1w1j: Difference between revisions
New page: left|200px<br /> <applet load="1w1j" size="450" color="white" frame="true" align="right" spinBox="true" caption="1w1j, resolution 2.70Å" /> '''STRUCTURE OF THE OC... |
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==About this Structure== | ==About this Structure== | ||
1W1J is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Penicillium_simplicissimum Penicillium simplicissimum]] with FAD and EUG as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.3.13 1.1.3.13]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1W1J OCA]]. | 1W1J is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Penicillium_simplicissimum Penicillium simplicissimum]] with FAD and EUG as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Alcohol_oxidase Alcohol oxidase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.3.13 1.1.3.13]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1W1J OCA]]. | ||
==Reference== | ==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15169773 15169773] | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15169773 15169773] | ||
[[Category: Alcohol oxidase]] | |||
[[Category: Penicillium simplicissimum]] | [[Category: Penicillium simplicissimum]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 12:55:25 2007'' | ||
Revision as of 13:50, 30 October 2007
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STRUCTURE OF THE OCTAMERIC FLAVOENZYME VANILLYL-ALCOHOL OXIDASE: THE505SER MUTANT
OverviewOverview
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 StructureAbout this Structure
1W1J 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].
ReferenceReference
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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