1w1m
From Proteopedia
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Revision as of 14:17, 30 October 2007
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STRUCTURE OF THE OCTAMERIC FLAVOENZYME VANILLYL-ALCOHOL OXIDASE: GLU502GLY 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
1W1M is a [Single protein] structure of sequence from [Penicillium simplicissimum] with FAD and EUG as [ligands]. Active as [Alcohol oxidase], with EC number [1.1.3.13]. Structure known Active Site: AC1. 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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