2e4a: Difference between revisions

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[[Image:2e4a.~~gif~~|left|200px]]

[[Image:2e4a.png|left|200px]]

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~~'''~~Crystal Structure of Human D-Amino Acid Oxidase in complex with o-aminobenzoate~~'''~~

===Crystal Structure of Human D-Amino Acid Oxidase in complex with o-aminobenzoate===

~~==Overview==~~

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D-~~amino acid oxidase (DAO) degrades the gliotransmitter D~~-~~serine~~, ~~a potent endogenous ligand of N-methyl-D-aspartate type glutamate receptors. It also has been suggested that D-DOPA~~, the ~~stereoisomer of L-DOPA, is oxidized by DAO and then converted~~ to ~~dopamine via an alternative biosynthetic pathway~~. ~~Here, we provide direct crystallographic evidence that D-DOPA is readily fitted into the active site of human DAO~~, where it is ~~oxidized by~~ the ~~enzyme~~. ~~Moreover, our kinetic data show that the maximal velocity for oxidation of D~~-~~DOPA is much greater than for D~~-serine, which strongly supports the proposed alternative pathway for dopamine biosynthesis in the treatment of Parkinson's disease. In addition, determination of the structures of human DAO in various states revealed that the conformation of the hydrophobic VAAGL stretch (residues 47-51) to be uniquely stable in the human enzyme, which provides a structural basis for the unique kinetic features of human DAO.

The line below this paragraph, {{ABSTRACT_PUBMED_17303072}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 17303072 is the PubMed ID number.

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==About this Structure==

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[[Category: O-aminobenzoate complex]]

[[Category: Structurally ambivalent peptide]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sun May 4 01~~:53:47 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 06:03:18 2008''

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-[[Image:2e4a.gif|left|200px]]
+{{Seed}}
+[[Image:2e4a.png|left|200px]]
 <!--
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 {{STRUCTURE_2e4a|  PDB=2e4a  |  SCENE=  }}
-'''Crystal Structure of Human D-Amino Acid Oxidase in complex with o-aminobenzoate'''
+===Crystal Structure of Human D-Amino Acid Oxidase in complex with o-aminobenzoate===
-==Overview==
+<!--
-D-amino acid oxidase (DAO) degrades the gliotransmitter D-serine, a potent endogenous ligand of N-methyl-D-aspartate type glutamate receptors. It also has been suggested that D-DOPA, the stereoisomer of L-DOPA, is oxidized by DAO and then converted to dopamine via an alternative biosynthetic pathway. Here, we provide direct crystallographic evidence that D-DOPA is readily fitted into the active site of human DAO, where it is oxidized by the enzyme. Moreover, our kinetic data show that the maximal velocity for oxidation of D-DOPA is much greater than for D-serine, which strongly supports the proposed alternative pathway for dopamine biosynthesis in the treatment of Parkinson's disease. In addition, determination of the structures of human DAO in various states revealed that the conformation of the hydrophobic VAAGL stretch (residues 47-51) to be uniquely stable in the human enzyme, which provides a structural basis for the unique kinetic features of human DAO.
+The line below this paragraph, {{ABSTRACT_PUBMED_17303072}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17303072 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_17303072}}
 ==About this Structure==
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 [[Category: O-aminobenzoate complex]]
 [[Category: Structurally ambivalent peptide]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 01:53:47 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 06:03:18 2008''