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Evolution of DAHP synthase: From arc...

Zhou, Mi.

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Evolution of DAHP synthase: From archaea to eubacteria.

紀錄類型:	書目-語言資料,印刷品 : Monograph/item
正題名/作者:	Evolution of DAHP synthase: From archaea to eubacteria./
作者:	Zhou, Mi.
面頁冊數:	121 p.
附註:	Adviser: Ronald W. Woodard.
Contained By:	Dissertation Abstracts International68-02B.
標題:	Chemistry, Biochemistry. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3253448

Evolution of DAHP synthase: From archaea to eubacteria.
Zhou, Mi.

Evolution of DAHP synthase: From archaea to eubacteria. - 121 p.

Adviser: Ronald W. Woodard.

Thesis (Ph.D.)--University of Michigan, 2007.

To combat the increased resistance of pathogenic bacteria, there needs to be incessant expansion of our standard antibacterial agents. 3-Deoxy- D-arabino-heptulosonate-7-phosphate synthase (DAHPS), the first enzyme in the shikimate pathway, which catalyzes the formation of DAHP from phospho enolpyruvate (PEP) and D-erythrose 4-phosphate, proves to be an interesting target for the design of antimicrobial agents since the shikimate pathway is absent in mammals.Subjects--Topical Terms:

1017722
Chemistry, Biochemistry.

Evolution of DAHP synthase: From archaea to eubacteria.
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245 1 0 $a Evolution of DAHP synthase: From archaea to eubacteria.
300 $a 121 p.
500 $a Adviser: Ronald W. Woodard.
500 $a Source: Dissertation Abstracts International, Volume: 68-02, Section: B, page: 0962.
502 $a Thesis (Ph.D.)--University of Michigan, 2007.
520 $a To combat the increased resistance of pathogenic bacteria, there needs to be incessant expansion of our standard antibacterial agents. 3-Deoxy- D-arabino-heptulosonate-7-phosphate synthase (DAHPS), the first enzyme in the shikimate pathway, which catalyzes the formation of DAHP from phospho enolpyruvate (PEP) and D-erythrose 4-phosphate, proves to be an interesting target for the design of antimicrobial agents since the shikimate pathway is absent in mammals.
520 $a DAHPSs from microorganisms vary in length of primary amino acid sequence, as well as their modes of regulation or lack of regulation. These differences have a profound effect on how inhibitors function; therefore, there is an urgent need to understand these differences for the rational design of inhibitors.
520 $a This thesis examines several different DAHPSs, including an archaeal DAHPS from Aeropyrum pernix (DAHPSAp), to illustrate that DAHPSS evolved from an ancient (beta/alpha) 8 barrel scaffold to more sophisticated (beta/alpha)8 barrels containing domains and insertions for feedback regulation. DAHPS Ap and the 260 residue Thermoanaerobacter tengcongensis DAHPS (DAHPSTt-short) are both unregulated DAHPS. The crystal structure of DAHPSAp shows only the (beta/alpha)8 barrel, which catalyzes the formation of DAHP. The 338 residue Thermoanaerobacter tengcongensis DAHPS (DAHPSTt-long) and the previously characterized Thermotoga maritima DAHPS (DAHPSTm) each have a regulatory domain at the N-terminus and are regulated by L-Phe and L-Tyr. Furthermore, the implications of domain truncation, appendage, and/or swapping are examined through creation and characterization of several truncated and fusion proteins from DAHPSAp, DAHPSTm, DAHPSTt-long, and DAHPSTt-short. Finally, a model mimicking the feedback inhibition of DAHPTm by L-Tyr is created from preliminary crystallographic data and characterization results.
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791 $a Ph.D.
792 $a 2007
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