Pseudouridine kinase
In enzymology, a pseudouridine kinase (EC 2.7.1.83) is an enzyme that catalyzes the chemical reaction
- ATP + pseudouridine ADP + pseudouridine 5'-phosphate
pseudouridine kinase | |||||||||
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Identifiers | |||||||||
EC number | 2.7.1.83 | ||||||||
CAS number | 62213-40-5 | ||||||||
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 / QuickGO | ||||||||
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Thus, the two substrates of this enzyme are ATP and pseudouridine, whereas its two products are ADP and pseudouridine 5'-phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:pseudouridine 5'-phosphotransferase. This enzyme is also called pseudouridine kinase (phosphorylating). This enzyme participates in pyrimidine metabolism.
References
- Solomon LR, Breitman TR (1971). "Pseudouridine kinase of escherichia coli: a new enzyme". Biochem. Biophys. Res. Commun. 44 (2): 299–304. doi:10.1016/0006-291X(71)90599-7. PMID 4334133.
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