EC Number   |
Substrates |
Organism |
Products |
Reversibility |
|---|
   1.14.13.82 | isovanillic acid + NAD(P)H + H+ + O2 |
O-demethylation by IvaAB |
Comamonas testosteroni |
protocatechuic acid + NAD(P)+ + H2O + formaldehyde |
- |
? |
| 1.14.13.82 | isovanillic acid + NAD(P)H + H+ + O2 |
i.e. 3-hydroxy-4-methoxybenzoate, O-demethylation by IvaAB |
Comamonas testosteroni |
protocatechuic acid + NAD(P)+ + H2O + formaldehyde |
procatechuic acid is 3,4-dihydroxybenzoate |
? |
| 1.14.13.82 | isovanillic acid + NAD(P)H + H+ + O2 |
O-demethylation by IvaAB |
Comamonas testosteroni BR6020 |
protocatechuic acid + NAD(P)+ + H2O + formaldehyde |
- |
? |
| 1.14.13.82 | isovanillic acid + NAD(P)H + H+ + O2 |
i.e. 3-hydroxy-4-methoxybenzoate, O-demethylation by IvaAB |
Comamonas testosteroni BR6020 |
protocatechuic acid + NAD(P)+ + H2O + formaldehyde |
procatechuic acid is 3,4-dihydroxybenzoate |
? |
| 1.14.13.82 | m-anisate + O2 + NADH + H+ |
- |
Acinetobacter sp. |
m-hydroxybenzoate + NAD+ + H2O + formaldehyde |
- |
? |
| 1.14.13.82 | m-anisate + O2 + NADH + H+ |
- |
Streptomyces sp. NL15-2K |
m-hydroxybenzoate + NAD+ + H2O + formaldehyde |
- |
? |
| 1.14.13.82 | m-anisate + O2 + NADH + H+ |
- |
Acinetobacter sp. ADP1 |
m-hydroxybenzoate + NAD+ + H2O + formaldehyde |
- |
? |
| 1.14.13.82 | more |
the enzyme forms a vanillate demethylase complex of VanA, a terminal oxygenase subunit, with VanB, a ferredoxin-like subunit, performing demethylation of vanillic acid and veratric acid |
Streptomyces sp. |
? |
- |
? |
| 1.14.13.82 | more |
substrate specificity for vanillate analogues by an in vivo assay using recombinant whole cells: among aromatic methyl ethers, vanillate, syringate, m-anisate, and veratrate are good substrates, whereas ferulate, vanillin, and guaiacol are not recognized by Streptomyces vanillate demethylase. Besides vanillate, 4-hydroxy-3-methylbenzoate is a better substrate than m-anisate and veratrate, and the 3-methyl group is efficiently oxidized to a hydroxymethyl group. The combination of a carboxyl group on the benzene ring and a hydroxyl group in the para-position relative to the carboxyl group may be preferable for substrate recognition by the enzyme. Demethylation by Streptomyces vanillate demethylase occurs only at the 3-position of veratrate and not at the 4-position |
Streptomyces sp. NL15-2K |
? |
- |
? |
| 1.14.13.82 | more |
to detect fungal demethylation and release of catechol-like structures, these are demonstrated using catechol, gallic acid and caffeic acid as standard model compounds to forms mono, bis- and/or tris-catechol-Fe3+ complexes. The catechol-Fe3+ complexes formation controlled by pH via the deprotonation of the catechol hydroxyls is investigated at pH 2.5, 8.0 and 10.0 and demonstrates that catechol formed mono, bis- and/or tris-catechol-Fe3+ complexes, and show maximum absorbance at 547 nm. Lignin demethylation (O-demethylase) and formation of dicatecholic structures is detected. The produced aromatic vicinal diol groups in lignin model compounds (LMCs) and KL are determined using different catecholic-binding reagents with the influence of H2O2, along with 4-antiaminopyrine reagent, and are analyzed by the following: 1. Fe3+-catechol complexation method, 2. HNO2 method, 3. FAS (ferric ammonium-sulfate) method, and 4. Ti(III)-NTA (titanium (III)-nitrilotriacetate) method for hydrolytic zone formation. Among the tested methods, Fe3+-catechol complexation shows lytic zone formation, mechanism, overview |
Aspergillus sp. |
? |
- |
- |
