UMP kinase

From Wikipedia, the free encyclopedia

In enzymology, an UMP kinase (EC 2.7.4.22) is an enzyme that catalyzes the chemical reaction

ATP + UMP ADP + UDP

Thus, the two substrates of this enzyme are ATP and UMP, whereas its two products are ADP and UDP.

This enzyme belongs to the family of transferases, specifically those 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. This enzyme participates in pyrimidine metabolism.

[edit] Structural studies

As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes 2J4J, 2J4K, 2J4L, and 2VA1.

[edit] References

• IUBMB entry for 2.7.4.22
• BRENDA references for 2.7.4.22 (Recommended.)
• PubMed references for 2.7.4.22
• PubMed Central references for 2.7.4.22
• Google Scholar references for 2.7.4.22
• Gilles AM, Barzu O (1995). "Escherichia coli UMP-kinase, a member of the aspartokinase family, is a hexamer regulated by guanine nucleotides and UTP". Biochemistry. 34: 5066–74. PMID 7711027. 
• Marco-Marin C, Gil-Ortiz F, Rubio V (2005). "The crystal structure of Pyrococcus furiosus UMP kinase provides insight into catalysis and regulation in microbial pyrimidine nucleotide biosynthesis". J. Mol. Biol. 352: 438–54. PMID 16095620. 

[edit] External links

• IUBMB entry for 2.7.4.22

• KEGG entry for 2.7.4.22

• BRENDA entry for 2.7.4.22

• NiceZyme view of 2.7.4.22

• EC2PDB: PDB structures for 2.7.4.22

• PRIAM entry for 2.7.4.22

• PUMA2 entry for 2.7.4.22

• IntEnz: Integrated Enzyme entry for 2.7.4.22

• MetaCyc entry for 2.7.4.22

• Atomic-resolution structures of enzymes belonging to this class