In molecular biology, kanamycin nucleotidyltransferase EC 2.7.7.- (KNTase) is an enzyme which is involved in conferring resistance to aminoglycoside antibiotics. It catalyses the transfer of a nucleoside monophosphate group from a nucleotide to kanamycin. This enzyme is dimeric with each subunit being composed of two domains. The C-terminal domain contains five alpha helices, four of which are organised into an up-and-down alpha helical bundle. Residues found in this domain may contribute to this enzyme's active site.[1]
^Pedersen LC, Benning MM, Holden HM (October 1995). "Structural investigation of the antibiotic and ATP-binding sites in kanamycin nucleotidyltransferase". Biochemistry. 34 (41): 13305–11. doi:10.1021/bi00041a005. PMID 7577914.
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In molecular biology, kanamycinnucleotidyltransferase EC 2.7.7.- (KNTase) is an enzyme which is involved in conferring resistance to aminoglycoside antibiotics...
structurally similar to the C-terminal all-alpha-helical domain of kanamycinnucleotidyltransferases (KNTases). It is composed of five alpha helices, three of...
aminoacetyltransferase and nucleotidyltransferase. This is accomplished by the L-hydroxyaminobuteroyl amide (L-HABA) moiety attached to N-1 (compare to kanamycin, which simply...
pactamycin 2-deoxy-scyllo-inosose derived aminoglycosides This class includes kanamycin, neomycin, gentamicin, apramycin, hygromycin. myo-inositol 1-phosphate...
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