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Structural and functional studies of Secondary Metabolite AcylTransferase superfamily members from the trichothecene mycotoxin biosynthetic pathway.

Record Type:	Electronic resources : Monograph/item
Title/Author:	Structural and functional studies of Secondary Metabolite AcylTransferase superfamily members from the trichothecene mycotoxin biosynthetic pathway./
Author:	Garvey, Graeme S.
Description:	145 p.
Notes:	Adviser: Ivan Rayment.
Contained By:	Dissertation Abstracts International69-05B.
Subject:	Agriculture, General. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3314341
ISBN:	9780549635277

Structural and functional studies of Secondary Metabolite AcylTransferase superfamily members from the trichothecene mycotoxin biosynthetic pathway.
Garvey, Graeme S.

Structural and functional studies of Secondary Metabolite AcylTransferase superfamily members from the trichothecene mycotoxin biosynthetic pathway. - 145 p.

Adviser: Ivan Rayment.

Thesis (Ph.D.)--The University of Wisconsin - Madison, 2008.

Secondary metabolites represent a vast reservoir of natural chemical diversity and are derived from a limited number of precursor molecules of primary metabolism. Acyltransfer reactions catalysed within the fold of the Secondary Metabolite AcylTransferase (SMAT) family are prevalent in the biosynthetic pathways of the major secondary metabolite classes. This fold is observed in the core biosynthetic machinery of the non-ribosomal peptide synthases and in the other three secondary metabolite classes: polyketides, terpenes, and alkaloids, it is an important modifier of the basic chemical structures. Unique in this enzyme family is the frequency of substrate promiscuity for the acyl acceptor, donor, and position of acceptor acylation.

ISBN: 9780549635277Subjects--Topical Terms:

1017510
Agriculture, General.

Structural and functional studies of Secondary Metabolite AcylTransferase superfamily members from the trichothecene mycotoxin biosynthetic pathway.
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020 $a 9780549635277
035 $a (UMI)AAI3314341
035 $a AAI3314341
040 $a UMI $c UMI
100 1 $a Garvey, Graeme S. $3 1031096
245 1 0 $a Structural and functional studies of Secondary Metabolite AcylTransferase superfamily members from the trichothecene mycotoxin biosynthetic pathway.
300 $a 145 p.
500 $a Adviser: Ivan Rayment.
500 $a Source: Dissertation Abstracts International, Volume: 69-05, Section: B, page: 2973.
502 $a Thesis (Ph.D.)--The University of Wisconsin - Madison, 2008.
520 $a Secondary metabolites represent a vast reservoir of natural chemical diversity and are derived from a limited number of precursor molecules of primary metabolism. Acyltransfer reactions catalysed within the fold of the Secondary Metabolite AcylTransferase (SMAT) family are prevalent in the biosynthetic pathways of the major secondary metabolite classes. This fold is observed in the core biosynthetic machinery of the non-ribosomal peptide synthases and in the other three secondary metabolite classes: polyketides, terpenes, and alkaloids, it is an important modifier of the basic chemical structures. Unique in this enzyme family is the frequency of substrate promiscuity for the acyl acceptor, donor, and position of acceptor acylation.
520 $a The trichothecene 3-O-acetyltransferase (TRI101), is an excellent example of promiscuity for the acyl acceptor within this family. TRI101 provides self protection to trichothecene mycotoxin producing Fusarium strains, the causal agents of Fusarium Head Blight, by acetylating the core ring structure of the toxin at the C3 hydroxyl. In an effort to control this serious cereal crop disease, transgenic cereal crops expressing TRI101 from F. sporotrichioides were generated, however these performed poorly in field trials. The X-ray crystallographic and kinetic studies of TRI101 enzymes from both A and B type mycotoxin producers provide a structural basis for understanding the poor field performance of the tri101 transgenic crops.
520 $a The second SMAT family member in the trichothecene biosynthetic pathway, trichothecene 15-O-acetyltransferase (TRI3), acetylates the C15 hydroxyl moiety. The product of this enzyme, calonectrin, is the last common intermediate in the biosynthetic pathways of A and B type trichothecenes. The X-ray crystallographic and kinetic studies of TRI3 reveal that this enzyme is an efficient catalyst with its native substrate, is not promiscuous with final mycotoxins, and the residues which line the active site are strictly conserved across A and B type trichothecene producers.
520 $a In Chapter four, the results of a collaborative project to functionally characterize PrpF are presented. PrpF is an enzyme involved in the 2-methyl citrate catabolic pathway. The X-ray crystallographic study revealed strong structural homology of PrpF to the non-PLP dependent diaminopimelate epimerase, which allowed an activity of epimerization to be hypothesized and experimentally validated.
590 $a School code: 0262.
650 4 $a Agriculture, General. $3 1017510
650 4 $a Agriculture, Plant Pathology. $3 1028950
650 4 $a Chemistry, Biochemistry. $3 1017722
690 $a 0473
690 $a 0480
690 $a 0487
710 2 $a The University of Wisconsin - Madison. $3 626640
773 0 $t Dissertation Abstracts International $g 69-05B.
790 $a 0262
790 1 0 $a Rayment, Ivan, $e advisor
791 $a Ph.D.
792 $a 2008
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3314341