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Showing 1 to 6 of 6 for “"PglB"”.
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Engineered Oligosaccharyltransferases With Unique N-Glycosylation Site Preferences
… the Campylobacter jejuni glycosylation pathway, PglB, has been one of the well-studied asparagine-linked oligosaccharyltransferase (OST) in bacterial glycoengineering area. While C. jejuni PglB performs well in transferring different glycans, the acceptor sites it can recognize are limited. We …
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Investigation of the structure requirements for oligosaccharyl transferase function
… the process. Specifically, the bacterial OTase, PglB, is monomeric and homologous to the catalytic subunit of the eukaryotic OTase. The following chapters describe studies designed to learn about the OTase transfer reaction using PglB as a model. Optimization of expression and purification of …
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Investigation of asparagine-linked glycosylation in archaeal and bacterial systems
… progress has been made with the bacterial OTase PglB from Campylobacterjejuni, problems with low protein expression yields and poor stability have complicated in depth study. In order to identify a more suitable OTase candidate, a selection of archaeal OTases was screened for heterologous …
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IMPROVING GLYCOSYLATION EFFICIENCY IN ESCHERICHIA COLI BY MAMMALIAN-CELL-INSPIRED PROTEIN-PROTEIN INTERACTIONS
… that fusion proteins of the Campylobacter jejuni PglB were able to improve the expression of challenging acceptor proteins without sacrificing glycosylation efficiency. Further investigations reveal significant implications relating OST expression to protein glycosylation efficiency.
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Elucidation of the pathways responsible for the biosynthesis of UDP-N,N'-diacetylbacillosamine in bacterial pathogens
… glycosylation pathways in N. gonorrhoeae (PglB-ATD) and A. baumannii (Weel). These enzymes are members of the left-handed [beta]-helix family and are responsible for the acetylation of UDP-2-acetamido-4-amino-2,4,6-trideoxy-[alpha]-D-glucose (UDP-4-amino) to produce UDP-diNAcBac. Based upon …
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ENGINEERING WATER-SOLUBLE VARIANTS OF THE SINGLE-SUBUNIT OLIGOSACCHARYLTRANSFERASE
Oligosaccharyltransferase (OST) is a key enzyme in the asparagine-linked (N-linked) protein glycosylation pathway. OSTs exist in all domains of life and are capable of transferring a preassembled glycan from lipid carrier to an acceptor peptide. Bacterial OSTs are an single-subunit enzyme that are …