Dihidrofolat reduktaza
| Dihidrofolat reduktaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 | |||||||||
| Identifikatori | |||||||||
| EC broj | 1.5.1.3 | ||||||||
| CAS broj | 2594015 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
Dihidrofolat reduktaza (EC 1.5.1.3, tetrahidrofolatna dehidrogenaza, DHFR, pteridinska reduktaza:dihidrofolat reduktaza, dihidrofolatna reduktaza:timidilat sintaza, timidilatna sintetaza-dihidrofolat reduktaza, folna kiselina reduktaza, folna reduktaza, dihidrofolna kiselina reduktaza, dihidrofolna reduktaza, 7,8-dihidrofolat reduktaza, NADPH-dihidrofolat reduktaza) je enzim sa sistematskim imenom 5,6,7,8-tetrahidrofolat:NADP+ oksidoreduktaza.[1][2][3][4] Ovaj enzim katalizuje sledeću hemijsku reakciju
- 5,6,7,8-tetrahidrofolat + NADP+ 7,8-dihidrofolat + NADPH + H+
Ovaj enzim iz životinaj i nekih mikroorganizama takođe u manjoj meri redukuje folat do 5,6,7,8-tetrahidrofolata.
Reference
- ↑ Blakley, R.L. and MacDougall, B.M. (1961). „Dihydrofolic reductase from Streptococcus faecalis R”. J. Biol. Chem. 236: 1163-1163.
- ↑ Bolin, J.T., Filman, D.J., Matthews, D.A. and Kraut, J. (1982). „Crystal structures of Escherichia coli and Lactobacillus casei dihydrofolate reductase refined at 1.7 Å resolution. I. General features and binding of methotrexate”. J. Biol. Chem. 257: 13650-13662. PMID 6815178.
- ↑ Kaufman, B.T. and Gardiner, R.C. (1966). „Studies on dihydrofolic reductase. I. Purification and properties of dihydrofolic reductase from chicken liver”. J. Biol. Chem. 241: 1319-1328. PMID 4379915.
- ↑ Young, I.G. and Gibson, F. (1969). „Regulation of the enzymes involved in the biosynthesis of 2,3-dihydroxybenzoic acid in Aerobacter aerogenes and Escherichia coli”. Biochim. Biophys. Acta 177: 401-411. PMID 4306838.
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 Dihydrofolate+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
