Ribonukleozid-difosfat reduktaza
Ribonukleozid-difosfat reduktaza (EC 1.17.4.1, ribonukleotidna reduktaza, CDP reduktaza, ribonukleozidna difosfatna reduktaza, UDP reduktaza, ADP reduktaza, nukleozid difosfatna reduktaza, ribonukleozid 5'-difosfatna reduktaza, ribonukleotidna difosfatna reduktaza, 2'-dezoksiribonukleozid-difosfat:oksidovani-tioredoksin 2'-oksidoreduktaza, RR) je enzim sa sistematskim imenom 2'-dezoksiribonukleozid-difosfat:tioredoksin-disulfid 2'-oksidoreduktaza.[1][2][3][4][5][6] Ovaj enzim katalizuje sledeću hemijsku reakciju
| Ribonukleozid-difosfat reduktaza | |||||||||
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| Identifikatori | |||||||||
| EC broj | 1.17.4.1 | ||||||||
| CAS broj | 9047-64-7 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
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- 2'-dezoksiribonukleozid difosfat + tioredoksin disulfid + H2O ribonukleozid difosfat + tioredoksin
Ovaj enzim je odgovoran za de novo konverziju ribonukleozid difosfata u dezoksiribonukleozid difosfate, što je esencijalno za DNK sintezu i popravku. On sadrži gvožđe. Enzim aktivira ATP, a inhibira ga dATP.
Reference uredi
- ↑ Lammers, M. and Follmann, H. (1983). „The ribonucleotide reductases - a unique group of metalloenzymes essential for cell-proliferation”. Struct. Bonding 54: 27-91.
- ↑ Larsson, A. (1973). „Ribonucleotide reductase from regenerating rat liver. II. Substrate phosphorylation level and effect of deoxyadenosine triphosphate”. Biochim. Biophys. Acta 324: 447-451. PMID 4543472.
- ↑ Larsson, A. and Reichard, P. (1966). „Enzymatic synthesis of deoxyribonucleotides. IX. Allosteric effects in the reduction of pyrimidine ribonucleotides by the ribonucleoside diphosphate reductase system of Escherichia coli”. J. Biol. Chem. 241: 2533-2539. PMID 5330119.
- ↑ Larsson, A. and Reichard, P. (1966). „Enzymatic synthesis of deoxyribonucleotides. X. Reduction of purine ribonucleotides; allosteric behavior and substrate specificity of the enzyme system from Escherichia coli B”. J. Biol. Chem. 241: 2540-2549. PMID 5330120.
- ↑ Moore, E.C. and Hurlbert, R.B. (1966). „Regulation of mammalian deoxyribonucleotide biosynthesis by nucleotides as activators and inhibitors”. J. Biol. Chem. 241: 4802-4809. PMID 5926184.
- ↑ Qiu, W., Zhou, B., Darwish, D., Shao, J. and Yen, Y. (2006). „Characterization of enzymatic properties of human ribonucleotide reductase holoenzyme reconstituted in vitro from hRRM1, hRRM2, and p53R2 subunits”. Biochem. Biophys. Res. Commun. 340: 428-434. PMID 16376858.
Literatura uredi
- 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.