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Literature summary for 1.1.3.13 extracted from

  • Kim, Y.; Rykov, V.; Ashin, V.; Molochkov, N.; Skarga, Y.
    Thermodynamic behavior and conformational changes of alcohol oxidase from yeast Hansenula polymorpha (2011), Biophysics, 56, 1021-1025.
No PubMed abstract available

General Stability

General Stability Organism
ethanol stabilizes the protein structure and increased the melting temperature Ogataea angusta

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
600000
-
-
Ogataea angusta

Organic Solvent Stability

Organic Solvent Comment Organism
Ethanol ethanol stabilizes the protein structure and increased the melting temperature Ogataea angusta

Organism

Organism UniProt Comment Textmining
Ogataea angusta
-
-
-
Ogataea angusta NCYC 495
-
-
-

Subunits

Subunits Comment Organism
More the secondary structure of alcohol oxidase is not influenced by ethanol or sodium azide, but ethanol significantly modified the circular dichroism spectrum associated with the tertiary structure of alcohol oxidase Ogataea angusta

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Ogataea angusta

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Ogataea angusta

Cofactor

Cofactor Comment Organism Structure
FAD noncovalently bound to the adenine moiety to the N-terminal domain of the subunit in the active site of the enzyme Ogataea angusta
additional information the enzyme does not require exogenous cofactors Ogataea angusta