Journal article
Mechanism of aminoglycoside 3'-phosphotransferase type IIIa: His188 is not a phosphate-accepting residue
Abstract
BACKGROUND: The enzyme aminoglycoside 3'-phosphotransferase Type IIIa (APH(3')-IIIa), confers resistance to many aminoglycoside antibiotics by regiospecific phosphorylation of their hydroxyl groups. The chemical mechanism of phosphoryl transfer is unknown. Based on sequence homology, it has been suggested that a conserved His residue, His188, could be phosphorylated by ATP, and this phospho-His would transfer the phosphate to the incoming …
Authors
Thompson PR; Hughes DW; Wright GD
Journal
Cell Chemical Biology, Vol. 3, No. 9, pp. 747–755
Publisher
Elsevier
Publication Date
9 1996
DOI
10.1016/s1074-5521(96)90251-3
ISSN
2451-9456
Fields of Research (FoR)
Medical Subject Headings (MeSH)
Adenosine TriphosphateBlotting, WesternCarbohydrate SequenceChemical PhenomenaChemistryCloning, MolecularConserved SequenceDiethyl PyrocarbonateDrug ResistanceEnterococcusHistidineKanamycin KinaseKineticsMagnetic Resonance SpectroscopyMolecular Sequence DataMutagenesis, Site-DirectedOligosaccharidesPhosphatesPhosphorylationPhosphotransferases (Alcohol Group Acceptor)Protein FoldingSequence AlignmentStaphylococcus