Conifeiyl alcohol oxidase - a catechol oxidase?

Udagama-Randeniya, Preethi V.; Savidge, Rodney A.

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dc.contributor.author	Udagama-Randeniya, Preethi V.
dc.contributor.author	Savidge, Rodney A.
dc.date.accessioned	2021-05-23T12:39:52Z
dc.date.available	2021-05-23T12:39:52Z
dc.date.issued	1995
dc.identifier.citation	37	en_US
dc.identifier.other	https://doi.org/10.1007/BF00192190
dc.identifier.uri	http://archive.cmb.ac.lk:8080/xmlui/handle/70130/5220
dc.description.abstract	The physico-chemical properties of coniferyl alcohol oxidase (CAO), a copper containing glycoprotein spatiotemporally associated with lignification in conifers, is reported here. By electron paramagnetic resonance spectroscopy, only type 3 copper was indicated in CAO. CAO oxidizes several laccase substrates; however, it is not a blue-copper protein and monoclonal antibodies against both native and deglycosylated CAO did not recognize any of several laccases. The N-terminal sequence of CAO, H2N-X E L A Y S P P Y X P S, was non-homologous with known enzymes. Transparent copper, tetrameric structure, aminoacid composition, phenylhydrazine and tropolone inhibition, and SDS enhancement of CAO activity indicate that CAO is an o-diphenol oxidase.	en_US
dc.description.sponsorship	This research was supported by Forestry Canada and the Natural Sciences and Engineering Research Council of Canada.	en_US
dc.language.iso	en	en_US
dc.publisher	Springer	en_US
dc.subject	Pinus strobus L	en_US
dc.subject	Cell wall	en_US
dc.subject	Polyphenol oxidase	en_US
dc.subject	Tracheid differentiation	en_US
dc.subject	lignin	en_US
dc.subject	Wood formation	en_US
dc.title	Conifeiyl alcohol oxidase - a catechol oxidase?	en_US
dc.type	Article	en_US