Glutationska hidrolaza
Изглед
Glutationska hidrolaza | |||||||||
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Identifikatori | |||||||||
EC broj | 3.4.19.13 | ||||||||
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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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
[уреди | уреди извор]- ^ Hanigan, M.H. & 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. & 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
[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]- Glutathione+hydrolase на US National Library of Medicine Medical Subject Headings (MeSH)