1w1j: Difference between revisions

Revision as of 06:02, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1w1j.png

Template:STRUCTURE 1w1j

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

Template:ABSTRACT PUBMED 15169773

About this StructureAbout this Structure

1W1J is a Single protein structure of sequence from Penicillium simplicissimum. 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

Page seeded by OCA on Mon Jul 28 06:02:08 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1w1j.gif|left|200px]]
+{{Seed}}
+[[Image:1w1j.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1w1j|  PDB=1w1j  |  SCENE=  }}
-'''STRUCTURE OF THE OCTAMERIC FLAVOENZYME VANILLYL-ALCOHOL OXIDASE: THE505SER MUTANT'''
+===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 with the wild-type enzyme. This enhanced reactivity was due to a lower stability of the covalent flavin-substrate adduct, thereby promoting vanillin formation. The catalytic efficiencies of the mutants were also enhanced for other ortho-substituted 4-methylphenols, but not for p-cresol (4-methylphenol). The replaced amino acid residues are not located within a distance of direct interaction with the substrate, and the determined three-dimensional structures of the mutant enzymes are highly similar to that of the wild-type enzyme. These results clearly show the importance of remote residues, not readily predicted by rational design, for the substrate specificity of enzymes.
+The line below this paragraph, {{ABSTRACT_PUBMED_15169773}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15169773 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15169773}}
 ==About this Structure==
@@ Line 28: / Line 32: @@
 [[Category: Flavoenzyme]]
 [[Category: Oxidoreductase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 13:01:37 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 06:02:08 2008''