1c0k
CRYSTAL STRUCTURE ANALYSIS OF D-AMINO ACID OXIDASE IN COMPLEX WITH L-LACTATE
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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 FAD and LAC 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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