1w1j

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(New page: 200px<br /> <applet load="1w1j" size="450" color="white" frame="true" align="right" spinBox="true" caption="1w1j, resolution 2.70&Aring;" /> '''STRUCTURE OF THE OC...)
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Revision as of 17:51, 29 October 2007

Image:1w1j.gif

1w1j, resolution 2.70Å

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STRUCTURE OF THE OCTAMERIC FLAVOENZYME VANILLYL-ALCOHOL OXIDASE: THE505SER MUTANT

Overview

The flavoenzyme vanillyl-alcohol oxidase was subjected to random, mutagenesis to generate mutants with enhanced reactivity to creosol, (2-methoxy-4-methylphenol). The vanillyl-alcohol oxidase-mediated, conversion of creosol proceeds via a two-step process in which the, initially formed vanillyl alcohol (4-hydroxy-3-methoxybenzyl alcohol) is, oxidized to the widely used flavor compound vanillin, (4-hydroxy-3-methoxybenzaldehyde). The first step of this reaction is, extremely slow due to the formation of a covalent FAD N-5-creosol adduct., After a single round of error-prone PCR, seven mutants were generated with, increased reactivity to creosol. The single-point mutants I238T, F454Y, E502G, and T505S showed an up to 40-fold increase in catalytic efficiency, (kcat/Km) with creosol compared ... [(full description)]

About this Structure

1W1J is a [Single protein] structure of sequence from [Penicillium simplicissimum] with FAD and EUG as [ligands]. Active as [[1]], with EC number [1.1.3.13]. Full crystallographic information is available from [OCA].

Reference

Laboratory-evolved vanillyl-alcohol oxidase produces natural vanillin., van den Heuvel RH, van den Berg WA, Rovida S, van Berkel WJ, J Biol Chem. 2004 Aug 6;279(32):33492-500. Epub 2004 May 28. PMID:15169773

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