Characterization of a transglycosylase domain of Streptococcus pneumoniae PBP1b.

Characterization of a transglycosylase domain of Streptococcus pneumoniae PBP1b. Research Abstract Details 

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Characterization of a transglycosylase domain of Streptococcus pneumoniae PBP1b. Abstract Text:

Haitian Liu,Chi-Huey Wong,

Inhibitors of transglycosylases may serve as potent antibiotics that are less prone to resistance development in bacterial pathogens. To facilitate the search of such compounds, a transglycosylase (TGase) domain of the membrane integral multidomain Streptococcus pneumoniae PBP1b was cloned and expressed. This TGase domain was characterized by a substrate-dependent fluorescence coupled enzyme assay and an inhibitor-tethered surface plasmon resonance binding assay. Both assays show that the catalytic efficiency of the domain is comparable to that of the monofunctional transglycosylases, and it is fully active in the absence of other domains. The isolation of the active TGase domain makes it possible to screen for potential antibiotics targeting transglycosylases.

Characterization of a transglycosylase domain of Streptococcus pneumoniae PBP1b. Publishing Authors By Initials

H Liu,CH Wong,

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Characterization of a transglycosylase domain of Streptococcus pneumoniae PBP1b. Journal Published:

PUBLICATION TYPE: Research Support, N.I.H., Extr

Journal: Bioorganic & medicinal chemistry

VOLUME: 14

Page Numbers: 7187-95

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ISSN: 0968-0896

DAY: 25

MONTH: 07

YEAR: 2006

Characterization of a transglycosylase domain of Streptococcus pneumoniae PBP1b. Information

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LANGUAGE: eng

NlmUniqueID: 9413298

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Grant and Affiliation Information for Characterization of a transglycosylase domain of Streptococcus pneumoniae PBP1b.

AFFILIATION: Department of Chemistry, The Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.

Country: England

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MEDLINETA: Bioorg Med Chem

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