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1e8h

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(New page: 200px<br /> <applet load="1e8h" size="450" color="white" frame="true" align="right" spinBox="true" caption="1e8h, resolution 2.6&Aring;" /> '''STRUCTURE OF THE H61...)
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==About this Structure==
==About this Structure==
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1E8H 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 ADP as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.3.7 1.1.3.7]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1E8H OCA]].
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1E8H 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 ADP as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[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]]. Structure known Active Sites: AC1 and AC2. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1E8H OCA]].
==Reference==
==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10984479 10984479]
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10984479 10984479]
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[[Category: Aryl-alcohol oxidase]]
[[Category: Penicillium simplicissimum]]
[[Category: Penicillium simplicissimum]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: peroxisome]]
[[Category: peroxisome]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 17:28:05 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 11:10:53 2007''

Revision as of 09:06, 30 October 2007


1e8h, resolution 2.6Å

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

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, ... [(full description)]

About this Structure

1E8H is a [Single protein] structure of sequence from [Penicillium simplicissimum] with ADP as [ligand]. Active as [Aryl-alcohol oxidase], with EC number [1.1.3.7]. Structure known Active Sites: AC1 and AC2. 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

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