Aciredukton dioksigenaza (Ni2+)
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| Aciredukton dioksigenaza (Ni2+) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 1.13.11.53 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
Aciredukton dioksigenaza (Ni2+) (EC 1.13.11.53, ARD, 2-hidroksi-3-keto-5-tiometilpent-1-en dioksigenaza (nespecifična), acireduktonska dioksigenaza (nespecifična), E-2) je enzim sa sistematskim imenom 1,2-dihidroksi-5-(metiltio)pent-1-en-3-on:kiseonik oksidoreduktaza (formira format- i CO).[1][2][3][4][5][6][7][8] Ovaj enzim katalizuje sledeću hemijsku reakciju
- 1,2-dihidroksi-5-(metiltio)pent-1-en-3-on + O2 3-(metiltio)propanoat + format + CO
Ovaj enzim sadrži Ni2+. Ako je gvožđe(II) vezano umesto Ni2+, on posreduje reakciju enzima EC 1.13.11.54, acireduktonske dioksigenaze.
Reference[uredi | uredi kod]
- ↑ Wray, J.W. and Abeles, R.H. (1993). „A bacterial enzyme that catalyzes formation of carbon monoxide”. J. Biol. Chem. 268: 21466-21469. PMID 8407993.
- ↑ Wray, J.W. and Abeles, R.H. (1995). „The methionine salvage pathway in Klebsiella pneumoniae and rat liver. Identification and characterization of two novel dioxygenases”. J. Biol. Chem. 270: 3147-3153. PMID 7852397.
- ↑ Furfine, E.S. and Abeles, R.H. (1988). „Intermediates in the conversion of 5′-S-methylthioadenosine to methionine in Klebsiella pneumoniae”. J. Biol. Chem. 263: 9598-9606. PMID 2838472.
- ↑ Dai, Y., Wensink, P.C. and Abeles, R.H. (1999). „One protein, two enzymes”. J. Biol. Chem. 274: 1193-1195. PMID 9880484.
- ↑ Mo, H., Dai, Y., Pochapsky, S.S. and Pochapsky, T.C. (1999). „1H, 13C and 15N NMR assignments for a carbon monoxide generating metalloenzyme from Klebsiella pneumoniae”. J. Biomol. NMR 14: 287-288. PMID 10481280.
- ↑ Dai, Y., Pochapsky, T.C. and Abeles, R.H. (2001). „Mechanistic studies of two dioxygenases in the methionine salvage pathway of Klebsiella pneumoniae”. Biochemistry 40: 6379-6387. PMID 11371200.
- ↑ Al-Mjeni, F., Ju, T., Pochapsky, T.C. and Maroney, M.J. (2002). „XAS investigation of the structure and function of Ni in acireductone dioxygenase”. Biochemistry 41: 6761-6769. PMID 12022880.
- ↑ Pochapsky, T.C., Pochapsky, S.S., Ju, T., Mo, H., Al-Mjeni, F. and Maroney, M.J. (2002). „Modeling and experiment yields the structure of acireductone dioxygenase from Klebsiella pneumoniae”. Nat. Struct. Biol. 9: 966-972. PMID 12402029.
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.