Chemical modification of salicylate hydroxylase

Simple item page
dc.contributor.advisorTu, Shiao-Chun
dc.contributor.committeeMemberKimball, Aubrey P.
dc.contributor.committeeMemberNelson, Daniel A.
dc.contributor.committeeMemberKohn, Harold Lewis
dc.creatorPaquatte, Olivier
dc.date.accessioned2024-04-22T20:17:11Z
dc.date.available2024-04-22T20:17:11Z
dc.date.issued1985
dc.description.abstractSalicylate hydroxylase from Pseudomonas cepacia was found to be inactivated by phenyl glyoxal, a reagent specific for arginyl residues. The reaction was found to display pseudo-first order kinetics but was not retarded by the addition of any of the substrates before initiating the inactivation. This suggests that the modification does not take place at the enzyme active site. Salicylate hydroxylase can also be effectively inactivated by di ethyl pyrocarbonate, a reagent highly reactive with histidyl residues. The enzyme inactivation was retarded by the addition of salicylate but not NADH, suggesting the modification was limited to the salicylate substrate site. However, the inactivation of enzyme with an excess amount of di ethyl pyrocarbonate did not display pseudo-first order kinetics, due to the appreciable autodecay of the reagent in an aqueous medium. A new method is described for the determination of both the pseudo-first order rate constant and the second order rate constant for the enzyme inactivation by a reagent such as di ethyl pyrocarbonate, which undergoes exponential decays. The validity of this method has been demonstrated by the successful application to the analysis of results of salicylate hydroxylase and bacterial luciferase inactivations by diethyl pyrocarbonate. The effects of temperature, pH and concentration of phosphate buffer on the stability of this reagent have been examined.
dc.description.departmentBiology and Biochemistry, Department of
dc.format.digitalOriginreformatted digital
dc.format.mimetypeapplication/pdf
dc.identifier.other13166218
dc.identifier.urihttps://hdl.handle.net/10657/17001
dc.language.isoen
dc.rightsThis item is protected by copyright but is made available here under a claim of fair use (17 U.S.C. Section 107) for non-profit research and educational purposes. Users of this work assume the responsibility for determining copyright status prior to reusing, publishing, or reproducing this item for purposes other than what is allowed by fair use or other copyright exemptions. Any reuse of this item in excess of fair use or other copyright exemptions requires express permission of the copyright holder.
dc.subjectSalicylates
dc.subjectHydroxylation
dc.subjectLuminous bacteria
dc.subjectEnzymes
dc.titleChemical modification of salicylate hydroxylase
dc.type.dcmiText
dc.type.genreThesis
thesis.degree.collegeCollege of Natural Sciences and Mathematics
thesis.degree.departmentBiochemical and Biophysical Sciences, Department of
thesis.degree.disciplineBiochemical and Biophysical Sciences
thesis.degree.grantorUniversity of Houston
thesis.degree.levelMasters
thesis.degree.nameMaster of Science

Files

Original bundle

Now showing 1 - 1 of 1
No Thumbnail Available
Name:
Paquatte_1985_13166218.pdf
Size:
1.35 MB
Format:
Adobe Portable Document Format
Download

Collections

Legacy Theses and Dissertations (1940-2009)