1C0K

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

1C0K の概要

• エントリーDOI: 10.2210/pdb1c0k/pdb
• 分子名称: PROTEIN (D-AMINO ACID OXIDASE), FLAVIN-ADENINE DINUCLEOTIDE, LACTIC ACID, ... (4 entities in total)
• 機能のキーワード: flavin containing protein, alpha-beta-alpha motif, oxidoreductase
• 由来する生物種: Rhodosporidium toruloides
• 細胞内の位置: Peroxisome : P80324
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 40490.55

構造登録者

Umhau, S.,Molla, G.,Diederichs, K.,Pilone, M.S.,Ghisla, S.,Welte, W.,Pollegioni, L. (登録日: 1999-07-16, 公開日: 2000-11-22, 最終更新日: 2023-11-15)

主引用文献

Umhau, S.,Pollegioni, L.,Molla, G.,Diederichs, K.,Welte, W.,Pilone, M.S.,Ghisla, S.
The x-ray structure of D-amino acid oxidase at very high resolution identifies the chemical mechanism of flavin-dependent substrate dehydrogenation.
Proc.Natl.Acad.Sci.USA, 97:12463-12468, 2000

PubMed Abstract: 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.

PubMed: 11070076
DOI: 10.1073/pnas.97.23.12463

実験手法

X-RAY DIFFRACTION (1.46 Å)