:10.1074/jbc.M313398200. PMID 15180982. 
  4. "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. August 2004. doi:10.1073/pnas.0404624101. PMID 15317939. 
  5. "The crystal structure of Escherichia coli MoaB suggests a probable role in molybdenum cofactor synthesis". The Journal of Biological Chemistry 279 (40): 42139–46. October 2004. doi:10.1074/jbc.M407694200. PMID 15269205. 
  6. "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. May 2006. doi:10.1073/pnas.0510711103. PMID 16632608. 
  7. "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. July 2009. doi:10.1021/ja903978u. PMID 19566093. 

External links