Por favor, use este identificador para citar o enlazar a este item:
http://hdl.handle.net/10261/73646
COMPARTIR / EXPORTAR:
SHARE CORE BASE | |
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE | |
Título: | New oxidase from Bjerkandera arthroconidial anamorph that oxidizes both phenolic and nonphenolic benzyl alcohols |
Autor: | Romero, Elvira CSIC; Ferreira, Patricia CSIC ORCID; Martínez, Ángel T. CSIC ORCID ; Martínez, María Jesús CSIC ORCID | Palabras clave: | Flavoenzyme; Benzyl alcohol; Hydroxybenzyl alcohol; Aromatic aldehyde; Aryl-alcohol oxidase; Vanillyl-alcohol oxidase | Fecha de publicación: | 6-dic-2009 | Editor: | Elsevier | Citación: | Biochimica et Biophysica Acta - Proteins and Proteomics 1794(4): 689-697(2009) | Resumen: | A new flavooxidase is described from a Bjerkandera arthroconidial anamorph. Its physicochemical characteristics, a monomeric enzyme containing non-covalently bound flavin adenine dinucleotide (FAD), and several catalytic properties, such as oxidation of aromatic and polyunsaturated aliphatic primary alcohols, are similar to those of Pleurotus eryngii aryl-alcohol oxidase (AAO). However, it also efficiently oxidizes phenolic benzyl and cinnamyl alcohols that are typical substrates of vanillyl-alcohol oxidase (VAO), a flavooxidase from a different family, characterized by its multimeric nature and presence of covalently-bound FAD. The enzyme also differs from P. eryngii AAO by having extremely high efficiency oxidizing chlorinated benzyl alcohols (1000-1500 s- 1 mM- 1), a feature related to the different alcohol metabolites secreted by the Pleurotus and Bjerkandera species including chloroaromatics, and higher activity on aromatic aldehydes. What is even more intriguing is the fact that, the new oxidase is optimally active at pH 6.0 on both p-anisyl and vanillyl alcohols, suggesting a mechanism for phenolic benzyl alcohol oxidation that is different from that described in VAO, which proceeds via the substrate phenolate anion formed at basic pH. Based on the above properties, and its ADP-binding motif, partially detected after N-terminus sequencing, the new enzyme is classified as a member of the GMC (glucose-methanol-choline oxidase) oxidoreductase family oxidizing both AAO and VAO substrates. | Descripción: | 9 pages, 5 figures.-- PMID: 19110079 [PubMed].-- Article in press | Versión del editor: | http://dx.doi.org/10.1016/j.bbapap.2008.11.013 | URI: | http://hdl.handle.net/10261/73646 | DOI: | 10.1016/j.bbapap.2008.11.013 | Identificadores: | doi: 10.1016/j.bbapap.2008.11.013 issn: 1570-9639 |
Aparece en las colecciones: | (CIB) Artículos |
Ficheros en este ítem:
Fichero | Descripción | Tamaño | Formato | |
---|---|---|---|---|
accesoRestringido.pdf | 15,38 kB | Adobe PDF | Visualizar/Abrir |
CORE Recommender
SCOPUSTM
Citations
33
checked on 28-mar-2024
WEB OF SCIENCETM
Citations
32
checked on 25-feb-2024
Page view(s)
338
checked on 18-abr-2024
Download(s)
113
checked on 18-abr-2024
Google ScholarTM
Check
Altmetric
Altmetric
NOTA: Los ítems de Digital.CSIC están protegidos por copyright, con todos los derechos reservados, a menos que se indique lo contrario.