نتایج جستجو برای: aminoglycoside modifying enzymes

تعداد نتایج: 166314  

Journal: :Protein science : a publication of the Protein Society 2004
Blair S Nield Robert D Willows Andrew E Torda Michael R Gillings Andrew J Holmes K M Helena Nevalainen H W Stokes Bridget C Mabbutt

By targeting gene cassettes by polymerase chain reaction (PCR) directly from environmentally derived DNA, we are able to amplify entire open reading frames (ORFs) independently of prior sequence knowledge. Approximately 10% of the mobile genes recovered by these means can be attributed to known protein families. Here we describe the characterization of two ORFs which show moderate homology to k...

Journal: :Bioorganic & medicinal chemistry letters 2013
Lei Shao Junsheng Chen Chunxia Wang Ji-an Li Yumin Tang Daijie Chen Wen Liu

Gentamicin is an aminoglycoside antibiotic obtained from cultures of Micromonospora as the important anti-infective agents. Gentamicin which lacks 3'-hydroxyl group can avoid the attack from the modification enzymes of antibiotic-resistant bacteria in clinic. Consequently, C-3' dehydroxylation is the key step in gentamicins biosynthesis. We suppose that there are some enzymes responsible for co...

Journal: :Antimicrobial agents and chemotherapy 1986
M H Perlin S A Lerner

Plasmid pMP1-1 in Escherichia coli L-0 encodes aminoglycoside (AG) 3'-phosphotransferase II [APH(3')-II]. This enzyme modifies and confers high-level resistance to kanamycin. Although amikacin is a substrate for APH(3')-II, strain L-0(pMP1-1) is susceptible to amikacin. Plasmid pMP1-2 is a spontaneous mutant of pMP1-1 which determines increased APH(3')-II activity for amikacin, apparently as a ...

Journal: :The Journal of biological chemistry 2010
Desiree H Fong Christopher T Lemke Jiyoung Hwang Bing Xiong Albert M Berghuis

Aminoglycoside phosphotransferases (APHs) constitute a diverse group of enzymes that are often the underlying cause of aminoglycoside resistance in the clinical setting. Several APHs have been extensively characterized, including the elucidation of the three-dimensional structure of two APH(3') isozymes and an APH(2'') enzyme. Although many APHs are plasmid-encoded and are capable of inactivati...

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