| EC |
2.7.4.22 |
| Accepted name: |
UMP kinase |
| Reaction: |
ATP + UMP = ADP + UDP |
| Other name(s): |
uridylate kinase; UMPK; uridine monophosphate kinase; PyrH; UMP-kinase; SmbA |
| Systematic name: |
ATP:UMP phosphotransferase |
| Comments: |
This enzyme is strictly specific for UMP as substrate and is used by prokaryotes in the de novo synthesis of pyrimidines, in contrast to eukaryotes, which use the dual-specificity enzyme UMP/CMP kinase (EC 2.7.4.14) for the same purpose [2]. This enzyme is the subject of feedback regulation, being inhibited by UTP and activated by GTP [1]. |
| Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9036-23-1 |
| References: |
| 1. |
Serina, L., Blondin, C., Krin, E., Sismeiro, O., Danchin, A., Sakamoto, H., Gilles, A.M. and Bârzu, O. Escherichia coli UMP-kinase, a member of the aspartokinase family, is a
hexamer regulated by guanine nucleotides and UTP. Biochemistry 34 (1995) 5066–5074. [PMID: 7711027] |
| 2. |
Marco-Marín, C., Gil-Ortiz, F. and Rubio, V. The crystal structure of Pyrococcus furiosus UMP kinase provides insight
into catalysis and regulation in microbial pyrimidine nucleotide
biosynthesis. J. Mol. Biol. 352 (2005) 438–454. [DOI] [PMID: 16095620] |
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| [EC 2.7.4.22 created 2006] |
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