Biology:CMP kinase
From HandWiki
Short description: Protein-coding gene in the species Homo sapiens
Generic protein structure example |
UMP-CMP kinase is an enzyme that in humans is encoded by the CMPK1 gene.[1][2]
Function
Uridine monophosphate (UMP)/cytidine monophosphate (CMP) kinase (EC 2.7.4.4) catalyzes the phosphoryl transfer from ATP to UMP, CMP, and deoxy-CMP (dCMP), resulting in the formation of ADP and the corresponding nucleoside diphosphate. These nucleoside diphosphates are required for cellular nucleic acid synthesis.[2][3]
References
- ↑ "Phosphorylation of deoxycytidine analog monophosphates by UMP-CMP kinase: molecular characterization of the human enzyme". Molecular Pharmacology 56 (3): 562–9. 1999. doi:10.1124/mol.56.3.562. PMID 10462544.
- ↑ 2.0 2.1 EntrezGene 51727
- ↑ "Characterization of human UMP/CMP kinase and its phosphorylation of D- and L-form deoxycytidine analogue monophosphates". Cancer Research 62 (6): 1624–31. 2002. PMID 11912132.
External links
- Human CMPK1 genome location and CMPK1 gene details page in the UCSC Genome Browser.
Further reading
- "Human liver protein map: A reference database established by microsequencing and gel comparison". Electrophoresis 13 (12): 992–1001. 1992. doi:10.1002/elps.11501301201. PMID 1286669.
- "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene 138 (1–2): 171–4. 1994. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
- "Human liver protein map: Update 1993". Electrophoresis 14 (11): 1216–22. 1993. doi:10.1002/elps.11501401181. PMID 8313870.
- "Construction and characterization of a full length-enriched and a 5′-end-enriched cDNA library". Gene 200 (1–2): 149–56. 1997. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
- "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning". Proceedings of the National Academy of Sciences 97 (17): 9543–8. 2000. doi:10.1073/pnas.160270997. PMID 10931946. Bibcode: 2000PNAS...97.9543H.
- "Characterization of human UMP-CMP kinase enzymatic activity and 5′ untranslated region". Life Sciences 69 (20): 2361–70. 2001. doi:10.1016/S0024-3205(01)01322-4. PMID 11681623.
- "Characterization of human UMP/CMP kinase and its phosphorylation of D- and L-form deoxycytidine analogue monophosphates". Cancer Research 62 (6): 1624–31. 2002. PMID 11912132.
- "Reaction of human UMP-CMP kinase with natural and analog substrates". European Journal of Biochemistry 270 (8): 1784–90. 2003. doi:10.1046/j.1432-1033.2003.03537.x. PMID 12694191.
- "Substrate-induced Conformational Changes in Human UMP/CMP Kinase". Journal of Biological Chemistry 279 (32): 33882–9. 2004. doi:10.1074/jbc.M401989200. PMID 15163660.
- "Phosphorylation of Cytidine, Deoxycytidine, and Their Analog Monophosphates by Human UMP/CMP Kinase is Differentially Regulated by ATP and Magnesium". Molecular Pharmacology 67 (3): 806–14. 2004. doi:10.1124/mol.104.006098. PMID 15550676.
- "Beta-Amyloid protein converting enzyme 1 and brain-specific type II membrane protein BRI3: binding partners processed by furin". Journal of Neurochemistry 92 (1): 93–102. 2005. doi:10.1111/j.1471-4159.2004.02840.x. PMID 15606899.
- "Nucleotide binding to human UMP-CMP kinase using fluorescent derivatives – a screening based on affinity for the UMP-CMP binding site". FEBS Journal 274 (14): 3704–14. 2007. doi:10.1111/j.1742-4658.2007.05902.x. PMID 17608725.
- "UMP kinase from the Gram-positive bacterium Bacillus subtilis is strongly dependent on GTP for optimal activity". European Journal of Biochemistry 270 (15): 3196–204. 2003. doi:10.1046/j.1432-1033.2003.03702.x. PMID 12869195.
- "Structural and functional consequences of single amino acid substitutions in the pyrimidine base binding pocket of Escherichia coli CMP kinase". The FEBS Journal 274 (13): 3363–73. 2007. doi:10.1111/j.1742-4658.2007.05870.x. PMID 17542990.
Original source: https://en.wikipedia.org/wiki/CMP kinase.
Read more |