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Literature summary extracted from

  • Jemel, I.; Fendri, A.; Gargouri, Y.; Bezzine, S.
    Kinetic properties of dromedary pancreatic lipase: A comparative study on emulsified and monomolecular substrate (2009), Colloids Surf. B Biointerfaces, 70, 238-242.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.1.3 5.5
-
 tributyrin at pH 8.5 and 37°C Camelus dromedarius
3.1.1.3 11
-
 trioctanoin at pH 8.5 and 37°C Camelus dromedarius

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.3 Camelus dromedarius
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.1.1.3 pancreas
-
 Camelus dromedarius
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.3 dicaprin + H2O hydrolyses more efficiently the 2,3-sn-dicaprin isomer than the 1,2-sn-dicaprin and the 1,3-sndicaprin monolayers Camelus dromedarius caprin + caprate
-
 ?
3.1.1.3 olive oil + H2O
-
 Camelus dromedarius ?
-
 ?
3.1.1.3 tributyrin + H2O
-
 Camelus dromedarius dibutyrin + butyrate
-
 ?
3.1.1.3 trioctanoin + H2O
-
 Camelus dromedarius dioctanoin + octanoate
-
 ?
3.1.1.3 triolein + H2O
-
 Camelus dromedarius diolein + oleate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.1.1.3 glycerol ester hydrolase
-
 Camelus dromedarius
3.1.1.3 lipase
-
 Camelus dromedarius

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.1.1.3 2416
-
 trioctanoin at pH 8.5 and 37°C Camelus dromedarius
3.1.1.3 4333
-
 tributyrin at pH 8.5 and 37°C Camelus dromedarius