The alcohol dehydrogenases of Bacillus stearothermophilus
Citation:Glynis A. Robinson, 'The alcohol dehydrogenases of Bacillus stearothermophilus', [thesis], Trinity College (Dublin, Ireland). School of Biochemistry and Immunology, 2001, pp 309
Robinson TCD THESIS 6158 The alcohol.pdf (PDF) 204.7Mb
A 1.5-kb fragment of Bacillus stearothermophilus DSM 2334 DNA was subcloned into pUC18, and the nucleotide sequence was determined. The fragment contained a complete open reading frame that encoded a 339-residue amino-acid sequence. The deduced amino-acid sequence was typical of a bacterial, NAD+- dependent, alcohol dehydrogenase (ADH). Seven residues that constitute the ligands to two zinc ions in horse liver ADH were strictly conserved. The N-terminal amino- acid sequence (forty residues) of purified B stearothermophilus DSM 2334 alcohol dehydrogenase (ADH 2334) was determined. The amino-acid sequence-data confirmed that the nucleotide sequence of the complete open reading frame was that of the gene (adh2334) that encodes ADH 2334.
Author: Robinson, Glynis A.
Advisor:Bailey, Christopher J.
Qualification name:Doctor of Philosophy (Ph.D.)
Publisher:Trinity College (Dublin, Ireland). School of Biochemistry and Immunology
Note:TARA (Trinity's Access to Research Archive) has a robust takedown policy. Please contact us if you have any concerns: email@example.com
Type of material:thesis
Availability:Full text available