Biochemical and structural explorations of α-hydroxyacid oxidases reveal a four-electron oxidative decarboxylation reaction

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.

doi:10.1107/S2059798319009574

Acta Crystallographica Section D
Acta Crystallographica
Section D STRUCTURAL BIOLOGY

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Figure 1
Pathways and structures. (a) Anabolic pathway of L-p-hydroxyphenylglycine. (b) Metabolic pathway of (R)-mandelate; MdlB is also referred to as S-mandelate dehydrogenase (MDH). (c) Chemical structure of oxidized flavin mononucleotide (FMN_ox). (d) The direct conversion of mandelate to benzoate by the Y128F mutant via a four-electron oxidative decarboxylation reaction. The numbering system is shown in red for FMN and phenylpyruvate; the si-face and re-face prochirality relative to the N5 atom of the isoalloxazine ring is indicated in blue and green, respectively.

STRUCTURAL
BIOLOGY

ISSN: 2059-7983

Volume 75| Part 8| August 2019| Pages 733-742

https://doi.org/10.1107/S2059798319009574

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