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Active site mapping of iterative pol...

University of California, San Diego., Chemistry.

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Active site mapping of iterative polyketide synthases and the detection of polyketide intermediates using high-resolution Fourier transform mass spectrometry.

Record Type:	Language materials, printed : Monograph/item
Title/Author:	Active site mapping of iterative polyketide synthases and the detection of polyketide intermediates using high-resolution Fourier transform mass spectrometry./
Author:	Meehan, Michael Jospeh.
Description:	164 p.
Notes:	Adviser: Pieter C. Dorrestein.
Contained By:	Masters Abstracts International47-06.
Subject:	Chemistry, Analytical. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoeng/servlet/advanced?query=1464918
ISBN:	9781109166651

Active site mapping of iterative polyketide synthases and the detection of polyketide intermediates using high-resolution Fourier transform mass spectrometry.
Meehan, Michael Jospeh.

Active site mapping of iterative polyketide synthases and the detection of polyketide intermediates using high-resolution Fourier transform mass spectrometry. - 164 p.

Adviser: Pieter C. Dorrestein.

Thesis (M.S.)--University of California, San Diego, 2009.

In an attempt to better understand the biosynthesis of the enediyne core of the antitumor compound C-1027 by SgcE and to investigated the iterative steps involved in the formation of the methylbutyrl side-chain of lovastatin by LovF, high resolution mass spectrometry was used to identify peptides containing domain active sites of these polyketide synthases and to determine with very high mass accuracy the mass of substrates covalently attached to the active site. In particular the phosphopantetheinyl ejection assay was used to successfully detect the formation of the methylbutyrate by LovF on the ACP active site. It was found that methylbutyrate is detectable only at very low substrate concentrations, but complete formation of the product was carried out by LovF. SgcE was found to be active and capable of catalyzing elongation of a polyene intermediate. The substrate loading and one iteration of elongation were detected using mass spectrometry and the phosphopantetheinyl ejection assay. The results from these experiments showed the power of high-resolution mass spectrometry in studying the mechanisms of action by which these iterative polyketide synthases function and form their fully elongated products.

ISBN: 9781109166651Subjects--Topical Terms:

586156
Chemistry, Analytical.

Active site mapping of iterative polyketide synthases and the detection of polyketide intermediates using high-resolution Fourier transform mass spectrometry.
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005 20100709
008 100709s2009 ||||||||||||||||| ||eng d
020 $a 9781109166651
035 $a (UMI)AAI1464918
035 $a AAI1464918
040 $a UMI $c UMI
100 1 $a Meehan, Michael Jospeh. $3 1024151
245 1 0 $a Active site mapping of iterative polyketide synthases and the detection of polyketide intermediates using high-resolution Fourier transform mass spectrometry.
300 $a 164 p.
500 $a Adviser: Pieter C. Dorrestein.
500 $a Source: Masters Abstracts International, Volume: 47-06, page: .
502 $a Thesis (M.S.)--University of California, San Diego, 2009.
520 $a In an attempt to better understand the biosynthesis of the enediyne core of the antitumor compound C-1027 by SgcE and to investigated the iterative steps involved in the formation of the methylbutyrl side-chain of lovastatin by LovF, high resolution mass spectrometry was used to identify peptides containing domain active sites of these polyketide synthases and to determine with very high mass accuracy the mass of substrates covalently attached to the active site. In particular the phosphopantetheinyl ejection assay was used to successfully detect the formation of the methylbutyrate by LovF on the ACP active site. It was found that methylbutyrate is detectable only at very low substrate concentrations, but complete formation of the product was carried out by LovF. SgcE was found to be active and capable of catalyzing elongation of a polyene intermediate. The substrate loading and one iteration of elongation were detected using mass spectrometry and the phosphopantetheinyl ejection assay. The results from these experiments showed the power of high-resolution mass spectrometry in studying the mechanisms of action by which these iterative polyketide synthases function and form their fully elongated products.
590 $a School code: 0033.
650 4 $a Chemistry, Analytical. $3 586156
650 4 $a Chemistry, Biochemistry. $3 1017722
690 $a 0486
690 $a 0487
710 2 $a University of California, San Diego. $b Chemistry. $3 1023460
773 0 $t Masters Abstracts International $g 47-06.
790 $a 0033
790 1 0 $a Bafna, Vineet $e committee member
790 1 0 $a Burkart, Michael $e committee member
790 1 0 $a Dorrestein, Pieter C., $e advisor
791 $a M.S.
792 $a 2009
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoeng/servlet/advanced?query=1464918