Matches in SemOpenAlex for { <https://semopenalex.org/work/W2051865460> ?p ?o ?g. }
Showing items 1 to 71 of
71
with 100 items per page.
- W2051865460 endingPage "11388" @default.
- W2051865460 startingPage "11381" @default.
- W2051865460 abstract "The copper amine oxidases (CAOs) catalyze the O2-dependent, two-electron oxidation of amines to aldehydes at an active site that contains Cu(II) and topaquinone (TPQ) cofactor. TPQ arises from the autocatalytic, post-translational oxidation of a tyrosine side chain in the active site. Monooxygenation within the ring of tyrosine at a single Cu(II) site is unique in biology and occurs as an early step in the formation of TPQ. The mechanism of this reaction has been further examined in the CAO from Hansenula polymorpha (HPAO). When a Clark electrode fitted to a custom-made, gastight apparatus over a range of initial concentrations of O2 was used, rates of O2 consumption at levels greater than air are seen to be reduced relative to earlier results, yielding KD(apparent) = 216 μM for O2. This is consistent with a mechanism in which O2 binds reversibly to the active site, triggering a conformational change that promotes ligation of tyrosinate to Cu(II). The activated Cu(II)-tyrosinate species has been proposed to react with O2 in a rate-limiting step, although it was also possible that breakdown of a putative peroxy-intermediate controlled TPQ formation. To test the latter hypothesis, Cu(II)-free HPAO was prepared with 3,5-ring-[2H2]-tyrosine incorporated throughout the primary sequence. The absence of an isotope effect on the rate of TPQ formation eliminates cleavage of this C−H bond in a proposed Cu(II)-aryl-peroxide intermediate as a rate limiting step. The role of methionine 634, previously found to moderate O2 binding during the catalytic cycle, is shown here to serve a similar function in TPQ formation. As with catalysis, the rate of TPQ formation correlates with the volume of the hydrophobic side chain at position 634, implicating similar binding sites for O2 during catalysis and cofactor biogenesis." @default.
- W2051865460 created "2016-06-24" @default.
- W2051865460 creator A5066409965 @default.
- W2051865460 creator A5090153715 @default.
- W2051865460 date "2005-08-01" @default.
- W2051865460 modified "2023-10-03" @default.
- W2051865460 title "The Nature of O<sub>2</sub> Reactivity Leading to Topa Quinone in the Copper Amine Oxidase from <i>Hansenula polymorpha</i> and Its Relationship to Catalytic Turnover" @default.
- W2051865460 doi "https://doi.org/10.1021/bi0504759" @default.
- W2051865460 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/16114875" @default.
- W2051865460 hasPublicationYear "2005" @default.
- W2051865460 type Work @default.
- W2051865460 sameAs 2051865460 @default.
- W2051865460 citedByCount "21" @default.
- W2051865460 countsByYear W20518654602012 @default.
- W2051865460 countsByYear W20518654602013 @default.
- W2051865460 countsByYear W20518654602014 @default.
- W2051865460 countsByYear W20518654602015 @default.
- W2051865460 countsByYear W20518654602016 @default.
- W2051865460 countsByYear W20518654602017 @default.
- W2051865460 countsByYear W20518654602019 @default.
- W2051865460 countsByYear W20518654602021 @default.
- W2051865460 countsByYear W20518654602022 @default.
- W2051865460 crossrefType "journal-article" @default.
- W2051865460 hasAuthorship W2051865460A5066409965 @default.
- W2051865460 hasAuthorship W2051865460A5090153715 @default.
- W2051865460 hasConcept C131779359 @default.
- W2051865460 hasConcept C161790260 @default.
- W2051865460 hasConcept C178790620 @default.
- W2051865460 hasConcept C185592680 @default.
- W2051865460 hasConcept C2776165026 @default.
- W2051865460 hasConcept C2780643102 @default.
- W2051865460 hasConcept C37263863 @default.
- W2051865460 hasConcept C41183919 @default.
- W2051865460 hasConcept C544778455 @default.
- W2051865460 hasConcept C55493867 @default.
- W2051865460 hasConcept C71240020 @default.
- W2051865460 hasConcept C75473681 @default.
- W2051865460 hasConceptScore W2051865460C131779359 @default.
- W2051865460 hasConceptScore W2051865460C161790260 @default.
- W2051865460 hasConceptScore W2051865460C178790620 @default.
- W2051865460 hasConceptScore W2051865460C185592680 @default.
- W2051865460 hasConceptScore W2051865460C2776165026 @default.
- W2051865460 hasConceptScore W2051865460C2780643102 @default.
- W2051865460 hasConceptScore W2051865460C37263863 @default.
- W2051865460 hasConceptScore W2051865460C41183919 @default.
- W2051865460 hasConceptScore W2051865460C544778455 @default.
- W2051865460 hasConceptScore W2051865460C55493867 @default.
- W2051865460 hasConceptScore W2051865460C71240020 @default.
- W2051865460 hasConceptScore W2051865460C75473681 @default.
- W2051865460 hasIssue "34" @default.
- W2051865460 hasLocation W20518654601 @default.
- W2051865460 hasLocation W20518654602 @default.
- W2051865460 hasOpenAccess W2051865460 @default.
- W2051865460 hasPrimaryLocation W20518654601 @default.
- W2051865460 hasRelatedWork W1965625910 @default.
- W2051865460 hasRelatedWork W1990944400 @default.
- W2051865460 hasRelatedWork W2004025737 @default.
- W2051865460 hasRelatedWork W2013828974 @default.
- W2051865460 hasRelatedWork W2015170546 @default.
- W2051865460 hasRelatedWork W2016267837 @default.
- W2051865460 hasRelatedWork W2051291172 @default.
- W2051865460 hasRelatedWork W2059466750 @default.
- W2051865460 hasRelatedWork W217893489 @default.
- W2051865460 hasRelatedWork W2963179619 @default.
- W2051865460 hasVolume "44" @default.
- W2051865460 isParatext "false" @default.
- W2051865460 isRetracted "false" @default.
- W2051865460 magId "2051865460" @default.
- W2051865460 workType "article" @default.