Ciklična piranopterin monofosfatna sintaza
Ciklična piranopterin monofosfatna sintaza (EC 4.1.99.18, MOCS1A, MoaA, MoaC, molibdenum kofaktor biosinteza protein 1) je enzim sa sistematskim imenom GTP 8,9-lijaza (formira ciklična piranopterin monofosfat).[1][2][3][4][5][6][7] Ovaj enzim katalizuje sledeću hemijsku reakciju
| Ciklična piranopterin monofosfatna sintaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 4.1.99.18 | ||||||||
| Baze podataka | |||||||||
| IntEnz | IntEnz pregled | ||||||||
| BRENDA | BRENDA pristup | ||||||||
| ExPASy | NiceZyme pregled | ||||||||
| KEGG | KEGG pristup | ||||||||
| MetaCyc | metabolički put | ||||||||
| PRIAM | profil | ||||||||
| Strukture PBP | RCSB PDB PDBe PDBj PDBsum | ||||||||
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- GTP ciklični piranopterin monofosfat + difosfat
Ovaj enzim katalizuje jedan od ranih kraka biosinteze molibdenum kofaktora (MoCo).
Reference уреди
- ^ 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: 24—36. PMID 9692897.
- ^ 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: 1082—1087. PMID 7836363.
- ^ 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. PMID 15180982.
- ^ 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. PMID 15317939.
- ^ 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. PMID 15269205.
- ^ 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. PMID 16632608.
- ^ 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. PMID 19566093.
Literatura уреди
- Nicholas C. Price; Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third изд.). USA: Oxford University Press. ISBN 019850229X.
- Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 изд.). Wiley-Interscience. ISBN 0471205036.
- Branden C; Tooze J. Introduction to Protein Structure. New York, NY: Garland Publishing. ISBN 0-8153-2305-0.
- Irwin H. Segel. Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems (Book 44 изд.). Wiley Classics Library. ISBN 0471303097.
- William P. Jencks (1987). Catalysis in Chemistry and Enzymology. Dover Publications. ISBN 0486654605.
Spoljašnje veze уреди
- Cyclic+pyranopterin+monophosphate+synthase на US National Library of Medicine Medical Subject Headings (MeSH)