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Literature summary for 3.1.1.1 extracted from

  • Park, K.M.; Lee, J.H.; Hong, S.C.; Kwon, C.W.; Jo, M.; Choi, S.J.; Kim, K.; Chang, P.S.
    Selective production of 1-monocaprin by porcine liver carboxylesterase-catalyzed esterification Its enzyme kinetics and catalytic performance (2016), Enzyme Microb. Technol., 82, 51-57 .
    View publication on PubMed
Search for more literature for 3.1.1.1

Inhibitors

Inhibitors Comment Organism Structure
cetyltrimethylammonium bromide complete inhibition Sus scrofa
dimyristoylphosphatidylcholine 88% inhibition Sus scrofa
dipalmitoylphosphatidylcholine 91.5% inhibition Sus scrofa
additional information no inhibition by sodium sulfosuccinate Sus scrofa
PEG 6000 complete inhibition Sus scrofa
Triton X-100 93.6% inhibition Sus scrofa

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information enzyme kinetics, overview. Michaelis-Menten equation can be calculated from Hanes-Woolf equation Sus scrofa
16.44
-
 capric acid pH 7.0, 60°C Sus scrofa

Organic Solvent Stability

Organic Solvent Comment Organism
Acetone pH 7.0, 60°C, 2 h, loss of 82% activity Sus scrofa
benzene pH 7.0, 60°C, 2 h, loss of 91.6% activity Sus scrofa
cyclohexane pH 7.0, 60°C, 2 h, loss of 98.7% activity Sus scrofa
heptane pH 7.0, 60°C, 2 h, complete loss of activity Sus scrofa
isooctane pH 7.0, 60°C, 2 h, completely stable Sus scrofa
n-hexane pH 7.0, 60°C, 2 h, complete loss of activity Sus scrofa

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
commercial preparation
-
 Sus scrofa
-
liver
-
 Sus scrofa
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
capric acid + glycerol PLE-catalyzed esterification of capric acid with glycerol in reverse micelles. The most suitable structure of reverse micelles is comprised of isooctane (reaction medium) and bis(2-ethylhexyl) sodium sulfosuccinate ( anionic surfactant) with 0.1 of R-value ([water]/[surfactant]) and 3.0 of G/F-value ([glycerol]/[fatty acid]) for the PLE-catalyzed esterification. PLE mainly produces 1-monocaprin without any other products (di- and/or tricaprins of subsequent reactions). The degree of esterification at equilibrium state (after 4 h from the initiation) is 62.7% under optimum conditions. Method optimization, overview Sus scrofa 1-monocaprin + H2O
-
 ?

Synonyms

Synonyms Comment Organism
PLE
-
 Sus scrofa
porcine liver carboxylesterase
-
 Sus scrofa

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
60
-
-
 Sus scrofa

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
-
 Sus scrofa

General Information

General Information Comment Organism
evolution porcine liver carboxylesterase (PLE), with the consensus sequence motif Gly-Glu-Ser-Ala-Gly in its lipolitic active site, belongs to carboxylesterase family as a serine-type esterase Sus scrofa