1KIF

D-AMINO ACID OXIDASE FROM PIG KIDNEY

1KIF の概要

• エントリーDOI: 10.2210/pdb1kif/pdb
• 分子名称: D-AMINO ACID OXIDASE, FLAVIN-ADENINE DINUCLEOTIDE, BENZOIC ACID, ... (4 entities in total)
• 機能のキーワード: fad cofactor, oxidase, flavoenzyme, flavoprotein
• 由来する生物種: Sus scrofa (pig)
• 細胞内の位置: Peroxisome: P00371
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 322283.86

構造登録者

Todone, F.,Mattevi, A. (登録日: 1996-01-19, 公開日: 1996-07-11, 最終更新日: 2024-02-14)

主引用文献

Mattevi, A.,Vanoni, M.A.,Todone, F.,Rizzi, M.,Teplyakov, A.,Coda, A.,Bolognesi, M.,Curti, B.
Crystal structure of D-amino acid oxidase: a case of active site mirror-image convergent evolution with flavocytochrome b2.
Proc.Natl.Acad.Sci.USA, 93:7496-7501, 1996

PubMed Abstract: D-amino acid oxidase is the prototype of the FAD-dependent oxidases. It catalyses the oxidation of D-amino acids to the corresponding alpha-ketoacids. The reducing equivalents are transferred to molecular oxygen with production of hydrogen peroxide. We have solved the crystal structure of the complex of D-amino acid oxidase with benzoate, a competitive inhibitor of the substrate, by single isomorphous replacement and eightfold averaging. Each monomer is formed by two domains with an overall topology similar to that of p-hydroxybenzoate hydroxylase. The benzoate molecule lays parallel to the flavin ring and is held in position by a salt bridge with Arg-283. Analysis of the active site shows that no side chains are properly positioned to act as the postulated base required for the catalytic carboanion mechanism. On the contrary, the benzoate binding mode suggests a direct transfer of the substrate alpha-hydrogen to the flavin during the enzyme reductive half-reaction. The active site Of D-amino acid oxidase exhibits a striking similarity with that of flavocytochrome b2, a structurally unrelated FMN-dependent flavoenzyme. The active site groups (if these two enzymes are in fact superimposable once the mirror-image of the flavocytochrome b2 active site is generated with respect to the flavin plane. Therefore, the catalytic sites of D-amino acid oxidase and flavocytochrome b2 appear to have converged to a highly similar but enantiomeric architecture in order to catalvze similar reactions (oxidation of alpha-amino acids or alpha-hydroxy acids), although with opposite stereochemistry.

PubMed: 8755502
DOI: 10.1073/pnas.93.15.7496

実験手法

X-RAY DIFFRACTION (2.6 Å)