5-metiltetrahidropteroiltriglutamat—homocistein S-metiltransferaza
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
| 5-metiltetrahidropteroiltriglutamat—homocistein S-metiltransferaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 2.1.1.14 | ||||||||
| CAS broj | 9068-29-5 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
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- 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 uredi
- ↑ 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 uredi
- Nicholas C. Price, Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third izd.). USA: Oxford University Press. ISBN 019850229X.
- Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 izd.). 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 izd.). Wiley Classics Library. ISBN 0471303097.
- Robert A. Copeland (2013). Evaluation of Enzyme Inhibitors in Drug Discovery: A Guide for Medicinal Chemists and Pharmacologists (2nd izd.). Wiley-Interscience. ISBN 111848813X.
- Gerhard Michal, Dietmar Schomburg (2012). Biochemical Pathways: An Atlas of Biochemistry and Molecular Biology (2nd izd.). Wiley. ISBN 0470146842.