Date of Award

1-1-2010

Language

English

Document Type

Dissertation

Degree Name

Doctor of Philosophy (PhD)

College/School/Department

Department of Chemistry

Content Description

1 online resource (xiv, 146 pages) : illustrations (some color)

Dissertation/Thesis Chair

Rabi A Musah

Committee Members

Charles P Scholes, Alexander Shekhtman, Igor K Lednev, Hua Shi

Keywords

alliinase, lachrymatory factor synthase, Petiveria alliacea, Alliaceae, Alliinase, Plant enzymes

Subject Categories

Biochemistry

Abstract

Isolation and characterization of an alliinase and a lachrymatory factor synthase from the Amazonian medicinal plant Petiveria alliacea is reported. The alliinase is unusual in that it is heteromeric, whereas all previous reports of characterized alliinases have shown them to be monomers or homomultimers. The protein possesses 5 subunits: two alpha subunits which are glycosylated and connected by a disulfide bond, and beta, gamma and delta subunits. The alliinase exhibits broad substrate specificity, reacting with S-substituted-L-cysteine sulfoxides with aromatic, aliphatic, alkenyl and polar side chains. The alliinase-mediated breakdown of a variety of cysteine sulfoxide derivatives yields transitory sulfenic acid intermediate that condense with loss of water to form thiosulfinates.

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