6A0D

The crystal structure of Mandelate oxidase mutant Y128F with (S)-2-phenylpropanoic acid

6A0D の概要

• エントリーDOI: 10.2210/pdb6a0d/pdb
• 分子名称: 4-hydroxymandelate oxidase, FLAVIN MONONUCLEOTIDE, (2~{S})-2-phenylpropanoic acid, ... (4 entities in total)
• 機能のキーワード: fmn-dependent oxidase, flavoprotein
• 由来する生物種: Amycolatopsis orientalis (Nocardia orientalis)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 40786.25

構造登録者

Li, T.L.,Lin, K.H. (登録日: 2018-06-05, 公開日: 2019-06-19, 最終更新日: 2023-11-22)

主引用文献

Yeh, H.W.,Lin, K.H.,Lyu, S.Y.,Li, Y.S.,Huang, C.M.,Wang, Y.L.,Shih, H.W.,Hsu, N.S.,Wu, C.J.,Li, T.L.
Biochemical and structural explorations of alpha-hydroxyacid oxidases reveal a four-electron oxidative decarboxylation reaction.
Acta Crystallogr D Struct Biol, 75:733-742, 2019

PubMed Abstract: p-Hydroxymandelate oxidase (Hmo) is a flavin mononucleotide (FMN)-dependent enzyme that oxidizes mandelate to benzoylformate. How the FMN-dependent oxidation is executed by Hmo remains unclear at the molecular level. A continuum of snapshots from crystal structures of Hmo and its mutants in complex with physiological/nonphysiological substrates, products and inhibitors provides a rationale for its substrate enantioselectivity/promiscuity, its active-site geometry/reactivity and its direct hydride-transfer mechanism. A single mutant, Y128F, that extends the two-electron oxidation reaction to a four-electron oxidative decarboxylation reaction was unexpectedly observed. Biochemical and structural approaches, including biochemistry, kinetics, stable isotope labeling and X-ray crystallography, were exploited to reach these conclusions and provide additional insights.

PubMed: 31373572
DOI: 10.1107/S2059798319009574

実験手法

X-RAY DIFFRACTION (1.65 Å)