Tripanotion-disulfid reduktaza
| Tripanotion-disulfid reduktaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 1.8.1.12 | ||||||||
| CAS broj | 102210-35-5 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
Tripanotion-disulfid reduktaza (EC 1.8.1.12, tripanotionska reduktaza, NADPH2:tripanotionska oksidoreduktaza) je enzim sa sistematskim imenom tripanotion:NADP+ oksidoreduktaza.[1][2][3] Ovaj enzim katalizuje sledeću hemijsku reakciju
- tripanotion + NADP+ tripanotion disulfid + NADPH + H+
Tripanotion disulfid je oksidovana forma N1,N8-bis(glutationil)-spermidina iz insektnog-parazitskog tripanozomatida Crithidia fasciculata. Enzim iz Crithidia fasciculata je flavoprotein (FAD). Njegovo dejstvo je zavisno od redoks-aktivnog cistina na aktivnom mestu.
Reference
- ↑ Shames, S.L., Fairlamb, A.H., Cerami, A. and Walsh, C.T. (1986). „Purification and characterization of trypanothione reductase from Crithidia fasciculata, a newly discovered member of the family of disulfide-containing flavoprotein reductases”. Biochemistry 25: 3519-3526. PMID 3718941.
- ↑ Marsh, I.R. and Bradley, M. (1977). „Substrate specificity of trypanothione reductase”. Eur. J. Biochem. 243: 690-694. PMID 9057833.
- ↑ Cunningham, M.L. and Fairlamb, A.H. (1995). „Trypanothione reductase from Leishmania donovani. Purification, characterisation and inhibition by trivalent antimonials”. Eur. J. Biochem. 230: 460-468. PMID 7607216.
Literatura
- 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.
Spoljašnje veze
- MeSH Trypanothione-disulfide+reductase
- p
- r
- u
Aktivno mesto • Alosterna regulacija • Mesto vezivanja • Katalitički perfektan enzim • Koenzim • Kofaktor • Kooperativnost • EC broj • Enzimska kataliza • Inhibicija enzima • Enzimska kinetika • Lajnviver–Burk dijagram • Mihaelis–Mentenova kinetika • Spisak enzima
EC1 Oksidoreduktaze/spisak • EC2 Transferaze/spisak • EC3 Hidrolaze/spisak • EC4 Lijaze/spisak • EC5 Izomeraze/spisak • EC6 Ligaze/spisak
B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6
