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Literature summary extracted from

  • Pilarek, M.; Szewczyk, K.W.
    Kinetic model of 1,3-specific triacylglycerols alcoholysis catalyzed by lipases (2007), J. Biotechnol., 127, 736-744.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.1.3 additional information competitive substrate inhibition Moesziomyces antarcticus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.1.3 additional information
-
 additional information kinetic model of 1,3-specific triacylglycerols alcoholysis, overview Moesziomyces antarcticus

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.3 Moesziomyces antarcticus
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
3.1.1.3 triacylglycerol + H2O = diacylglycerol + a carboxylate mechanism of 1,3-specific alcoholysis, ping pong bi bi reaction mechanism Moesziomyces antarcticus
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.1.1.3 commercial preparation
-
 Moesziomyces antarcticus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.3 additional information the enzyme performs a reversible monoglyceride isomerization, the rate of iso-propanolysis reactions is higher than propanolysis, mechanism of 1,3-specific alcoholysis, overview Moesziomyces antarcticus ?
-
 ?
3.1.1.3 triacetin + H2O
-
 Moesziomyces antarcticus diacetin + acetate
-
 ir
3.1.1.3 tricaprylin + H2O preferred substrate Moesziomyces antarcticus dicaprylin + caprylate
-
 ir

Synonyms

EC Number Synonyms Comment Organism
3.1.1.3 lipase B
-
 Moesziomyces antarcticus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.1.3 50
-
 assay at Moesziomyces antarcticus