Date of Award

8-7-2024

Author's School

Graduate School of Arts and Sciences

Author's Department

Biology & Biomedical Sciences (Plant & Microbial Biosciences)

Degree Name

Doctor of Philosophy (PhD)

Degree Type

Dissertation

Abstract

In Brassica plants, glucosinolates are a diverse class of natural products that serve as plant defense molecules. Their structural diversity comes from the use of amino acids as precursors and elongation of side chains by up to nine carbons, as well as further chemical modifications. Aliphatic methionine-derived glucosinolates are the most abundant form of these compounds. Although both elongation and chemical modification of amino acid sidechains are important for methionine-glucosinolate diversity, its elongation process has not been well described. The chain elongation enzyme methylthioalkylmalate synthase (MAMS) functions as the glucosinolate pathway gatekeeper through its substrate specificity. The x-ray crystal structure of MAMS has only recently been solved and biochemical studies of the enzyme have yet to be carried out. Here we describe the studies that examine the kinetic and chemical mechanisms of Brassica juncea (Indian mustard) MAMS isoforms through initial velocity and mutagenesis studies. These studies were made possible using a 4-aldithriol-based MAMS assay that we developed. We also analyze the evolution of MAMS substrate specificity from alpha-isopropylmalate synthase (IPMS), of which MAMS is a homolog, through structural/sequence comparison methods, and discuss efforts to determine the x-ray crystallography structure of Brassica rapa IPMS. Overall, this work highlights the importance of localized structural changes in the active site for the evolution of substrate specificity in Claisen-condensing enzymes despite the conservation of chemistry. This work also provides more insights into the structure and biochemistry of MAMS, which are a useful addition to the breadth of knowledge required for efforts in metabolically engineering glucosinolates in plants and bacteria for plant defense, human health, and nutrition.

Language

English (en)

Chair and Committee

Joseph Jez

Committee Members

Hani Zaher; Robert Kranz; Tim Wencewicz; Toni Kutchan

Available for download on Wednesday, November 19, 2025

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