FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2000421888> ?p ?o ?g. }

• W2000421888 endingPage "4694" @default.
• W2000421888 startingPage "4683" @default.
• W2000421888 abstract "The expression of a copper amine oxidase (CAO) from Hansenula polymorpha in Saccharomyces cerevisiae under differing culture conditions leads to the incorporation of varied levels of CAO-bound zinc. The presence of substantial amount of zinc results in two distinctive enzyme species, designated as the fast and slow enzymes. Both forms are rapidly reduced by substrate methylamine with a rate constant of 199 s(-1) but behave remarkably differently in their oxidation rates; the fast enzyme is oxidized by dioxygen at a rate of 22.1 s(-1), whereas the slow enzyme reacts at a rate of 1.8 x 10(-4) s(-1). The apparent kcat of the enzyme preparation is linearly proportional to the fraction of the fast enzyme, with an extrapolated value of 6.17 s(-1) when the enzyme is 100% in its fast form. A comparison of rate constants for cofactor reduction and reoxidation steps, measured in stopped flow experiments, to the extrapolated kcat implicates additional steps in the steady state reaction. Measurement of the proportion of oxidized (ETPQ(ox)) and reduced cofactor (ETPQ(red)) under steady state conditions indicates approximately 50% of each cofactor form at 0.8 or 2 mM methylamine. Kinetic isotope effect measurements using deuterated amine substrate lead to the following steady state values: (D)(k(red)) = 8.5 (0.5), (D)(kcat) = 1.7 (0.1), and (D)(kcat/K(m)) = 4.3 (0.2). The collective data allow the calculation of partially rate-determining constants during the reductive half-reaction (ca. 200 s(-1) for binding of substrate to ETPQ(ox) and 27.9 s(-1) for release of aldehyde product or a protein isomerization from ETPQ(red)); an additional step with a rate constant of 13.2 s(-1) is assigned to the oxidative half-reaction, most likely for the release of product hydrogen peroxide. These results, together with the sole detection of oxidized and reduced cofactor during rapid scanning stopped flow experiments, indicate that four steps contribute to kcat, with the first electron transfer from cofactor to O2 contributing ca. 29%. An investigation of the relationship between the copper content and the extent of the fast enzyme shows that only the copper-containing homodimer is capable of rapid reoxidation and that zinc-copper heterodimers are incapable of rapid turnover at either subunit. This implies communication between the metal sites of the two subunits per dimer that impacts O2 binding and/or electron transfer from reduced cofactor to bound O2." @default.
• W2000421888 created "2016-06-24" @default.
• W2000421888 creator A5026791298 @default.
• W2000421888 creator A5066409965 @default.
• W2000421888 date "2006-03-21" @default.
• W2000421888 modified "2023-09-27" @default.
• W2000421888 title "Relationship of Stopped Flow to Steady State Parameters in the Dimeric Copper Amine Oxidase from <i>Hansenula polymorpha </i>and the Role of Zinc in Inhibiting Activity at Alternate Copper-Containing Subunits" @default.
• W2000421888 cites W1576384803 @default.
• W2000421888 cites W171746247 @default.
• W2000421888 cites W1977256489 @default.
• W2000421888 cites W1981940760 @default.
• W2000421888 cites W2001698467 @default.
• W2000421888 cites W2005575697 @default.
• W2000421888 cites W2005781284 @default.
• W2000421888 cites W2069492842 @default.
• W2000421888 cites W2116838198 @default.
• W2000421888 cites W2339755204 @default.
• W2000421888 cites W2413934543 @default.
• W2000421888 doi "https://doi.org/10.1021/bi0521893" @default.
• W2000421888 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/16584203" @default.
• W2000421888 hasPublicationYear "2006" @default.
• W2000421888 type Work @default.
• W2000421888 sameAs 2000421888 @default.
• W2000421888 citedByCount "18" @default.
• W2000421888 countsByYear W20004218882012 @default.
• W2000421888 countsByYear W20004218882013 @default.
• W2000421888 countsByYear W20004218882016 @default.
• W2000421888 countsByYear W20004218882017 @default.
• W2000421888 countsByYear W20004218882022 @default.
• W2000421888 crossrefType "journal-article" @default.
