1e8f

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[[Image:1e8f.gif|left|200px]]
[[Image:1e8f.gif|left|200px]]
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{{Structure
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|PDB= 1e8f |SIZE=350|CAPTION= <scene name='initialview01'>1e8f</scene>, resolution 2.9&Aring;
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The line below this paragraph, containing "STRUCTURE_1e8f", creates the "Structure Box" on the page.
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|SITE=
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Aryl-alcohol_oxidase Aryl-alcohol oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.3.7 1.1.3.7] </span>
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{{STRUCTURE_1e8f| PDB=1e8f | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1e8f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e8f OCA], [http://www.ebi.ac.uk/pdbsum/1e8f PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1e8f RCSB]</span>
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'''STRUCTURE OF THE H61T MUTANT OF THE FLAVOENZYME VANILLYL-ALCOHOL OXIDASE IN THE APO FORM'''
'''STRUCTURE OF THE H61T MUTANT OF THE FLAVOENZYME VANILLYL-ALCOHOL OXIDASE IN THE APO FORM'''
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[[Category: Fraaije, M.]]
[[Category: Fraaije, M.]]
[[Category: Mattevi, A.]]
[[Category: Mattevi, A.]]
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[[Category: catalysis]]
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[[Category: Catalysis]]
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[[Category: flavoenzyme]]
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[[Category: Flavoenzyme]]
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[[Category: flavoprotein]]
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[[Category: Flavoprotein]]
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[[Category: methanol utilization]]
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[[Category: Methanol utilization]]
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[[Category: oxidase]]
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[[Category: Oxidase]]
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[[Category: oxidoreductase]]
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[[Category: Oxidoreductase]]
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[[Category: peroxisome]]
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[[Category: Peroxisome]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:47:37 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:57:21 2008''
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Revision as of 11:47, 2 May 2008

Image:1e8f.gif

Template:STRUCTURE 1e8f

STRUCTURE OF THE H61T MUTANT OF THE FLAVOENZYME VANILLYL-ALCOHOL OXIDASE IN THE APO FORM


Overview

Vanillyl-alcohol oxidase (VAO) is member of a newly recognized flavoprotein family of structurally related oxidoreductases. The enzyme contains a covalently linked FAD cofactor. To study the mechanism of flavinylation we have created a design point mutation (His-61 --> Thr). In the mutant enzyme the covalent His-C8alpha-flavin linkage is not formed, while the enzyme is still able to bind FAD and perform catalysis. The H61T mutant displays a similar affinity for FAD and ADP (K(d) = 1.8 and 2.1 microm, respectively) but does not interact with FMN. H61T is about 10-fold less active with 4-(methoxymethyl)phenol) (k(cat) = 0.24 s(-)(1), K(m) = 40 microm) than the wild-type enzyme. The crystal structures of both the holo and apo form of H61T are highly similar to the structure of wild-type VAO, indicating that binding of FAD to the apoprotein does not require major structural rearrangements. These results show that covalent flavinylation is an autocatalytical process in which His-61 plays a crucial role by activating His-422. Furthermore, our studies clearly demonstrate that in VAO, the FAD binds via a typical lock-and-key approach to a preorganized binding site.

About this Structure

1E8F is a Single protein structure of sequence from Penicillium simplicissimum. Full crystallographic information is available from OCA.

Reference

Structural analysis of flavinylation in vanillyl-alcohol oxidase., Fraaije MW, van Den Heuvel RH, van Berkel WJ, Mattevi A, J Biol Chem. 2000 Dec 8;275(49):38654-8. PMID:10984479 Page seeded by OCA on Fri May 2 14:47:37 2008

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