5-metiltetrahidropteroiltriglutamat—homocistein S-metiltransferaza
| 5-metiltetrahidropteroiltriglutamat—homocistein S-metiltransferaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 2.1.1.14 | ||||||||
| CAS broj | 9068-29-5 | ||||||||
| 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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5-metiltetrahidropteroiltriglutamat—homocistein S-metiltransferaza (EC 2.1.1.14, tetrahidropteroiltriglutamatna metiltransferaza, homocisteinska metilaza, metiltransferaza, tetrahidropteroilglutamat-homocisteinska transmetilaza, metiltetrahidropteroilpoliglutamat:homocistein metiltransferaza, kobalamin-nezavisna metioninska sintaza, metioninska sintaza (kobalamin-nezavisni), METE) je enzim sa sistematskim imenom 5-metiltetrahidropteroiltri-L-glutamat:L-homocistein S-metiltransferaza.[1][2][3][4][5] Ovaj enzim katalizuje sledeću hemijsku reakciju
- S-metiltetrahidropteroiltri-L-glutamat + L-homocistein tetrahidropteroiltri-L-glutamat + L-metionin
Za dejstvo ovog enzima je neophodan fosfat i cink. Enzim iz Escherichia coli takođe koristi redukujući sistem.
Reference
[уреди | уреди извор]- ^ Guest, J.R., Friedman, S., Foster, M.A., Tejerina, G. and Woods, D.D. (1964). „Transfer of the methyl group from N5-methyltetrahydrofolates to homocysteine in Escherichia coli”. Biochem. J. 92: 497—504. PMID 5319972.
- ^ Whitfield, C.D., Steers, E.J., Jr. and Weissbach, H. (1970). „Purification and properties of 5-methyltetrahydropteroyltriglutamate-homocysteine transmethylase”. J. Biol. Chem. 245: 390—401. PMID 4904482.
- ^ Eichel, J., Gonzalez, J.C., Hotze, M., Matthews, R.G. and Schroder, J. (1995). „Vitamin B12-independent methionine synthase from a higher-plant (Catharanthus roseus) - molecular characterization, regulation, heterologous expression, and enzyme properties”. Eur. J. Biochem. 230: 1053—1058. PMID 7601135.
- ^ Gonzalez, J.C., Peariso, K., PennerHahn, J.E. and Matthews, R.G. (1996). „Cobalamin-independent methionine synthase from Escherichia coli: A zinc metalloenzyme”. Biochemistry. 35: 12228—12234. PMID 8823155.
- ^ Peariso, K., Goulding, C.W., Huang, S., Matthews, R.G. and Penner-Hahn, J.E. (1998). „Characterization of the zinc binding site in methionine synthase enzymes of Escherichia coli: The role of zinc in the methylation of homocysteine”. J. Am. Chem. Soc. 120: 8410—8416.
Literatura
[уреди | уреди извор]- 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 | уреди извор]- 5-methyltetrahydropteroyltriglutamate-homocysteine+S-methyltransferase на US National Library of Medicine Medical Subject Headings (MeSH)
