2e48

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[[Image:2e48.gif|left|200px]]
[[Image:2e48.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 2e48 |SIZE=350|CAPTION= <scene name='initialview01'>2e48</scene>, resolution 2.90&Aring;
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The line below this paragraph, containing "STRUCTURE_2e48", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>
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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/D-amino-acid_oxidase D-amino-acid oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.3 1.4.3.3] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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|DOMAIN=
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{{STRUCTURE_2e48| PDB=2e48 | SCENE= }}
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|RELATEDENTRY=[[2du8|2DU8]], [[2e49|2E49]], [[2e4a|2E4A]], [[2e82|2E82]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2e48 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e48 OCA], [http://www.ebi.ac.uk/pdbsum/2e48 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2e48 RCSB]</span>
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}}
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'''Crystal Structure of Human D-Amino Acid Oxidase: Substrate-Free Holoenzyme'''
'''Crystal Structure of Human D-Amino Acid Oxidase: Substrate-Free Holoenzyme'''
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[[Category: Kawazoe, T.]]
[[Category: Kawazoe, T.]]
[[Category: Tsuge, H.]]
[[Category: Tsuge, H.]]
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[[Category: structurally ambivalent peptide]]
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[[Category: Structurally ambivalent peptide]]
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[[Category: substrate-free holoenzyme]]
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[[Category: Substrate-free holoenzyme]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 01:53:44 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:43:32 2008''
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Revision as of 22:53, 3 May 2008

Image:2e48.gif

Template:STRUCTURE 2e48

Crystal Structure of Human D-Amino Acid Oxidase: Substrate-Free Holoenzyme


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.

About this Structure

2E48 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structural basis of D-DOPA oxidation by D-amino acid oxidase: alternative pathway for dopamine biosynthesis., Kawazoe T, Tsuge H, Imagawa T, Aki K, Kuramitsu S, Fukui K, Biochem Biophys Res Commun. 2007 Apr 6;355(2):385-91. Epub 2007 Feb 8. PMID:17303072 Page seeded by OCA on Sun May 4 01:53:44 2008

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