6A0D
The crystal structure of Mandelate oxidase mutant Y128F with (S)-2-phenylpropanoic acid
Summary for 6A0D
| Entry DOI | 10.2210/pdb6a0d/pdb |
| Descriptor | 4-hydroxymandelate oxidase, FLAVIN MONONUCLEOTIDE, (2~{S})-2-phenylpropanoic acid, ... (4 entities in total) |
| Functional Keywords | fmn-dependent oxidase, flavoprotein |
| Biological source | Amycolatopsis orientalis (Nocardia orientalis) |
| Total number of polymer chains | 1 |
| Total formula weight | 40786.25 |
| Authors | |
| Primary citation | 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 Cited by 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: 31373572DOI: 10.1107/S2059798319009574 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.65 Å) |
Structure validation
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