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3cuk
From Proteopedia
(Difference between revisions)
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3cuk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cuk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3cuk RCSB], [http://www.ebi.ac.uk/pdbsum/3cuk PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3cuk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cuk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3cuk RCSB], [http://www.ebi.ac.uk/pdbsum/3cuk PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/OXDA_HUMAN OXDA_HUMAN]] Regulates the level of the neuromodulator D-serine in the brain. Has high activity towards D-DOPA and contributes to dopamine synthesis. Could act as a detoxifying agent which removes D-amino acids accumulated during aging. Acts on a variety of D-amino acids with a preference for those having small hydrophobic side chains followed by those bearing polar, aromatic, and basic groups. Does not act on acidic amino acids.<ref>PMID:17303072</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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[[Category: D-amino-acid oxidase]] | [[Category: D-amino-acid oxidase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: Munshi, S | + | [[Category: Munshi, S]] |
| - | [[Category: Prasad, S | + | [[Category: Prasad, S]] |
[[Category: Alpha-beta-alpha motif]] | [[Category: Alpha-beta-alpha motif]] | ||
[[Category: Fad]] | [[Category: Fad]] | ||
Revision as of 07:09, 25 December 2014
Crystal structure of human D-amino acid oxidase: bound to an inhibitor
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