Citidilat kinaza
| Citidilat kinaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 2.7.4.14 | ||||||||
| CAS broj | 37278-21-0 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
Citidilat kinaza (EC 2.7.4.14, citidilatna kinaza, dezoksicitidilatna kinaza, CTP:CMP fosfotransferaza, dCMP kinaza, dezoksicitidinska monofosfokinaza, UMP-CMP kinaza, ATP:UMP-CMP fosfotransferaza, pirimidin nukleozid monofosfatna kinaza, uridin monofosfat-citidin monofosfatna fosfotransferaza) je enzim sa sistematskim imenom ATP:CMP(UMP) fosfotransferaza.[1][2][3][4][5] Ovaj enzim katalizuje sledeću hemijsku reakciju
- (1) ATP + (d)CMP ADP + (d)CDP
- (2) ATP + UMP ADP + UDP
Ovaj eukariotski enzim je bifunkcionalan. On katalizuje fosforilaciju CMP i UMP molekula sa sličnom efikasnošću.
Reference
- ↑ Hurwitz, J. (1959). „The enzymatic incorporation of ribonucleotides into polydeoxynucleotide material”. J. Biol. Chem. 234: 2351-2358. PMID 14405566.
- ↑ Ruffner, B.W., Jr. and Anderson, E.P. (1969). „Adenosine triphosphate: uridine monophosphate-cytidine monophosphate phosphotransferase from Tetrahymena pyriformis”. J. Biol. Chem. 244: 5994-6002. PMID 5350952.
- ↑ Scheffzek, K., Kliche, W., Wiesmuller, L. and Reinstein, J. (1996). „Crystal structure of the complex of UMP/CMP kinase from Dictyostelium discoideum and the bisubstrate inhibitor P1-(5′-adenosyl) P5-(5′-uridyl) pentaphosphate (UP5A) and Mg2+ at 2.2 Å: implications for water-mediated specificity”. Biochemistry 35: 9716-9727. PMID 8703943.
- ↑ Zhou, L., Lacroute, F. and Thornburg, R. (1998). „Cloning, expression in Escherichia coli, and characterization of Arabidopsis thaliana UMP/CMP kinase”. Plant Physiol. 117: 245-254. PMID 9576794.
- ↑ Van Rompay, A.R., Johansson, M. and Karlsson, A. (1999). „Phosphorylation of deoxycytidine analog monophosphates by UMP-CMP kinase: molecular characterization of the human enzyme”. Mol. Pharmacol. 56: 562-569. PMID 10462544.
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 UMP/CMP+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
