Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.1.1.40 extracted from

  • Garcia-Junceda, E.; Cambon, C.; Vicente, C.
    Kinetics and stability of an immobilized orsellinate depside hydrolase in polyacrylamide gel (1991), Enzyme Microb. Technol., 13, 275-279.
No PubMed abstract available

Application

Application Comment Organism
synthesis depsides and their constitutive untis are used in the perfume industry Evernia prunastri

Inhibitors

Inhibitors Comment Organism Structure
3,5-dihydroxytoluene noncompetitive Evernia prunastri

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
7.5
-
Evernic acid
-
Evernia prunastri

Organism

Organism UniProt Comment Textmining
Evernia prunastri
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Evernia prunastri

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
evernic acid + H2O
-
Evernia prunastri orsellinic acid + everninic acid
-
r
lecanoric acid + H2O i.e. orsellinate depside Evernia prunastri orsellinic acid
-
?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
25
-
25 d, 50% loss of activity Evernia prunastri
100
-
immobilized enzyme, 15 min, no loss of activity Evernia prunastri

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5
-
immobilized enzyme Evernia prunastri