1e0y: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,615 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,615 edits
No edit summary
Line 1: Line 1:
[[Image:1e0y.jpg|left|200px]]
{{Seed}}
[[Image:1e0y.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1e0y|  PDB=1e0y  |  SCENE=  }}  
{{STRUCTURE_1e0y|  PDB=1e0y  |  SCENE=  }}  


'''STRUCTURE OF THE D170S/T457E DOUBLE MUTANT OF VANILLYL-ALCOHOL OXIDASE'''
===STRUCTURE OF THE D170S/T457E DOUBLE MUTANT OF VANILLYL-ALCOHOL OXIDASE===




==Overview==
<!--  
Vanillyl-alcohol oxidase (VAO) is the prototype of a newly recognized family of structurally related oxidoreductases sharing a conserved FAD-binding domain. The active site of VAO is formed by a cavity where the enzyme is able to catalyze many reactions with phenolic substrates. Among these reactions is the stereospecific hydroxylation of 4-ethylphenol-forming (R)-1-(4'-hydroxyphenyl)ethanol. During this conversion, Asp-170 is probably critical for the hydration of the initially formed p-quinone methide intermediate. By site-directed mutagenesis, the putative active site base has been relocated to the opposite face of the active site cavity. In this way, a change in stereospecificity has been achieved. Like native VAO, the single mutants T457E, D170A, and D170S preferentially converted 4-ethylphenol to the (R)-enantiomer of 1-(4'-hydroxyphenyl)ethanol. The double mutants D170A/T457E and D170S/T457E exhibited an inverted stereospecificity with 4-ethylphenol. Particularly, D170S/T457E was strongly (S)-selective, with an enantiomeric excess of 80%. The crystal structure of D170S/T457E, in complex with trifluoromethylphenol, showed a highly conserved mode of ligand binding and revealed that the distinctive catalytic properties of this mutant are not caused by major structural changes.
The line below this paragraph, {{ABSTRACT_PUBMED_10920192}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 10920192 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_10920192}}


==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Flavoenzyme]]
[[Category: Flavoenzyme]]
[[Category: Specificity]]
[[Category: Specificity]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 14:31:34 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:57:48 2008''

Revision as of 20:57, 30 June 2008

File:1e0y.png

Template:STRUCTURE 1e0y

STRUCTURE OF THE D170S/T457E DOUBLE MUTANT OF VANILLYL-ALCOHOL OXIDASE

Template:ABSTRACT PUBMED 10920192

About this Structure

1E0Y is a Single protein structure of sequence from Penicillium simplicissimum. Full crystallographic information is available from OCA.

Reference

Inversion of stereospecificity of vanillyl-alcohol oxidase., van Den Heuvel RH, Fraaije MW, Ferrer M, Mattevi A, van Berkel WJ, Proc Natl Acad Sci U S A. 2000 Aug 15;97(17):9455-60. PMID:10920192

Page seeded by OCA on Mon Jun 30 23:57:48 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1e0y&oldid=590112"