6a0m

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Mandelate oxidase mutant-Y128F with 2-Phenylacetic acid

Structural highlights

6a0m is a 1 chain structure with sequence from Amycolatopsis orientalis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.75Å
Ligands:FMN, PAC
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

HMO_AMYOR Catalyzes the oxidation of p-hydroxymandelate to p-hydroxybenzoylformate in the biosynthesis of L-(4-hydroxyphenyl)glycine and L-(3,5-dihydroxyphenyl)glycine, 2 non-proteinogenic amino acids occurring in the vancomycin group of antibiotics.[1] [2]

Publication Abstract from PubMed

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.

Biochemical and structural explorations of alpha-hydroxyacid oxidases reveal a four-electron oxidative decarboxylation reaction.,Yeh HW, Lin KH, Lyu SY, Li YS, Huang CM, Wang YL, Shih HW, Hsu NS, Wu CJ, Li TL Acta Crystallogr D Struct Biol. 2019 Aug 1;75(Pt 8):733-742. doi:, 10.1107/S2059798319009574. Epub 2019 Jul 30. PMID:31373572[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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Citations
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Flavin Mononucleotide-Dependent l-Lactate Dehydrogenases: Expanding the Toolbox of Enzymes for l-Lactate Biosensors.
Tsvik et al. (2022)
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1 other articles
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References

  1. ↑ Hubbard BK, Thomas MG, Walsh CT. Biosynthesis of L-p-hydroxyphenylglycine, a non-proteinogenic amino acid constituent of peptide antibiotics. Chem Biol. 2000 Dec;7(12):931-42. PMID:11137816
  2. ↑ Li TL, Choroba OW, Charles EH, Sandercock AM, Williams DH, Spencer JB. Characterisation of a hydroxymandelate oxidase involved in the biosynthesis of two unusual amino acids occurring in the vancomycin group of antibiotics. Chem Commun (Camb). 2001 Sep 21;(18):1752-3. PMID:12240298
  3. ↑ Yeh HW, Lin KH, Lyu SY, Li YS, Huang CM, Wang YL, Shih HW, Hsu NS, Wu CJ, Li TL. Biochemical and structural explorations of alpha-hydroxyacid oxidases reveal a four-electron oxidative decarboxylation reaction. Acta Crystallogr D Struct Biol. 2019 Aug 1;75(Pt 8):733-742. doi:, 10.1107/S2059798319009574. Epub 2019 Jul 30. PMID:31373572 doi:http://dx.doi.org/10.1107/S2059798319009574

Contents


PDB ID 6a0m

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