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Literature summary extracted from

  • Vina-Gonzalez, J.; Jimenez-Lalana, D.; Sancho, F.; Serrano, A.; Martinez, A.; Guallar, V.; Alcalde, M.
    Structure-guided evolution of aryl alcohol oxidase from Pleurotus eryngii for the selective oxidation of secondary benzyl alcohols (2019), Adv. Synth. Catal., 361, 2514-2525 .
No PubMed abstract available

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.3.7 in fusion with chimeric prepro-leader (pre-alpha-factor-proKiller) that enhances secretion by introducing the F[3alpha]S, N[25proK]D, T[50proK]A and F[52proK]L mutations Pleurotus eryngii

Protein Variants

EC Number Protein Variants Comment Organism
1.1.3.7 A77W/R80C/H91N/L170M/V340A/I500M/F501W best performer with substrate (S)-1-(4-methoxyphenyl)-ethanol, with a total 800fold enhancement of activity relative to the parental type Pleurotus eryngii
1.1.3.7 H91N/L170M/I500L/F501I mutation H91N in an alpha-helix situated at the protein surface, and the consensus mutation H91N in the FAD attachment loop, to enhance stability and improve production by Saccharomyces cerevisiae to 4.5 mg/l and by Pichia pastoris in a bioreactor to 25.5 mg/l. I500L/F501I present a 15fold enhancement in activity with substrate (S)-1-(4-methoxyphenyl)-ethanol Pleurotus eryngii
1.1.3.7 H91N/L170M/I500M/F501V mutation H91N in an alpha-helix situated at the protein surface, and the consensus mutation H91N in the FAD attachment loop, to enhance stability and improve production by Saccharomyces cerevisiae to 4.5 mg/l and by Pichia pastoris in a bioreactor to 25.5 mg/l. I500M/F501V present a 30fold enhancement in activity with substrate (S)-1-(4-methoxyphenyl)-ethanol Pleurotus eryngii
1.1.3.7 H91N/L170M/I500M/F501W mutation H91N in an alpha-helix situated at the protein surface, and the consensus mutation H91N in the FAD attachment loop, to enhance stability and improve production by Saccharomyces cerevisiae to 4.5 mg/l and by Pichia pastoris in a bioreactor to 25.5 mg/l. I500M/F501W present a 160fold enhancement in activity with substrate (S)-1-(4-methoxyphenyl)-ethanol, while the specific activity on primary alcohols is dramatically reduced Pleurotus eryngii
1.1.3.7 H91N/L170M/I500Q/F501W mutation H91N in an alpha-helix situated at the protein surface, and the consensus mutation H91N in the FAD attachment loop, to enhance stability and improve production by Saccharomyces cerevisiae to 4.5 mg/l and by Pichia pastoris in a bioreactor to 25.5 mg/l. I500Q/F501W present a 5fold enhancement in activity with substrate (S)-1-(4-methoxyphenyl)-ethanol Pleurotus eryngii

Organism

EC Number Organism UniProt Comment Textmining
1.1.3.7 Pleurotus eryngii O94219
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-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.3.7 (S)-1-(4-fluorophenyl)ethanol + O2
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 Pleurotus eryngii 1-(4-fluorophenyl)acetaldehyde + H2O2
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 ?
1.1.3.7 (S)-1-(4-methoxyphenyl)-ethanol + O2
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 Pleurotus eryngii 1-(4-methoxyphenyl)acetaldehyde + H2O2
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.1.3.7 AAOx
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 Pleurotus eryngii