S-(hidroksimetil)glutation dehidrogenaza
| S-(hidroksimetil)glutation dehidrogenaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 1.1.1.284 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
S-(hidroksimetil)glutation dehidrogenaza (EC 1.1.1.284, NAD-vezani formaldehid dehidrogenaza, formaldehidna dehidrogenaza, forminska dehidrogenaza, klasa III alkoholna dehidrogenaza, ADH3, chi-ADH, FDH, formaldehidna dehidrogenaza (glutation), GS-FDH, glutation-zavisna formaldehidna dehidrogenaza, NAD-zavisna formaldehidna dehidrogenaza, GD-FALDH, NAD- i glutation-zavisna formaldehidna dehidrogenaza) je enzim sa sistematskim imenom S-(hidroksimetil)glutation:NAD+ oksidoreduktaza.[1][2][3][4][5][6][7] Ovaj enzim katalizuje sledeću hemijsku reakciju
- S-(hidroksimetil)glutation + NAD(P)+ S-formilglutation + NAD(P)H + H+
Supstrat ovog enzima, S-(hidroksimetil)glutation, se spontano formira iz glutationa i formaldehida. Njegova brzina formiranja je povećana kod nekih bakterija presustvom EC 4.4.1.22, S-(hidroksimetil)glutation sintaze. Ovaj enzim formira deo metaboličkog puta kojim se detoksifikuje formaldehid, pošto je produkt hidrolizovan dejstvom EC 3.1.2.12, S-formilglutation hidrolaze. Ljudski enzim pripada familiji od cinka zavisnih alkoholnih dehidrogenaza.
Ovaj enzim takođe specifično redukuje S-nitrozilglutation.
Reference[uredi | uredi kod]
- ↑ Jakoby, W.B. (1963). „Aldehyde dehydrogenases”. u: Boyer, P.D., Lardy, H. and Myrbäck, K.. The Enzymes. 7 (2nd izd.). New York: Academic Press. str. 203-221.
- ↑ Rose, Z.B. and Racker, E. (1966). „Formaldehyde dehydrogenase”. Methods Enzymol. 9: 357-360.
- ↑ Liu, L., Hausladen, A., Zeng, M., Que, L., Heitman, J. and Stamler, J.S. (2001). „A metabolic enzyme for S-nitrosothiol conserved from bacteria to humans”. Nature 410: 490-494. PMID 11260719.
- ↑ Sanghani, P.C., Stone, C.L., Ray, B.D., Pindel, E.V., Hurley, T.D. and Bosron, W.F. (2000). „Kinetic mechanism of human glutathione-dependent formaldehyde dehydrogenase”. Biochemistry 39: 10720-10729. PMID 10978156.
- ↑ van Ophem, P.W. and Duine, J.A. (1994). „NAD- and co-substrate (GSH or factor)-dependent formaldehyde dehydrogenases from methylotrophic microorganisms act as a class III alcohol dehydrogenase”. FEMS Microbiol. Lett. 116: 87-94.
- ↑ Ras, J., van Ophem, P.W., Reijnders, W.N., Van Spanning, R.J., Duine, J.A., Stouthamer, A.H. and Harms, N. (1995). „Isolation, sequencing, and mutagenesis of the gene encoding NAD- and glutathione-dependent formaldehyde dehydrogenase (GD-FALDH) from Paracoccus denitrificans, in which GD-FALDH is essential for methylotrophic growth”. J. Bacteriol. 177: 247-251. PMID 7798140.
- ↑ Barber, R.D., Rott, M.A. and Donohue, T.J. (1996). „Characterization of a glutathione-dependent formaldehyde dehydrogenase from Rhodobacter sphaeroides”. J. Bacteriol. 178: 1386-1393. PMID 8631716.
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.