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Literature summary extracted from

  • Berton, A.; Sebban-Kreuzer, C.; Crenon, I.
    Role of the structural domains in the functional properties of pancreatic lipase-related protein 2 (2007), FEBS J., 274, 6011-6023.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.1.1.3 Colipase required for full activity by the pancreatic lipase, the inability of PLRP2 to form a high-affinity complex with colipase is only due to the C-terminal domain, the N-terminal domain can interact with the colipase, overview Equus caballus
3.1.1.3 additional information activation of the pancreatic lipase is a mechanism allowing accessibility of the active site to the substrate and resulting in the unmasking of the catalytic triad of the enzyme induced by the motion of the flap Equus caballus
3.1.1.3 sodium taurodeoxycholate bile salts are required by the pancreatic lipase, optimal activation at 0.1 mM, inhibits the recombinant chimeric protein NcC2 at concentration above 2 mM Equus caballus

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.1.3 expression of chimeric proteins NcC2 and N2Cc in Spodoptera frugiperda Sf9 cells using the baculovirus infection system Equus caballus

Protein Variants

EC Number Protein Variants Comment Organism
3.1.1.3 additional information construction of two chimeric proteins, NcC2 and N2Cc, by swapping the N and C structural domains between the horse pancreatic lipase Nc and Cc domains and the horse PLRP2 N2 and C2 domains, in contrast to N2Cc, NcC2 is highly sensitive to interfacial denaturation, the lipolytic activity of both chimeric proteins is inhibited by bile salts and not restorable by colipase, N2Cc is a strong inhibitor of pancreatic lipase activity due to competition for colipase binding, overview, NcCc is probably irreversibly inactivated at the surface of tributyrin droplets Equus caballus

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.1.3 E600 different inhibition levels of recombinant wild-type enzymes and chimeric mutant enzymes, influenced by bile salt, overview Equus caballus
3.1.1.3 additional information pancreatic lipase NcCc is probably irreversibly inactivated at the surface of tributyrin droplets which is prevented by colipase Equus caballus
3.1.1.3 sodium taurodeoxycholate bile salts are required by the pancreatic lipase, optimal activation at 0.1 mM, inhibits the recombinant chimeric protein NcC2 at concentration above 2 mM Equus caballus

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.3 Equus caballus
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
3.1.1.3 triacylglycerol + H2O = diacylglycerol + a carboxylate activation of the pancreatic lipase is a mechanism allowing accessibility of the active site to the substrate and resulting in the unmasking of the catalytic triad of the enzyme induced by the motion of the flap Equus caballus
a

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.1.1.3 560
-
 purified PLRP2 N2 and C2 domains in the absence and in the presence of colipase Equus caballus
3.1.1.3 650
-
 purified recombinant chimeric protein N2Cc in the presence of colipase and bile salts Equus caballus
3.1.1.3 3000
-
 purified pancreatic lipase Nc and Cc domains in the presence of colipase and bile salts Equus caballus
3.1.1.3 6000
-
 purified recombinant chimeric protein NcC2 in the presence of colipase and bile salts Equus caballus
3.1.1.3 8000
-
 purified pancreatic lipase Nc and Cc domains in the presence of colipase and 0.1 mM sodium taurodeoxycholate, incubation with colipase prior to activity assay Equus caballus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.3 additional information PLRP and pancreatic lipase differ in enzymatic properties such as substrate specificity, sensitivity to inhibition by bile salts and colipase dependence Equus caballus ?
-
 ?
3.1.1.3 tributyrin + H2O
-
 Equus caballus dibutyrin + butyrate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.1.1.3 Pancreatic lipase
-
 Equus caballus
3.1.1.3 pancreatic lipase-related protein 2
-
 Equus caballus
3.1.1.3 PLRP2
-
 Equus caballus