Kinetic mechanism of streptomycin adenylyltransferase from a recombinant Escherichia coli.
作者： Snehasis Jana , J. K. Deb
DOI: 10.1007/S10529-005-2544-9
关键词:
摘要: Bacterial resistance to the aminoglycoside antibiotics is manifested primarily by enzymic modification of these drugs. One important mechanism streptomycin through ATP-dependent O-adenylation, catalyzed adenylyltransferase. Initial velocity patterns deduced from steady state kinetics indicate a sequential mechanism. Dead-end inhibition tobramycin and neomycin non-competitive versus uncompetitive ATP, indicative ordered substrate binding where ATP binds first then streptomycin. These results surmise that adenylyltransferase follows an ordered, kinetic in which one (ATP) prior antibiotic pyrophosphate released formation AMP-streptomycin.
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