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

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. and 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. and 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. Hänzelmann, P., Hernandez, H.L., Menzel, C., Garcia-Serres, R., Huynh, B.H., Johnson, M.K., Mendel, R.R. and 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. Hänzelmann, P. and 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. and 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. Hänzelmann, P. and 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., Hänzelmann, P., Hernandez, H.L., Subramanian, S., Schindelin, H., Johnson, M.K. and 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

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