UMP kinase

UMP kinase
Identifiers
EC no.2.7.4.22
CAS no.9036-23-1
Databases
BRENDAenzyme data
ExPASyNiceZyme view
KEGGenzyme entry
MetaCycmetabolic pathway
Rheareactions
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
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PMCarticles
PubMedarticles
NCBIproteins

UMP kinase (EC 2.7.4.22) is an enzyme that catalyzes the 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 PDB: 2J4J​, PDB: 2J4K​, PDB: 2J4L​, and PDB: 2VA1​.

Search for all UMP Kinases in the PDB using the enzyme Browser at PDBe. (input the EC number)

References

  1. ↑ 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 (15): 5066–5074. doi:10.1021/bi00015a018. PMID 7711027.
  2. ↑ 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 (2): 438–454. doi:10.1016/j.jmb.2005.07.045. PMID 16095620.
  3. ↑ Enzyme 2.7.4.22 at KEGG Pathway Database.