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
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 ${\displaystyle \rightleftharpoons }$ cyclic pyranopterin monophosphate + diphosphate

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

References

1. 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.
2. 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.
3. 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.
4. 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. Bibcode:2004PNAS..10112870H. doi: 10.1073/pnas.0404624101 . PMC   516487 . PMID   15317939.
5. 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.
6. 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. Bibcode:2006PNAS..103.6829H. doi: 10.1073/pnas.0510711103 . PMC   1458979 . PMID   16632608.
7. 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

• Cyclic+pyranopterin+monophosphate+synthase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)