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http://archive.cmb.ac.lk:8080/xmlui/handle/70130/5220
Title: | Conifeiyl alcohol oxidase - a catechol oxidase? |
Authors: | Udagama-Randeniya, Preethi V. Savidge, Rodney A. |
Keywords: | Pinus strobus L Cell wall Polyphenol oxidase Tracheid differentiation lignin Wood formation |
Issue Date: | 1995 |
Publisher: | Springer |
Citation: | 37 |
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. |
URI: | http://archive.cmb.ac.lk:8080/xmlui/handle/70130/5220 |
Appears in Collections: | Department of Zoology |
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