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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
Search for more literature for 3.1.1.40

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