Coniferyl alcohol oxidase, anew enzyme of lignification

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dc.contributor.authorSavidge, R A
dc.contributor.authorUdagama-Randeniya, P V
dc.contributor.authorYijun, Xu
dc.contributor.authorLeinhos, V
dc.contributor.authorForster, H
dc.date.accessioned2021-06-11T05:08:31Z
dc.date.available2021-06-11T05:08:31Z
dc.date.issued1998
dc.descriptionSummary In conifers, CAO is an oxygen-dependent oxidase capable of oxidizing coniferyl alcohol into dilignols, and the activity of CAO is specifically associated with lignification. Whether CAO actually participates in lignification remains uncertain; however, the same difficulty attends the presumed roles of peroxidase and laccase in production of the lignin polymer. Stable genetic transformants having inactivated gene expression for CAO, peroxidase, or laccase need to be produced in order to clarify the role of each enzyme in lignification.en_US
dc.description.abstractConiferyl alcohol oxidase (CAO), a catechol oxidase (o-diphenol:oxygen oxidoreductase, E.C.1.10.3.1) specifically associated with lignification during wood formation in conifers, is described and its activity is compared with that of peroxidase. CAO activity is not affected by provision of H2O2, and although CAO is an O2-requiring enzyme able to oxidize substrates in common with laccase, CAO is distinct from laccase in catalytic rate, amino acid composition, response to effectors, copper content and type, protein size, and immunodetectability. Peroxidase activity, readily detected in phloem, cambium and xylem, was inversely correlated with lignification. In contrast, CAO activity was restricted to the lignifying zone. Peroxide and superoxide anion were found in the phloem and cambial zone, respectively, but a pool of H2O2 in support of lignification could not be detected in lignifying xylem or elsewhere. Additional evidence has indicated that coniferin hydrolysis may be the rate limiting step in the supply of coniferyl alcohol for oxidation by CAO.en_US
dc.description.sponsorshipThe research was supported primarily by the Natural Sciences and Engineering Research Council of Canada with supplementary funding from the Canadian Forestry Service. H.F. was supported by the Ministry of Science, Research and Culture of Thuringia, Germany.en_US
dc.identifier.isbn‍9780841235663
dc.identifier.other10.1021/bk-1998-0697
dc.identifier.urihttp://archive.cmb.ac.lk:8080/xmlui/handle/70130/5372
dc.language.isoenen_US
dc.publisher“Lingnin and Lignan Biosynthesis”, in ACS Symposium Series Volume 697, Lewis, N. G. and Sarkanen, S (eds), American Chemical Society, 109-130.en_US
dc.subjectConiferyl alcohol oxidaseen_US
dc.subjectenzymeen_US
dc.subjectlignificationen_US
dc.titleConiferyl alcohol oxidase, anew enzyme of lignificationen_US
dc.typeBook chapteren_US

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