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Literature summary for 1.11.2.1 extracted from

  • Kinne, M.; Zeisig, C.; Ullrich, R.; Kayser, G.; Hammel, K.E.; Hofrichter, M.
    Stepwise oxygenations of toluene and 4-nitrotoluene by a fungal peroxygenase (2010), Biochem. Biophys. Res. Commun., 397, 18-21.
    View publication on PubMed
Search for more literature for 1.11.2.1

Inhibitors

Inhibitors Comment Organism Structure
4-nitrotoluene the low extent of 4-nitrotoluene oxidation is attributable to inhibition of the enzyme by the substrate Cyclocybe aegerita

Organism

Organism UniProt Comment Textmining
Cyclocybe aegerita
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Cyclocybe aegerita

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
117
-
 using 3,4-dimethoxybenzyl alcohol as substrate, at 23°C, pH not specified in the publication Cyclocybe aegerita

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3,4-dimethoxybenzyl alcohol + H2O2
-
 Cyclocybe aegerita 3,4-dimethoxybenzaldehyde + H2O
-
 ?
4-nitrobenzaldehyde + H2O2
-
 Cyclocybe aegerita 4-nitrobenzoic acid + H2O
-
 ?
4-nitrobenzyl alcohol + H2O2
-
 Cyclocybe aegerita 4-nitrobenzaldehyde + H2O
-
 ?
4-nitrotoluene + H2O2 APO hydroxylates 4-nitrotoluene to 4-nitrobenzyl alcohol, then to 4-nitrobenzaldehyde and then to 4-nitrobenzoic acid. The reactions proceed stepwise with total conversions of 12% for 4-nitrotoluene Cyclocybe aegerita 4-nitrobenzyl alcohol + H2O
-
 ?
benzaldehyde + H2O2
-
 Cyclocybe aegerita benzoic acid + H2O
-
 ?
benzyl alcohol + H2O2
-
 Cyclocybe aegerita benzaldehyde + H2O
-
 ?
toluene + H2O2 the initial product of toluene oxidation is benzyl alcohol, which then declines with concomitant production of benzaldehyde, which in turn declines with concomitant production of benzoic acid. The reactions proceed stepwise with total conversions of 93% for toluene Cyclocybe aegerita benzyl alcohol + H2O
-
 ?

Synonyms

Synonyms Comment Organism
APO
-
 Cyclocybe aegerita
aromatic peroxygenase
-
 Cyclocybe aegerita

pI Value

Organism Comment pI Value Maximum pI Value
Cyclocybe aegerita isoform II, isoelectric focusing
-
 5.6

General Information

General Information Comment Organism
physiological function APO-catalyzed reactions resemble the benzylic hydroxylations catalyzed by P450s via their H2O2-dependent peroxide shunt mechanism Cyclocybe aegerita