Conifeiyl alcohol oxidase - a catechol oxidase?
| 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.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.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.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 |