Glutationska hidrolaza
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| Glutationska hidrolaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 3.4.19.13 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
Glutationska hidrolaza (EC 3.4.19.13, glutationaza, GGT, gama-glutamiltranspeptidaza) je enzim.[1][2][3][4][5][6][7] Ovaj enzim katalizuje sledeću hemijsku reakciju
- glutation + H2O L-cisteinilglicin + L-glutamat
Ovaj protein takođe deluje kao enzim EC 2.3.2.2 (gama-glutamiltransferaza).
Reference[uredi | uredi kod]
- ↑ Hanigan, M.H. and Ricketts, W.A. (1993). „Extracellular glutathione is a source of cysteine for cells that express γ-glutamyl transpeptidase”. Biochemistry 32: 6302-6306. PMID 8099811.
- ↑ Suzuki, H. and Kumagai, H. (2002). „Autocatalytic processing of γ-glutamyltranspeptidase”. J. Biol. Chem. 277: 43536-43543. PMID 12207027.
- ↑ Okada, T., Suzuki, H., Wada, K., Kumagai, H. and Fukuyama, K. (2006). „Crystal structures of γ-glutamyltranspeptidase from Escherichia coli, a key enzyme in glutathione metabolism, and its reaction intermediate”. Proc. Natl. Acad. Sci. USA 103: 6471-6476. PMID 16618936.
- ↑ Boanca, G., Sand, A., Okada, T., Suzuki, H., Kumagai, H., Fukuyama, K. and Barycki, J.J. (2007). „Autoprocessing of Helicobacter pylori γ-glutamyltranspeptidase leads to the formation of a threonine-threonine catalytic dyad”. J. Biol. Chem. 282: 534-541. PMID 17107958.
- ↑ Okada, T., Suzuki, H., Wada, K., Kumagai, H. and Fukuyama, K. (2007). „Crystal structure of the γ-glutamyltranspeptidase precursor protein from Escherichia coli. Structural changes upon autocatalytic processing and implications for the maturation mechanism”. J. Biol. Chem. 282: 2433-2439. PMID 17135273.
- ↑ Wickham, S., West, M.B., Cook, P.F. and Hanigan, M.H. (2011). „Gamma-glutamyl compounds: substrate specificity of γ-glutamyl transpeptidase enzymes”. Anal. Biochem. 414: 208-214. PMID 21447318.
- ↑ Carter, B.Z., Wiseman, A.L., Orkiszewski, R., Ballard, K.D., Ou, C.N. and Lieberman, M.W. (1997). „Metabolism of leukotriene C4 in γ-glutamyl transpeptidase-deficient mice”. J. Biol. Chem. 272: 12305-12310. PMID 9139674.
Literatura[uredi | uredi kod]
- 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.