Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1111/j.1432-1033.1972.tb01968.x | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Mechanism of the Flavoprotein d-6-Hydroxynicotine Oxidase: Substrate Specificity, pH and Solvent Isotope Effects, and Roles of Key Active-Site Residues.
Biochemistry
May 2019
Department of Chemistry , St. Mary's University, San Antonio , Texas 78228 , United States.
The flavoprotein d-6-hydroxynicotine oxidase catalyzes an early step in the oxidation of ( R)-nicotine, the oxidation of a carbon-nitrogen bond in the pyrrolidine ring of ( R)-6-hydroxynicotine. The enzyme is a member of the vanillyl alcohol oxidase/ p-cresol methylhydroxylase family of flavoproteins. The effects of substrate modifications on the steady-state and rapid-reaction kinetic parameters are not consistent with the quinone-methide mechanism of p-cresol methylhydroxylase.
View Article and Find Full Text PDFInduction of D-6-hydroxynicotine oxidase in resting cells of Arthrobacter oxidans.
Arch Microbiol
December 1976
Resting cell suspensions of Arthrobacter oxidans were shown to synthesize the inducible enantiozyme, D-6-hydroxynicotine oxidase, in the presence of D-nicotine or D-6-hydroxynicotine. The corresponding L-enantiomers, as well as gamma-methylaminopropyl-(6-OH-pyridyl-3)-ketone, which is the product of the reaction catalyzed by the enzyme, were ineffective as inducers. L-6-Hydroxynicotine inhibited induction by D-nicotine and D-6-hydroxynicotine while L-nicotine inhibited induction by D-6-hydroxynicotine and had no effect on induction by D-nicotine.
View Article and Find Full Text PDFAntersera prepared against both enantiozymes, D- and L-6-hydroxynicotine oxidase, formed precipitins in double diffusion tests with their respective antigens only. A mixture of the two antisera caused spur formation of the two precipitin lines obtained with the pure enzymes. Antiserum to L-apoprotein reacted with native L-enzyme and L-apoprotein but not with the D-sspecific enzyme.
View Article and Find Full Text PDFCovalently bound flavin in D-6-hydroxynicotine oxidase from Arthrobacter oxidans.
Z Naturforsch B Anorg Chem Org Chem Biochem Biophys Biol
September 1972
Want AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!