Thesis (M. Med. Sc.)--University of Hong Kong, 2001. / Includes bibliographical references (leaves 30-33).

Thesis (Ph. D.)--University of Adelaide, Dept. of Microbiology and Immunology, 1989. / "Erratum" [i.e. Errata] inserted. Includes bibliographical references.

Thesis (Ph.D.) - University of Glasgow, 2007. / Ph.D. thesis submitted to the Institute of Comparative Medicine, Faculty of Veterinary Medicine, University of Glasgow, 2007. Includes bibliographical references. Print version also available.

Thesis (M.Med.Sc.)--University of Hong Kong, 2001. / Includes bibliographical references (leaves 30-33). Also available in print.

München, Univ., Diss., 2002. / Computerdatei im Fernzugriff.

München, Univ., Diss., 2002. / Computerdatei im Fernzugriff.

Thesis (Ph. D.)--University of Washington, 2003. / Vita. Includes bibliographical references (leaves 105-123).

Thesis (Ph. D.)--University of Adelaide, Dept. of Microbiology and Immunology, 1988. / Includes bibliographical references (leaves 126-171).

Thesis (Ph. D.)--West Virginia University, 1999. / Title from document title page. Document formatted into pages; contains xiii, 145 p. : ill. (some col.) Includes abstract. Includes bibliographical references.

Initial velocity studies of O-acetylserine sulfhydrylase-B (OASS-B) from Salmonella typhimurium using both natural and alternative substrates suggest a Bi Bi ping pong kinetic mechanism with double substrate competitive inhibition. The ping pong mechanism is corroborated by a qualitative and quantitative analysis of product and dead-end inhibition. Product inhibition by acetate is S-parabolic noncompetitive, indication of a combination of acetate with E followed by OAS. These data suggest some randomness to the OASS-B kinetic mechanism. The pH dependence of kinetic parameters was determined in order to obtain information on the acid-base chemical mechanism for the OASS-B reaction. A mechanism is proposed in which an enzyme general base accepts a proton from α-amine of O-acetylserine, while a second enzyme general base acts by polarizing the acetyl carbonyl assisting in the β-elimination of the acetyl group of O-acetylserine. The ε-amine of the active site lysine acts as a general base to abstract the α-proton in the β-elimination of acetate. At the end of the first half reaction the ε-amine of the active site lysine that formed the internal Schiff base and the general base are protonated. The resulting α-aminoacrylate intermediate undergoes a Michael addition with HS‾ and the active site lysine donates its proton to the α-carbon to give cysteine and regenerate enzyme to start the second half reaction. In addition, substrate specificity, stereochemistry of the internal Schiff base at C4', and sequence around active site lysine of O-acetylserine sulfhydrylase-A have been determined. The [4'-^3H]pyridoxamine generated by reduction of the internal Schiff base with sodium [^3H]borohydride retained most of its tritium after incubation with apoaspartate aminotransferase. These results agree with the hypothesis put forth by Dunathan (Dunathan, 1971; Dunathan and Voet, 1974) that a single surface (Re face) of the active site PLP is accessible to solvent. The sequence around the active site lysine is AsnProSerPheSerValLysCysArg.