1c0k: Difference between revisions
New page: left|200px<br /><applet load="1c0k" size="450" color="white" frame="true" align="right" spinBox="true" caption="1c0k, resolution 1.46Å" /> '''CRYSTAL STRUCTURE AN... |
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[[Image:1c0k.jpg|left|200px]]<br /><applet load="1c0k" size=" | [[Image:1c0k.jpg|left|200px]]<br /><applet load="1c0k" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1c0k, resolution 1.46Å" /> | caption="1c0k, resolution 1.46Å" /> | ||
'''CRYSTAL STRUCTURE ANALYSIS OF D-AMINO ACID OXIDASE IN COMPLEX WITH L-LACTATE'''<br /> | '''CRYSTAL STRUCTURE ANALYSIS OF D-AMINO ACID OXIDASE IN COMPLEX WITH L-LACTATE'''<br /> | ||
==Overview== | ==Overview== | ||
Flavin is one of the most versatile redox cofactors in nature and is used | 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 Structure== | ==About this Structure== | ||
1C0K is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rhodosporidium_toruloides Rhodosporidium toruloides] with FAD and LAC as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http:// | 1C0K is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rhodosporidium_toruloides Rhodosporidium toruloides] with <scene name='pdbligand=FAD:'>FAD</scene> and <scene name='pdbligand=LAC:'>LAC</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C0K OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Ghisla, S.]] | [[Category: Ghisla, S.]] | ||
[[Category: Molla, G.]] | [[Category: Molla, G.]] | ||
[[Category: Pilone, M | [[Category: Pilone, M S.]] | ||
[[Category: Pollegioni, L.]] | [[Category: Pollegioni, L.]] | ||
[[Category: Umhau, S.]] | [[Category: Umhau, S.]] | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:01:11 2008'' | ||
Revision as of 13:01, 21 February 2008
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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 with and as ligands. Active as D-amino-acid oxidase, with EC number 1.4.3.3 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
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