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Literature summary for 1.1.3.38 extracted from

  • Jin, J.; Mazon, H.; van den Heuvel, R.H.; Heck, A.J.; Janssen, D.B.; Fraaije, M.W.
    Covalent flavinylation of vanillyl-alcohol oxidase is an autocatalytic process (2008), FEBS J., 275, 5191-5200.
    View publication on PubMed
Search for more literature for 1.1.3.38

Cloned(Commentary)

Cloned (Comment) Organism
overexpression of apoVAO in Escherichia coli strain BSV11, which is defective in riboflavin synthesis. Incubation of apoVAO with FAD results in full restoration of enzyme activity dependent on FAD concentration, displaying a hyperbolic relationship, overview Penicillium simplicissimum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information
-
 Penicillium simplicissimum

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
62786
-
 1 x * 62786, apoVAO, mass spectrometry Penicillium simplicissimum
62790
-
 monomeric apoVAO, mass spectrometry Penicillium simplicissimum
125600
-
 dimeric apoVAO, mass spectrometry Penicillium simplicissimum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Penicillium simplicissimum covalent flavinylation of vanillyl-alcohol oxidase is an autocatalytic process ?
-
 ?
vanillyl alcohol + O2 Penicillium simplicissimum
-
 vanillin + H2O2
-
 ?

Organism

Organism UniProt Comment Textmining
Penicillium simplicissimum P56216
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
flavoprotein covalent flavinylation of vanillyl-alcohol oxidase is an autocatalytic process Penicillium simplicissimum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information covalent flavinylation of vanillyl-alcohol oxidase is an autocatalytic process Penicillium simplicissimum ?
-
 ?
vanillyl alcohol + O2
-
 Penicillium simplicissimum vanillin + H2O2
-
 ?

Subunits

Subunits Comment Organism
dimer 2 x 62786, apoVAO, mass spectrometry Penicillium simplicissimum
monomer 1 x * 62786, apoVAO, mass spectrometry Penicillium simplicissimum
More although apo VAO mainly exists as monomers and dimers, FAD binding promotes the formation of VAO dimers and octamers, the enzyme is dimeric to about 80% Penicillium simplicissimum
octamer FAD-VAO Penicillium simplicissimum

Synonyms

Synonyms Comment Organism
VAO
-
 Penicillium simplicissimum

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 flavinylation and oxidase assay at Penicillium simplicissimum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.8
-
 flavinylation assay at Penicillium simplicissimum
7.5
-
 oxidase assay at Penicillium simplicissimum

Cofactor

Cofactor Comment Organism Structure
FAD a 8alpha-histidyl-C6-cysteinyl bound FAD, vanillyl-alcohol oxidase contains a covalently alpha-histidyl bound FAD, which represents the most frequently encountered covalent flavin-protein linkage, autocatalytic incorporation mechanism, overview. Incubation of recombinant apoVAO with FAD results in full restoration of enzyme activity dependent on FAD concentration, displaying a hyperbolic relationship with KFAD = 0.0023 mM, kactivation = 0.13/min. Formation of the covalent flavin-protein bond is an autocatalytic process, which proceeds via a reduced flavin intermediate, overview Penicillium simplicissimum
additional information no activity with riboflavin, FMN, ADP, or AMP Penicillium simplicissimum