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Literature summary for 1.1.3.38 extracted from

  • Fraaije, M.W.; van den Heuvel, R.H.; van Berkel, W.J.; Mattevi, A.
    Covalent flavinylation is essential for efficient redox catalysis in vanillyl-alcohol oxidase (1999), J. Biol. Chem., 274, 35514-35520.
    View publication on PubMed
Search for more literature for 1.1.3.38

Crystallization (Commentary)

Crystallization (Comment) Organism
-
 Penicillium simplicissimum

Protein Variants

Protein Variants Comment Organism
H422A mutant enzyme retains activity, turnover rates decrease by 1 order of magnitude. Mutant enzyme is still able to form a stable binary complex of reduced enzyme and a quinone methide product intermediate, a crucial step during vanillyl-alcohol oxidase-mediated catalysis. Although mutation prevents covalent linkage of FAD, mutant enzyme contains tightly bound FAD Penicillium simplicissimum
H422C mutant enzyme retains activity, turnover rates decrease by 1 order of magnitude. Although mutation prevents covalent linkage of FAD, mutant enzyme contains tightly bound FAD Penicillium simplicissimum
H422T mutant enzyme retains activity, turnover rates decrease by 1 order of magnitude. Although mutation prevents covalent linkage of FAD, mutant enzyme contains tightly bound FAD Penicillium simplicissimum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.034
-
 4-(Methoxymethyl)phenol pH 7.5, 25°C, mutant enzyme H422A Penicillium simplicissimum
0.037
-
 4-(Methoxymethyl)phenol pH 7.5, 25°C, mutant enzyme H422C Penicillium simplicissimum
0.041
-
 4-(Methoxymethyl)phenol pH 7.5, 25°C, mutant enzyme H422T Penicillium simplicissimum

Organism

Organism UniProt Comment Textmining
Penicillium simplicissimum P56216
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Penicillium simplicissimum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-(methoxymethyl)phenol + O2
-
 Penicillium simplicissimum ?
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.27
-
 4-(Methoxymethyl)phenol pH 7.5, 25°C, mutant enzyme H422A Penicillium simplicissimum
0.28
-
 4-(Methoxymethyl)phenol pH 7.5, 25°C, mutant enzyme H422T Penicillium simplicissimum
0.32
-
 4-(Methoxymethyl)phenol pH 7.5, 25°C, mutant enzyme H422C Penicillium simplicissimum

Cofactor

Cofactor Comment Organism Structure
FAD although mutations H422A, H422T or H422C, prevents covalent linkage of FAD, mutant enzymes contains tightly bound FAD. Covalent histidyl-FAD bond is not essential for FAD binding Penicillium simplicissimum