Kanamycin nucleotidyltransferase

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]

KNTase C-terminal domain
kanamycin nucleotidyltransferase
Identifiers
SymbolKNTase_C
PfamPF07827
Pfam clanCL0291
InterProIPR012481
SCOP21kny / SCOPe / SUPFAM

References

  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.
This article incorporates text from the public domain Pfam and InterPro: IPR012481
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