1c0k: Difference between revisions

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[[Image:1c0k.jpg|left|200px]]
[[Image:1c0k.jpg|left|200px]]


{{Structure
<!--
|PDB= 1c0k |SIZE=350|CAPTION= <scene name='initialview01'>1c0k</scene>, resolution 1.46&Aring;
The line below this paragraph, containing "STRUCTURE_1c0k", creates the "Structure Box" on the page.
|SITE=
You may change the PDB parameter (which sets the PDB file loaded into the applet)
|LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=LAC:LACTIC+ACID'>LAC</scene>
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
|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>
or leave the SCENE parameter empty for the default display.
|GENE=  
-->
|DOMAIN=
{{STRUCTURE_1c0k| PDB=1c0k  | SCENE= }}  
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1c0k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c0k OCA], [http://www.ebi.ac.uk/pdbsum/1c0k PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1c0k RCSB]</span>
}}


'''CRYSTAL STRUCTURE ANALYSIS OF D-AMINO ACID OXIDASE IN COMPLEX WITH L-LACTATE'''
'''CRYSTAL STRUCTURE ANALYSIS OF D-AMINO ACID OXIDASE IN COMPLEX WITH L-LACTATE'''
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[[Category: Umhau, S.]]
[[Category: Umhau, S.]]
[[Category: Welte, W.]]
[[Category: Welte, W.]]
[[Category: alpha-beta-alpha motif]]
[[Category: Alpha-beta-alpha motif]]
[[Category: flavin containing protein]]
[[Category: Flavin containing protein]]
[[Category: oxidoreductase]]
[[Category: Oxidoreductase]]
 
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:12:05 2008''

Revision as of 12:11, 2 May 2008

File:1c0k.jpg

Template:STRUCTURE 1c0k

CRYSTAL STRUCTURE ANALYSIS OF D-AMINO ACID OXIDASE IN COMPLEX WITH L-LACTATE


OverviewOverview

Flavin is one of the most versatile redox cofactors in nature and is used by many enzymes to perform a multitude of chemical reactions. d-Amino acid oxidase (DAAO), a member of the flavoprotein oxidase family, is regarded as a key enzyme for the understanding of the mechanism underlying flavin catalysis. The very high-resolution structures of yeast DAAO complexed with d-alanine, d-trifluoroalanine, and l-lactate (1.20, 1.47, and 1.72 A) provide strong evidence for hydride transfer as the mechanism of dehydrogenation. This is inconsistent with the alternative carbanion mechanism originally favored for this type of enzymatic reaction. The step of hydride transfer can proceed without involvement of amino acid functional groups. These structures, together with results from site-directed mutagenesis, point to orbital orientation/steering as the major factor in catalysis. A diatomic species, proposed to be a peroxide, is found at the active center and on the Re-side of the flavin. These results are of general relevance for the mechanisms of flavoproteins and lead to the proposal of a common dehydrogenation mechanism for oxidases and dehydrogenases.

About this StructureAbout this Structure

1C0K is a Single protein structure of sequence from Rhodosporidium toruloides. Full crystallographic information is available from OCA.

ReferenceReference

The x-ray structure of D-amino acid oxidase at very high resolution identifies the chemical mechanism of flavin-dependent substrate dehydrogenation., Umhau S, Pollegioni L, Molla G, Diederichs K, Welte W, Pilone MS, Ghisla S, Proc Natl Acad Sci U S A. 2000 Nov 7;97(23):12463-8. PMID:11070076 Page seeded by OCA on Fri May 2 12:11:17 2008

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