| 词条 | Kanamycin nucleotidyltransferase |
| 释义 |
| Symbol = KNTase_C | Name = KNTase C-terminal domain | image = PDB 1kny EBI.jpg | width = | caption = kanamycin nucleotidyltransferase | Pfam = PF07827 | Pfam_clan = CL0291 | InterPro = IPR012481 | SMART = | PROSITE = | MEROPS = | SCOP = 1kny | TCDB = | OPM family = | OPM protein = | CAZy = | CDD = }} In molecular biology, kanamycin nucleotidyltransferase {{EC number|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] References1. ^{{cite journal |vauthors=Pedersen LC, Benning MM, Holden HM | title = Structural investigation of the antibiotic and ATP-binding sites in kanamycin nucleotidyltransferase | journal = Biochemistry | volume = 34 | issue = 41 | pages = 13305–11 |date=October 1995 | pmid = 7577914 | doi = 10.1021/bi00041a005| url = }} {{InterPro content|IPR012481}} 1 : Protein domains |
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