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Literature summary for 1.1.3.46 extracted from

  • Lyu, S.; Lin, K.; Yeh, H.; Li, Y.; Huang, C.; Wang, Y.; Shih, H.; Hsu, N.; Wu, C.; Li, T.
    The flavin mononucleotide cofactor in alpha-hydroxyacid oxidases exerts its electrophilic/nucleophilic duality in control of the substrate-oxidation level (2019), Acta Crystallogr. Sect. D, 75, 918-929 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Amycolatopsis orientalis

Crystallization (Commentary)

Crystallization (Comment) Organism
structures of wild-type and mutant Y128F with and without substrate. Cofactor FMNox possesses an electrophilic/nucleophilic duality. In the Y128F mutant the active-site perturbation ensemble facilitates the polarization of FMNox to a nucleophilic ylide, which is in a position to act on an alpha-ketoacid, forming an N5-acyl-FMNred dead-end adduct. In four-electron oxidation of mutant Y128F, an intramolecular disproportionation reaction via an N5-alkanol-FMNred C'alpha carbanion intermediate may account for the ThDP/PLP/NADPH-independent oxidative decarboxylation reaction Amycolatopsis orientalis

Protein Variants

Protein Variants Comment Organism
Y128F mutant is capable of oxidizing mandelate to benzoate via a four-electron oxidative decarboxylation reaction Amycolatopsis orientalis

Organism

Organism UniProt Comment Textmining
Amycolatopsis orientalis O52792
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(S)-mandelate + O2
-
Amycolatopsis orientalis 2-phenyl-2-oxoacetate + H2O2
-
?
2 (S)-mandelate + O2
-
Amycolatopsis orientalis 2 benzoate + 2 CO2
-
?

Cofactor

Cofactor Comment Organism Structure
FMN
-
Amycolatopsis orientalis