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Carbohydrate biosynthetic enzymes fr...

Kowal, Przemyslaw.

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Carbohydrate biosynthetic enzymes from gram-negative bacteria.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	Carbohydrate biosynthetic enzymes from gram-negative bacteria./
作者:	Kowal, Przemyslaw.
面頁冊數:	154 p.
附註:	Source: Dissertation Abstracts International, Volume: 65-01, Section: B, page: 0206.
Contained By:	Dissertation Abstracts International65-01B.
標題:	Chemistry, Biochemistry. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3117244

Carbohydrate biosynthetic enzymes from gram-negative bacteria.
Kowal, Przemyslaw.

Carbohydrate biosynthetic enzymes from gram-negative bacteria. - 154 p.

Source: Dissertation Abstracts International, Volume: 65-01, Section: B, page: 0206.

Thesis (Ph.D.)--Wayne State University, 2003.

Carbohydrates are now recognized as being of major importance in a great variety of physiological and pathological processes. Glycosyltransferases are enzymes responsible for the assembly of bacterial cell walls (e.g. succinoglycan) and lipopolysaccharides on the outer membrane of Gram negative bacterial cells. Two transferases, alpha1,4-galactosyltransferase (LgtC) and beta,3-N-acetylglucosaminyltransferase (LgtA) that participate in the synthesis of Neisseria meningitidis were expressed in E. coli. LgtC proved to be a very efficient catalyst in the syntheses of globotriose and a variety of alpha1,4-galactosylated derivatives as potential antibacterial agents. The synthetic utility of the transferase was further demonstrated by its use in whole cell and on-bead large scale syntheses of globotriose.Subjects--Topical Terms:

1017722
Chemistry, Biochemistry.

Carbohydrate biosynthetic enzymes from gram-negative bacteria.
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100 1 $a Kowal, Przemyslaw. $3 1948698
245 1 0 $a Carbohydrate biosynthetic enzymes from gram-negative bacteria.
300 $a 154 p.
500 $a Source: Dissertation Abstracts International, Volume: 65-01, Section: B, page: 0206.
500 $a Adviser: Peng George Wang.
502 $a Thesis (Ph.D.)--Wayne State University, 2003.
520 $a Carbohydrates are now recognized as being of major importance in a great variety of physiological and pathological processes. Glycosyltransferases are enzymes responsible for the assembly of bacterial cell walls (e.g. succinoglycan) and lipopolysaccharides on the outer membrane of Gram negative bacterial cells. Two transferases, alpha1,4-galactosyltransferase (LgtC) and beta,3-N-acetylglucosaminyltransferase (LgtA) that participate in the synthesis of Neisseria meningitidis were expressed in E. coli. LgtC proved to be a very efficient catalyst in the syntheses of globotriose and a variety of alpha1,4-galactosylated derivatives as potential antibacterial agents. The synthetic utility of the transferase was further demonstrated by its use in whole cell and on-bead large scale syntheses of globotriose.
520 $a O-antigen is the outermost component of the smooth lipopolysaccharide. Plesiomonas shigelloides O-unit contains only two sugars and is therefore ideal for studies on the biosynthesis of the O-antigen. The repeating unit consists of two sugars: 2-acetamino-4-amino-2,4,6-trideoxy-D-galactose (4n-FucNAc) and 2-acetamino-2-deoxy-L-altruronic acid (2Ac-AltUA), however, its biosynthesis has not been studied. Biochemical characterization has confirmed that WbgU encodes a UDP-GlcNAc C4 epimerase, catalyzing the first committed step in the biosynthesis of 2Ac-AltUA. The enzyme catalyzes the epimerization of UDP-GlcNAc to UDP-GalNAc with high efficiency and can also interchange UDP-Glc and UDP-Gal but with much lesser efficiency. The epimerization reaction is thought to proceed via a deprotonation-reprotonation mechanism and has been the basis for the design of a potential inhibitor UDP-5F-GlcNAc. The fluorinated substrate analogue proved to be a relatively poor inhibitor.
520 $a The second step in the synthesis of UDP-2Ac-AltUA is likely catalyzed by the dehydrogenase WbgT. A series of dehydrogenase homologues from three different species were expressed in order to characterize there enzymes. The UDP-Glc dehydrogenase for E. coli was expressed successfully though it requires the use of expensive UDP-Glc substrate during purification. UDP-GalNAc dehydrogenase from P. shigelloides and P. aeruginosa proved very difficult to obtain in active form despite high expression levels. The enzymes can only be expressed in the form of inclusion bodies and despite numerous attempts at refolding, active enzymes could not be obtained.
590 $a School code: 0254.
650 4 $a Chemistry, Biochemistry. $3 1017722
650 4 $a Biology, Microbiology. $3 1017734
690 $a 0487
690 $a 0410
710 2 0 $a Wayne State University. $3 975058
773 0 $t Dissertation Abstracts International $g 65-01B.
790 1 0 $a Wang, Peng George, $e advisor
790 $a 0254
791 $a Ph.D.
792 $a 2003
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3117244