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Literature summary for 1.10.3.4 extracted from

  • Nair, P.M.; Vining, I.C.
    Isophenoxazine synthase apoenzyme from Pygnoporus coccineus (1965), Biochim. Biophys. Acta, 96, 318-327.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
apoenzyme Trametes coccinea

Inhibitors

Inhibitors Comment Organism Structure
ascorbic acid
-
Trametes coccinea
CuSO4
-
Trametes coccinea
cysteine
-
Trametes coccinea
FeSO4
-
Trametes coccinea
glutathione
-
Trametes coccinea
N-ethylmaleimide
-
Trametes coccinea
Na3AsO3
-
Trametes coccinea
NaBH4
-
Trametes coccinea
o-aminophenol substrate inhibition above 0.6 mM Trametes coccinea
p-chloromercuribenzoate
-
Trametes coccinea

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.264
-
FMN
-
Trametes coccinea

Metals/Ions

Metals/Ions Comment Organism Structure
Mn2+ holoenzyme reconstituted by addition of riboflavin and Mn2+ required for maximal activity, ineffective in absence of FMN Trametes coccinea

Organism

Organism UniProt Comment Textmining
Trametes coccinea
-
wood-rotting fungus
-

Purification (Commentary)

Purification (Comment) Organism
partial Trametes coccinea

Source Tissue

Source Tissue Comment Organism Textmining
mycelium
-
Trametes coccinea
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
Trametes coccinea

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 2-aminophenol + 2 O2 oxidation of o-aminophenol to o-quinoneimine and subsequent condensation of o-aminophenol to 2-amino-3H-isophenoxazin-3-one in absence of Mn2+ requires about 1 mol of riboflavin 5'-phosphate per mol of o-aminophenol oxidized, in presence of Mn2+ riboflavin 5'-phosphate acts as catalyst Trametes coccinea isophenoxazine + 2 H2O + H2O2
-
?

Cofactor

Cofactor Comment Organism Structure
additional information FAD no action as cofactor Trametes coccinea
riboflavin 5'-monophosphate holoenzyme reconstituted by addition of riboflavin 5'-phosphate and Mn2+ Trametes coccinea