6-S-Cysteinylation of Bi-covalently Attached FAD in Berberine Bridge Enzyme Tunes the Redox Potential for Optimal Activity
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Functional Roles of the 6-S-Cysteinyl, 8 -N1-Histidyl FAD in Glucooligosaccharide Oxidase from Acremonium strictumA concerted mechanism for berberine bridge enzymeThe Crystal Structure and Mechanism of an Unusual Oxidoreductase, GilR, Involved in Gilvocarcin V BiosynthesisCatalytic and Structural Role of a Conserved Active Site Histidine in Berberine Bridge EnzymeTirandamycin biosynthesis is mediated by co-dependent oxidative enzymesRationally engineered flavin-dependent oxidase reveals steric control of dioxygen reductionEngineering of pyranose dehydrogenase for increased oxygen reactivityOxidation of Monolignols by Members of the Berberine Bridge Enzyme Family Suggests a Role in Plant Cell Wall MetabolismStructure of a Berberine Bridge Enzyme-Like Enzyme with an Active Site Specific to the Plant Family BrassicaceaeMechanistic advances in plant natural product enzymes.The impact of structural biology on alkaloid biosynthesis research.Oxidative Cyclization in Natural Product BiosynthesisOpium poppy and Madagascar periwinkle: model non-model systems to investigate alkaloid biosynthesis in plants.Biocatalytic organic synthesis of optically pure (S)-scoulerine and berbine and benzylisoquinoline alkaloidsContribution of flavin covalent linkage with histidine 99 to the reaction catalyzed by choline oxidase.Isotope effects suggest a stepwise mechanism for berberine bridge enzyme.Inverting the regioselectivity of the berberine bridge enzyme by employing customized fluorine-containing substrates.Structural and mechanistic studies reveal the functional role of bicovalent flavinylation in berberine bridge enzymeIdentification of a gatekeeper residue that prevents dehydrogenases from acting as oxidases.Covalent flavinylation of vanillyl-alcohol oxidase is an autocatalytic process.Mathematically combined half-cell reduction potentials of low-molecular-weight thiols as markers of seed ageing.The single berberine bridge enzyme homolog of Physcomitrella patens is a cellobiose oxidase.Biocatalytic Oxidative CC Bond Formation Catalysed by the Berberine Bridge Enzyme: Optimal Reaction Conditions
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P2860
6-S-Cysteinylation of Bi-covalently Attached FAD in Berberine Bridge Enzyme Tunes the Redox Potential for Optimal Activity
description
article publié dans la revue scientifique Journal of Biological Chemistry
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im Juni 2007 veröffentlichter wissenschaftlicher Artikel
@de
scientific article published in Journal of Biological Chemistry
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wetenschappelijk artikel
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наукова стаття, опублікована в червні 2007
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name
6-S-Cysteinylation of Bi-coval ...... Potential for Optimal Activity
@en
6-S-Cysteinylation of Bi-coval ...... Potential for Optimal Activity
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type
label
6-S-Cysteinylation of Bi-coval ...... Potential for Optimal Activity
@en
6-S-Cysteinylation of Bi-coval ...... Potential for Optimal Activity
@nl
prefLabel
6-S-Cysteinylation of Bi-coval ...... Potential for Optimal Activity
@en
6-S-Cysteinylation of Bi-coval ...... Potential for Optimal Activity
@nl
P2860
P356
P1476
6-S-cysteinylation of bi-coval ...... potential for optimal activity
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P2093
Toni M Kutchan
P2860
P304
24437-24443
P356
10.1074/JBC.M703642200
P407
P577
2007-06-15T00:00:00Z