UMP kinase
| UMP kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 2.7.4.22 | ||||||||
| CAS number | 9036-23-1 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / EGO | ||||||||
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| Search | |
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| PMC | articles |
| PubMed | articles |
| NCBI | proteins |
In enzymology, an UMP kinase (EC 2.7.4.22) is an enzyme that catalyzes the chemical reaction
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.
As of March 2010, 19 structures have been solved for this class of enzymes, and are deposited in the PDB. All have a 3-layer (aba) sandwich) architecture (CATH code 3.40.1160.10). These include accession codes 2J4J, 2J4K, 2J4L, and 2VA1.
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