Kanamycin kinase

From Wikipedia, the free encyclopedia

In enzymology, a kanamycin kinase (EC 2.7.1.95) is an enzyme that catalyzes the chemical reaction

ATP + kanamycin $\rightleftharpoons$ ADP + kanamycin 3'-phosphate

Thus, the two substrates of this enzyme are ATP and kanamycin, whereas its two products are ADP and kanamycin 3'-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:kanamycin 3'-O-phosphotransferase. This enzyme is also called neomycin-kanamycin phosphotransferase.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes 1J7I, 1J7L, 1J7U, 1L8T, 1ND4, 2B0Q, and 2BKK.

[edit] References

IUBMB entry for 2.7.1.95
BRENDA references for 2.7.1.95 (Recommended.)
PubMed references for 2.7.1.95
PubMed Central references for 2.7.1.95
Google Scholar references for 2.7.1.95
Doi O, Ogura M, Tanaka N, Umezawa H (1968). "Inactivation of kanamycin, neomycin, and streptomycin by enzymes obtained in cells of Pseudomonas aeruginoa". Appl. Microbiol. 16: 1276–81. PMID 4970990.
DOLIN MI (1957). "The Streptococcus faecalis oxidases for reduced diphosphopyridine nucleotide. III. Isolation and properties of a flavin peroxidase for reduced diphosphopyridine nucleotide". J. Biol. Chem. 225: 557–73. PMID 13416259.