Enantioselective hydroxylation of 4-alkylphenols by vanillyl alcohol oxidase
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چکیده
منابع مشابه
Regio- and stereospecific conversion of 4-alkylphenols by the covalent flavoprotein vanillyl-alcohol oxidase.
The regio- and stereospecific conversion of prochiral 4-alkylphenols by the covalent flavoprotein vanillyl-alcohol oxidase was investigated. The enzyme was active, with 4-alkylphenols bearing aliphatic side chains of up to seven carbon atoms. Optimal catalytic efficiency occurred with 4-ethylphenol and 4-n-propylphenols. These short-chain 4-alkylphenols are stereoselectively hydroxylated to the...
متن کاملDirection of the reactivity of vanillyl-alcohol oxidase with 4-alkylphenols.
The covalent flavoprotein vanillyl-alcohol oxidase (VAO) predominantly converts short-chain 4-alkylphenols, like 4-ethylphenol, to (R)-1-(4'-hydroxyphenyl)alcohols and medium-chain 4-alkylphenols, like 4-butylphenol, to 1-(4'-hydroxyphenyl)alkenes. Crystallographic studies have indicated that the active site residue Asp170 is involved in determining the efficiency of substrate hydroxylation. To...
متن کاملInversion of stereospecificity of vanillyl-alcohol oxidase.
Vanillyl-alcohol oxidase (VAO) is the prototype of a newly recognized family of structurally related oxidoreductases sharing a conserved FAD-binding domain. The active site of VAO is formed by a cavity where the enzyme is able to catalyze many reactions with phenolic substrates. Among these reactions is the stereospecific hydroxylation of 4-ethylphenol-forming (R)-1-(4'-hydroxyphenyl)ethanol. D...
متن کاملStructure, function and redesign of vanillyl-alcohol oxidase
Vanillyl-alcohol oxidase (VAO) from Penicillium simplicissimum is an inducible flavoprotein involved in the biodegradation of lignin-derived aromatic compounds. The enzyme is the prototype of a newly recognized family of structurally related oxidoreductases, whose members share a conserved FAD-binding domain. The flavin cofactor in VAO is covalently linked to His422 of the cap domain. This cova...
متن کاملSubcellular localization of vanillyl-alcohol oxidase in Penicillium simplicissimum.
Growth of Penicillium simplicissimum on anisyl alcohol, veratryl alcohol or 4-(methoxymethyl)phenol, is associated with the synthesis of relatively large amounts of the hydrogen peroxide producing flavoprotein vanillyl-alcohol oxidase (VAO). Immunocytochemistry revealed that the enzyme has a dual location namely in peroxisomes and in the cytosol. The C-terminus of the primary structure of VAO d...
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ژورنال
عنوان ژورنال: Biotechnology and Bioengineering
سال: 1998
ISSN: 0006-3592,1097-0290
DOI: 10.1002/(sici)1097-0290(19980720)59:2<171::aid-bit5>3.0.co;2-e