Biology:UMP kinase
UMP kinase (EC 2.7.4.22) is an enzyme that catalyzes the chemical reaction
- REDIRECT Template:Chemical reaction
The enzyme characterised from Escherichia coli and Pyrococcus furiosus converts the nucleotide, uridine monophosphate, to uridine diphosphate by transferring a phosphate group from the cofactor, adenosine triphosphate (ATP), which is converted to adenosine diphosphate (ADP).[1][2]
Nomenclature
The enzyme is a transferase, specifically one transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. The systematic name of this enzyme class is ATP:UMP phosphotransferase. Other names in common use include uridylate kinase, UMPK, uridine monophosphate kinase, PyrH, UMP-kinase, and SmbA.[3]
Structural studies
As of March 2010, 19 structures have been solved for this class of enzymes, and are deposited in the Protein Data Bank. All have a 3-layer (aba) sandwich) architecture (CATH code 3.40.1160.10). These include accession codes 2J4J, 2J4K, 2J4L, and 2VA1.
Search for all UMP Kinases in the PDB using the enzyme Browser at PDBe. (input the EC number)
References
- ↑ "Escherichia coli UMP-kinase, a member of the aspartokinase family, is a hexamer regulated by guanine nucleotides and UTP". Biochemistry 34 (15): 5066–5074. 1995. doi:10.1021/bi00015a018. PMID 7711027.
- ↑ "The crystal structure of Pyrococcus furiosus UMP kinase provides insight into catalysis and regulation in microbial pyrimidine nucleotide biosynthesis". J. Mol. Biol. 352 (2): 438–454. 2005. doi:10.1016/j.jmb.2005.07.045. PMID 16095620.
- ↑ Enzyme 2.7.4.22 at KEGG Pathway Database.
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