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Literature summary 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

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

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.1.40 3,5-dihydroxytoluene noncompetitive Evernia prunastri

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.1.40 7.5
-
 Evernic acid
-
 Evernia prunastri

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.40 Evernia prunastri
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.1.40
-
 Evernia prunastri

Substrates and Products (Substrate)

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

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.1.1.40 25
-
 25 d, 50% loss of activity Evernia prunastri
3.1.1.40 100
-
 immobilized enzyme, 15 min, no loss of activity Evernia prunastri

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.1.40 6.5
-
 immobilized enzyme Evernia prunastri