Tetrahidrofolatna sintaza
Tetrahidrofolatna sintaza (EC 6.3.2.17, folilpoliglutamatna sintaza, folat poliglutamatna sintetaza, formiltetrahidropteroildiglutamatna sintetaza, N10-formiltetrahidropteroildiglutamat sintetaza, folilpoli-gama-glutamatna sintaza, folilpoliglutamil sintetaza, folilpoli(gama-glutamat) sintaza, folilpoliglutamatna sintetaza, folilpoli-gama-glutamat sintetaza-dihidrofolatna sintetaza, FPGS, tetrahidrofolilpoliglutamat sintaza, tetrahidrofolat:L-glutamat gama-ligaza (formira ADP), tetrahidropteroil-(gama-Glu)n:L-glutamat gama-ligaza (formira ADP)) je enzim sa sistematskim imenom tetrahidropteroil-gama-poliglutamat:L-glutamat gama-ligaza (formira ADP).[1][2][3][4][5][6] Ovaj enzim katalizuje sledeću hemijsku reakciju
| Tetrahidrofolatna sintaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 6.3.2.17 | ||||||||
| CAS broj | 63363-84-8 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
Kod pojedinih bakterija, isti protein katalizuje ovu reakciju i reakciju enzima EC 6.3.2.12.
Reference uredi
- ↑ Cichowicz, D., Foo, S.K. and Shane, B. (1981). „Folylpoly-γ-glutamate synthesis by bacteria and mammalian cells”. Mol. Cell. Biochem. 39: 209-228. PMID 6458762.
- ↑ McGuire, J.J. and Bertino, J.R. (1981). „Enzymatic synthesis and function of folylpolyglutamates”. Mol. Cell. Biochem. 38: 19-48. PMID 7027025.
- ↑ Bognar, A.L., Osborne, C., Shane, B., Singer, S.C. and Ferone, R. (1985). „Folylpoly-γ-glutamate synthetase-dihydrofolate synthetase. Cloning and high expression of the Escherichia coli folC gene and purification and properties of the gene product”. J. Biol. Chem. 260: 5625-5630. PMID 2985605.
- ↑ Ravanel, S., Cherest, H., Jabrin, S., Grunwald, D., Surdin-Kerjan, Y., Douce, R. and Rébeillé, F. (2001). „Tetrahydrofolate biosynthesis in plants: molecular and functional characterization of dihydrofolate synthetase and three isoforms of folylpolyglutamate synthetase in Arabidopsis thaliana”. Proc. Natl. Acad. Sci. USA 98: 15360-15365. PMID 11752472.
- ↑ Cossins, E.A. and Chen, L. (1997). „Folates and one-carbon metabolism in plants and fungi”. Phytochemistry 45: 437-452. PMID 9190084.
- ↑ Cherest, H., Thomas, D. and Surdin-Kerjan, Y. (2000). „Polyglutamylation of folate coenzymes is necessary for methionine biosynthesis and maintenance of intact mitochondrial genome in Saccharomyces cerevisiae”. J. Biol. Chem. 275: 14056-14063. PMID 10799479.
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.