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Novel substrates of sugar nucleotide...

Sweet, Charles Robert.

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Novel substrates of sugar nucleotide acyltransferases that initiate lipid A biosynthesis.

紀錄類型:	書目-語言資料,印刷品 : Monograph/item
正題名/作者:	Novel substrates of sugar nucleotide acyltransferases that initiate lipid A biosynthesis./
作者:	Sweet, Charles Robert.
面頁冊數:	305 p.
附註:	Source: Dissertation Abstracts International, Volume: 63-09, Section: B, page: 4164.
Contained By:	Dissertation Abstracts International63-09B.
標題:	Biology, Microbiology. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3063208
ISBN:	0493819649

Novel substrates of sugar nucleotide acyltransferases that initiate lipid A biosynthesis.
Sweet, Charles Robert.

Novel substrates of sugar nucleotide acyltransferases that initiate lipid A biosynthesis. - 305 p.

Source: Dissertation Abstracts International, Volume: 63-09, Section: B, page: 4164.

Thesis (Ph.D.)--Duke University, 2002.

The acylation of UDP-<italic>N</italic>-acetylglucosamine is the first step in the canonical biosynthesis of lipid A, a unique glycolipid that is the predominant structural component of the outer leaflet of the outer membrane of Gram-negative bacteria. This acylation reaction is catalyzed by UDP-<italic>N</italic>-acetylglucosamine acyltransferase, LpxA. The unusual substrates and substrate specificities of the LpxA proteins studied in this thesis generate distinct lipid A structural variations, as compared to the archetype structure of <italic>Escherichia coli</italic>, hexa-acyl Kdo<sub> 2</sub>-lipid A. This structural diversity may have important effects on the function of lipid A as a structural component of the cellular envelope and as endotoxin, a primary mediator of the eukaryotic innate immune response to Gram-negative infection. This dissertation describes elucidation of the genetic and enzymatic basis of these structural variations.

ISBN: 0493819649Subjects--Topical Terms:

1017734
Biology, Microbiology.

Novel substrates of sugar nucleotide acyltransferases that initiate lipid A biosynthesis.
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100 1 $a Sweet, Charles Robert. $3 1251353
245 1 0 $a Novel substrates of sugar nucleotide acyltransferases that initiate lipid A biosynthesis.
300 $a 305 p.
500 $a Source: Dissertation Abstracts International, Volume: 63-09, Section: B, page: 4164.
500 $a Supervisor: C. R. H. Raetz.
502 $a Thesis (Ph.D.)--Duke University, 2002.
520 $a The acylation of UDP-<italic>N</italic>-acetylglucosamine is the first step in the canonical biosynthesis of lipid A, a unique glycolipid that is the predominant structural component of the outer leaflet of the outer membrane of Gram-negative bacteria. This acylation reaction is catalyzed by UDP-<italic>N</italic>-acetylglucosamine acyltransferase, LpxA. The unusual substrates and substrate specificities of the LpxA proteins studied in this thesis generate distinct lipid A structural variations, as compared to the archetype structure of <italic>Escherichia coli</italic>, hexa-acyl Kdo<sub> 2</sub>-lipid A. This structural diversity may have important effects on the function of lipid A as a structural component of the cellular envelope and as endotoxin, a primary mediator of the eukaryotic innate immune response to Gram-negative infection. This dissertation describes elucidation of the genetic and enzymatic basis of these structural variations.
520 $a Specifically, this work explores (1) The presence of 3 and 3<super> ′</super> primary acyl chains that lack hydroxyl groups in <italic> Chlamydia trachomatis</italic>, (2) The incorporation of multiple lengths of 3-OH acyl chain in 3 and 3<super>′</super> primary acyl positions of <italic>Bordetella</italic> species, and (3) The biosynthetic origin of lipid A containing 2,3-diamino-2,3-dideoxy-D-glucose as a backbone sugar. The latter effort involved not only the characterization of LpxA proteins with novel sugar nucleotide specificity, but also the discovery of two <italic> Acidithiobacillus ferrooxidans</italic> proteins, GnnA and GnnB, which are necessary and sufficient for the conversion of UDP-<italic>N</italic>-acetylglucosamine to UDP-2-<italic>N</italic>-acetyl-2,3-diamino-2,3-dideoxy-D-glucose, a novel sugar nucleotide that is the precursor of lipid A containing 2,3-diamino-2,3-dideoxy-D-glucose as a backbone sugar.
520 $a The substrate specificities of the LpxA acyltransferase enzymes were characterized by <italic>in vitro</italic> thin-layer chromatography assays of acyltransferase activity and <italic>in vivo</italic> by complementation of a temperature-sensitive <italic>E. coli</italic> mutant, <italic>lpxA2 </italic>. These activities were further examined by MALDI-TOF mass spectrometry of the hybrid lipid A structures isolated from the <italic>lpxA2</italic> conditional mutant covered with the foreign <italic>lpxA</italic> genes. The <italic> A. ferrooxidans</italic> genes <italic>gnnA</italic> and <italic>gnnB</italic> were cloned and expressed in <italic>E. coli</italic>, and the proteins were purified and characterized by <italic>in vitro</italic> thin-layer chromatography activity assays. Furthermore, the <italic>in vitro</italic> reaction product UDP-2-<italic>N</italic>-acetyl-2,3-diamino-2,3-dideoxy-D-glucose was purified by ion-exchange chromatography and characterized by one- and two-dimensional NMR spectroscopy.
590 $a School code: 0066.
650 4 $a Biology, Microbiology. $3 1017734
650 4 $a Chemistry, Biochemistry. $3 1017722
690 $a 0410
690 $a 0487
710 2 0 $a Duke University. $3 569686
773 0 $t Dissertation Abstracts International $g 63-09B.
790 $a 0066
790 1 0 $a Raetz, C. R. H., $e advisor
791 $a Ph.D.
792 $a 2002
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3063208