• W2000421888 hasAuthorship W2000421888A5026791298 @default.
• W2000421888 hasAuthorship W2000421888A5066409965 @default.
• W2000421888 hasConcept C117001961 @default.
• W2000421888 hasConcept C121332964 @default.
• W2000421888 hasConcept C131779359 @default.
• W2000421888 hasConcept C148898269 @default.
• W2000421888 hasConcept C155647269 @default.
• W2000421888 hasConcept C178790620 @default.
• W2000421888 hasConcept C179104552 @default.
• W2000421888 hasConcept C181199279 @default.
• W2000421888 hasConcept C185592680 @default.
• W2000421888 hasConcept C18903297 @default.
• W2000421888 hasConcept C197957613 @default.
• W2000421888 hasConcept C2777289219 @default.
• W2000421888 hasConcept C2778969155 @default.
• W2000421888 hasConcept C41183919 @default.
• W2000421888 hasConcept C535196362 @default.
• W2000421888 hasConcept C56856141 @default.
• W2000421888 hasConcept C58364064 @default.
• W2000421888 hasConcept C62520636 @default.
• W2000421888 hasConcept C69928629 @default.
• W2000421888 hasConcept C71240020 @default.
• W2000421888 hasConcept C73969872 @default.
• W2000421888 hasConcept C8171440 @default.
• W2000421888 hasConcept C86803240 @default.
• W2000421888 hasConcept C93391505 @default.
• W2000421888 hasConceptScore W2000421888C117001961 @default.
• W2000421888 hasConceptScore W2000421888C121332964 @default.
• W2000421888 hasConceptScore W2000421888C131779359 @default.
• W2000421888 hasConceptScore W2000421888C148898269 @default.
• W2000421888 hasConceptScore W2000421888C155647269 @default.
• W2000421888 hasConceptScore W2000421888C178790620 @default.
• W2000421888 hasConceptScore W2000421888C179104552 @default.
• W2000421888 hasConceptScore W2000421888C181199279 @default.
• W2000421888 hasConceptScore W2000421888C185592680 @default.
• W2000421888 hasConceptScore W2000421888C18903297 @default.
• W2000421888 hasConceptScore W2000421888C197957613 @default.
• W2000421888 hasConceptScore W2000421888C2777289219 @default.
• W2000421888 hasConceptScore W2000421888C2778969155 @default.
• W2000421888 hasConceptScore W2000421888C41183919 @default.
• W2000421888 hasConceptScore W2000421888C535196362 @default.
• W2000421888 hasConceptScore W2000421888C56856141 @default.
• W2000421888 hasConceptScore W2000421888C58364064 @default.
• W2000421888 hasConceptScore W2000421888C62520636 @default.
• W2000421888 hasConceptScore W2000421888C69928629 @default.
• W2000421888 hasConceptScore W2000421888C71240020 @default.
• W2000421888 hasConceptScore W2000421888C73969872 @default.
• W2000421888 hasConceptScore W2000421888C8171440 @default.
• W2000421888 hasConceptScore W2000421888C86803240 @default.
• W2000421888 hasConceptScore W2000421888C93391505 @default.
• W2000421888 hasIssue "14" @default.
• W2000421888 hasLocation W20004218881 @default.
• W2000421888 hasLocation W20004218882 @default.
• W2000421888 hasOpenAccess W2000421888 @default.
• W2000421888 hasPrimaryLocation W20004218881 @default.
• W2000421888 hasRelatedWork W1551283513 @default.
• W2000421888 hasRelatedWork W2000421888 @default.
• W2000421888 hasRelatedWork W2015676956 @default.
• W2000421888 hasRelatedWork W2017515303 @default.
• W2000421888 hasRelatedWork W2025788670 @default.
• W2000421888 hasRelatedWork W2029587448 @default.
• W2000421888 hasRelatedWork W2077211817 @default.
• W2000421888 hasRelatedWork W2370792838 @default.
• W2000421888 hasRelatedWork W2949445124 @default.
• W2000421888 hasRelatedWork W2189239354 @default.
• W2000421888 hasVolume "45" @default.
• W2000421888 isParatext "false" @default.
• W2000421888 isRetracted "false" @default.

• next