related to degree

• Liu, Haitian, Ph.D. in Chemistry, Scripps Research 1999 - 2005

authors

• Liu, Haitian
• Wong, Chi-Huey

publication date

• November 2006

journal

• Bioorganic & Medicinal Chemistry  Journal

abstract

• 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.

subject areas

• Amino Acid Sequence
• Carbohydrate Sequence
• Fluorescence
• Magnetic Resonance Spectroscopy
• Mass Spectrometry
• Molecular Sequence Data
• Peptidoglycan Glycosyltransferase
• Sequence Homology, Amino Acid
• Streptococcus pneumoniae
• Surface Plasmon Resonance

keywords

• Streptococcus pneumoniae
• enzyme catalysis
• lipid II
• transglycosylase

International Standard Serial Number (ISSN)

• 0968-0896

Digital Object Identifier (DOI)

• 10.1016/j.bmc.2006.06.058

PubMed ID

• 16870450

start page

• 7187

end page

• 7195

volume

• 14

issue

• 21