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 Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | - |
Penicillium simplicissimum |
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 | 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 | UniProt | Comment | Textmining |
---|---|---|---|
Penicillium simplicissimum | P56216 | - |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
flavoprotein | covalent flavinylation of vanillyl-alcohol oxidase is an autocatalytic process | Penicillium simplicissimum |
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 | 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 | Comment | Organism |
---|---|---|
VAO | - |
Penicillium simplicissimum |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
flavinylation and oxidase assay at | Penicillium simplicissimum |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6.8 | - |
flavinylation assay at | Penicillium simplicissimum |
7.5 | - |
oxidase assay at | Penicillium simplicissimum |
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 |