Aryl-alcohol oxidase

Guillen F, AT Martinez, MJ Martinez (1992) Substrate specificity and properties of the aryl-alcohol oxidase from the ligninolytic fungus Pleurotus eryngii. Eur J Biochem 209 603-611. 

Muheim A, R Waldner, MSA Leisola, A Fiechter (1990) An extracellular aryl-alcohol oxidase from the vihite-rot ivmgm Bjerkandera adusta. Enzyme Microbiol Technol 12 204-209. 

Aryl alcohol oxidase from the ligninolytic fungus Pleurotus eryngii had a strong preference for benzylic and allylic alcohols, showing activity on phenyl-substituted benzyl, cinnamyl, naphthyl and 2,4-hexadien-l-ol [103,104]. Another aryl alcohol oxidase, vanillyl alcohol oxidase (VAO) from the ascomycete Penicillium simplicissimum catalyzed the oxidation of vanillyl alcohol and the demethylation of 4-(methoxymethyl)phenol to vanillin and 4-hydro-xybenzaldehyde. In addition, VAO also catalyzed deamination of vanillyl amine to vanillin, and hydroxylation and dehydrogenation of 4-alkylphenols. For the oxidation of 4-alkylphenol, the ratio between the alcohol and alkene product depended on the length and bulkiness of the alkyl side-chain [105,106]. 4-Ethylphenol and 4-propylphenol, were mainly converted to (R)-l-(4 -hydroxyphenyl) alcohols, whereas medium-chain 4-alkylphenols such as 4-butylphenol were converted to l-(4 -hydroxyphenyl)alkenes. 

Varela, E., Guillen, F., Martinez, A.T. and Martinez, M.J. (2001) Expression of Pleurotus eryngii aryl-alcohol oxidase in Aspergillus nidulans purification and characterization of the recombinant enzyme. Biochimica et Biophysica Acta, Protein Structure and Molecular, Enzymology, 1546 (1), 107-113. 

An aryl-alcohol oxidase produced optimally under carbon limitation from Bjerkandera adusta oxidized a number of benzyl alcohols including 4-methoxybenzyl alcohol, 3,4-dimethoxybenzyl alcohol (veratryl alcohol), and 4-hydroxy-3-methoxybenzyl alcohol, with the production of H202 from 02 monosaccharides were not oxidized (Muheim et al. 1990). An aryl-alcohol oxidase from Pleurotus eryngii is a flavoprotein with range of substrates comparable to that from B. adusta (Guillen et al. 1992). 

Gutierrez, A., Caramelo, L., Prieto, A., Martinez, M. J., Martinez, A. T. (1994). Anisaldehyde production and aryl-alcohol oxidase and dehydrogenase activities in hgninolytic fungi of the genus Pleurotus. Appl Environ Microbiol, 60,1783-1788. 

Muheim, A., Waldner, R., Leisola, M. S. A., Fiechter, A. (1990). An extracellular aryl-alcohol oxidase from the white-rot fungus Bjerkandera adusta. Enzyme Microb. Technol.,L, 204-209. 

Cytochrome P450 Alcohol dehydrogenase Aldehyde dehydrogenase Aldehyde oxidase Carboxylesterase Aiylesterase Acetylesterase Aryl 4-hydroxylase Aryl sulphatase... 

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