http://scholars.ntou.edu.tw/handle/123456789/22439
Title: | Biochemical and structural explorations of alpha-hydroxyacid oxidases reveal a four-electron oxidative decarboxylation reaction | Authors: | Yeh, Hsien-Wei Lin, Kuan-Hung Lyu, Syue-Yi Li, Yi-Shan Huang, Chun-Man Wang, Yung-Lin Shih, Hao-Wei Hsu, Ning-Shian Wu, Chang-Jer Li, Tsung-Lin |
Keywords: | mandelate oxidase;flavin mononucleotide;oxidative decarboxylation;hydride transfer;alpha-hydroxyacids | Issue Date: | 1-Aug-2019 | Publisher: | INT UNION CRYSTALLOGRAPHY | Journal Volume: | 75 | Start page/Pages: | 733-742 | Source: | ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 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. |
URI: | http://scholars.ntou.edu.tw/handle/123456789/22439 | ISSN: | 2059-7983 | DOI: | 10.1107/S2059798319009574 |
Appears in Collections: | 食品科學系 |
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