Riboflavin kinaza
| Riboflavin kinaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 | |||||||||
| Identifikatori | |||||||||
| EC broj | 2.7.1.26 | ||||||||
| CAS broj | 9032-82-0 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
Riboflavin kinaza (EC 2.7.1.26, flavokinaza, FK, RFK) je enzim sa sistematskim imenom ATP:riboflavin 5'-fosfotransferaza.[1][2][3][4][5][6][7] Ovaj enzim katalizuje sledeću hemijsku reakciju
- ATP + riboflavin ADP + FMN
Kofaktori FMN i FAD učestvuju u brojnim procesima u svim organizmima, uključujući mitohondrijski elektronski transport, fotosintezu, masna-kiselinsku oksidaciju, i metabolizam vitamina B6, vitamina B12 i folata.
Reference
- ↑ Chassy, B.M., Arsenis, C. and McCormick, D.B. (1965). „The effect of the length of the side chain of flavins on reactivity with flavokinase”. J. Biol. Chem. 240: 1338-1340. PMID 14284745.
- ↑ Giri, K.V., Krishnaswamy, P.R. and Rao, N.A. (1958). „Studies on plant flavokinase”. Biochem. J. 70: 66-71. PMID 13584303.
- ↑ Kearney, E.B. (1952). „The interaction of yeast flavokinase with riboflavin analogues”. J. Biol. Chem. 194: 747-754. PMID 14927668.
- ↑ McCormick, D.B. and Butler, R.C. (1962). „Substrate specificity of liver flavokinase”. Biochim. Biophys. Acta 65: 326-332.
- ↑ Sandoval, F.J. and Roje, S. (2005). „An FMN hydrolase is fused to a riboflavin kinase homolog in plants”. J. Biol. Chem. 280: 38337-38345. PMID 16183635.
- ↑ Solovieva, I.M., Tarasov, K.V. and Perumov, D.A. (2003). „Main physicochemical features of monofunctional flavokinase from Bacillus subtilis”. Biochemistry (Mosc) 68: 177-181. PMID 12693963.
- ↑ Solovieva, I.M., Kreneva, R.A., Leak, D.J. and Perumov, D.A. (1999). „The ribR gene encodes a monofunctional riboflavin kinase which is involved in regulation of the Bacillus subtilis riboflavin operon”. Microbiology 145: 67-73. PMID 10206712.
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 Riboflavin+kinase
- 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
