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Titolo:
Exploring the biocatalytic potential of vanillyl-alcohol oxidase by site-directed mutagenesis
Autore:
van den Heuvel, RHH; Laane, C; van Berkel, WJH;
Indirizzi:
Univ Wageningen & Res Ctr, Dept Agrotechnol & Food Sci, Biochem Lab, NL-6703 HA Wageningen, Netherlands Univ Wageningen & Res Ctr Wageningen Netherlands NL-6703 HA Netherlands
Titolo Testata:
ADVANCED SYNTHESIS & CATALYSIS
fascicolo: 6-7, volume: 343, anno: 2001,
pagine: 515 - 520
SICI:
1615-4150(200108)343:6-7<515:ETBPOV>2.0.ZU;2-B
Fonte:
ISI
Lingua:
ENG
Soggetto:
ENZYME-SUBSTRATE COMPLEX; PENICILLIUM-SIMPLICISSIMUM; CRESOL METHYLHYDROXYLASE; CATALYTIC MECHANISM; CRYSTAL-STRUCTURES; NMDA RECEPTORS; RAT-LIVER; 4-ALKYLPHENOLS; CAPSAICIN; BINDING;
Keywords:
enzyme catalysis; flavoprotein; site-directed mutagenesis; stereoselectivity; vanillyl-alcohol oxidase;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Physical, Chemical & Earth Sciences
Citazioni:
39
Recensione:
Indirizzi per estratti:
Indirizzo: van Berkel, WJH Univ Wageningen & Res Ctr, Dept Agrotechnol & Food Sci, Biochem Lab, Dreijenlaan 3, NL-6703 HA Wageningen, Netherlands Univ Wageningen & Res Ctr Dreijenlaan 3 Wageningen Netherlands NL-6703 HA
Citazione:
R.H.H. van den Heuvel et al., "Exploring the biocatalytic potential of vanillyl-alcohol oxidase by site-directed mutagenesis", ADV SYNTH C, 343(6-7), 2001, pp. 515-520

Abstract

Vanillyl-alcohol oxidase (VAO) is a flavoprotein containing a covalently bound FAD cofactor. The enzyme acts on a wide variety of 4-alkylphenols bearing aliphatic side-chains up to seven carbon atoms in length. Short-chain 4-alkylphenols are predominantly hydroxylated to (R)-1-(4'-hydroxyphenyl) alcohols, whereas medium-chain 4-alkylphenols are dehydrogenated to the corresponding I(4'-hydroxyphenyl)alkenes. In this account, we summarize our workon the structure, mechanism, and biocatalytic potential of VAO. It is shown that the efficiency of hydroxylation of 4-alkylphenols is dependent on the type or amino acid residue engineered at position 170. Furthermore, it isdemonstrated that the stereospecificity of the hydroxylation reaction can be inverted by relocating the active site base to the opposite face or the substrate-binding pocket.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 31/03/20 alle ore 05:12:28