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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.
    Structural analysis of flavinylation in vanillyl-alcohol oxidase (2000), J. Biol. Chem., 275, 38654-38658.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging-drop vapor diffusion method, apoenzyme, ADP-complex and holoenzyme. Crystal structure of both the holo and apo form of H61T are highly similar to the structure of the wild-type enzyme Penicillium simplicissimum

Protein Variants

Protein Variants Comment Organism
H61T in the mutant enzyme the covalent His-C8alpha-flavin linkage is not formed, while the enzyme is still able to bind FAD and perform catalysis. The mutant enzyme is about 10fold less active with 4-(methoxymethyl)phenol than the wild-type enzyme. Crystal structure of both the holo and apo form of H61T are highly similar to the structure of the wild-type enzyme Penicillium simplicissimum

Inhibitors

Inhibitors Comment Organism Structure
ADP competitive Penicillium simplicissimum
AMP
-
Penicillium simplicissimum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.04
-
4-(Methoxymethyl)phenol pH 7.5, 25°C, mutant enzyme H61T Penicillium simplicissimum

Organism

Organism UniProt Comment Textmining
Penicillium simplicissimum P56216
-
-

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
0.24
-
4-(Methoxymethyl)phenol pH 7.5, 25°C, mutant enzyme H61T Penicillium simplicissimum

Cofactor

Cofactor Comment Organism Structure
FAD covalently bound. Covalent flavinylation is an autocatalytical process in which His61 plays a crucial role by activating His422 Penicillium simplicissimum