The human lactating mammary gland and pancreas produce a lipolytic enzyme, carboxyl-ester lipase, earlier called bile salt-stimulated lipase. Carboxyl-ester lipase is a major component of pancreatic juice and is responsible for the hydrolysis of cholesterol esters as well as a variety of other dietary esters. The enzyme is activated when mixed with bile salts, and plays an important role in the digestion of milk fat in newborn infants. This enzyme combines properties of esterases (activity on esters soluble in water) and lipases (activity on insoluble long chain acylglycerols) Numerous repeats at the c-term excluded in ESTHER (only n-term Pfam A COesterase 1 544)
Interpro : IPR002018 Carboxylesterase, type B , IPR033560 Bile salt-activated lipase BAL
PIRSF : PIRSF005676 COesterase
Pdoc : PDOC00112
Pfam : PF00135 COesterase
Prints : No Print
EC Number : 3.1.1.13
Structures (10)
Genes Proteins in Cholesterol_esterase family (128)
Fragments of genes in Cholesterol_esterase family (65)
Structures in Cholesterol_esterase family (10)Substrates in Cholesterol_esterase family (13)
Inhibitors in Cholesterol_esterase family (15)
Title : Comparative Study of the Molecular Characterization, Evolution, and Structure Modeling of Digestive Lipase Genes Reveals the Different Evolutionary Selection Between Mammals and Fishes - Tang_2022_Front.Genet_13_909091 |
Author(s) : Tang SL , Liang XF , He S , Li L , Alam MS , Wu J |
Ref : Front Genet , 13 :909091 , 2022 |
Abstract : Tang_2022_Front.Genet_13_909091 |
ESTHER : Tang_2022_Front.Genet_13_909091 |
PubMedSearch : Tang_2022_Front.Genet_13_909091 |
PubMedID: 35991544 |
Title : Comparative Structures and Evolution of Vertebrate Carboxyl Ester Lipase (CEL) Genes and Proteins with a Major Role in Reverse Cholesterol Transport - Holmes_2011_Cholesterol_2011_781643 |
Author(s) : Holmes RS , Cox LA |
Ref : Cholesterol , 2011 :781643 , 2011 |
Abstract : Holmes_2011_Cholesterol_2011_781643 |
ESTHER : Holmes_2011_Cholesterol_2011_781643 |
PubMedSearch : Holmes_2011_Cholesterol_2011_781643 |
PubMedID: 22162806 |
Title : The structure of truncated recombinant human bile salt-stimulated lipase reveals bile salt-independent conformational flexibility at the active-site loop and provides insights into heparin binding - Moore_2001_J.Mol.Biol_312_511 |
Author(s) : Moore SA , Kingston RL , Loomes KM , Hernell O , Blackberg L , Baker HM , Baker EN |
Ref : Journal of Molecular Biology , 312 :511 , 2001 |
Abstract : Moore_2001_J.Mol.Biol_312_511 |
ESTHER : Moore_2001_J.Mol.Biol_312_511 |
PubMedSearch : Moore_2001_J.Mol.Biol_312_511 |
PubMedID: 11563913 |
Gene_locus related to this paper: human-CEL |
Title : Crystal structure of the catalytic domain of human bile salt activated lipase - Terzyan_2000_Protein.Sci_9_1783 |
Author(s) : Terzyan S , Wang CS , Downs D , Hunter B , Zhang XC |
Ref : Protein Science , 9 :1783 , 2000 |
Abstract : Terzyan_2000_Protein.Sci_9_1783 |
ESTHER : Terzyan_2000_Protein.Sci_9_1783 |
PubMedSearch : Terzyan_2000_Protein.Sci_9_1783 |
PubMedID: 11045623 |
Gene_locus related to this paper: human-CEL |
Title : Structure of bovine pancreatic cholesterol esterase at 1.6 A: novel structural features involved in lipase activation - Chen_1998_Biochemistry_37_5107 |
Author(s) : Chen JC , Miercke LJ , Krucinski J , Starr JR , Saenz G , Wang X , Spilburg CA , Lange LG , Ellsworth JL , Stroud RM |
Ref : Biochemistry , 37 :5107 , 1998 |
Abstract : Chen_1998_Biochemistry_37_5107 |
ESTHER : Chen_1998_Biochemistry_37_5107 |
PubMedSearch : Chen_1998_Biochemistry_37_5107 |
PubMedID: 9548741 |
Gene_locus related to this paper: bovin-balip |
Title : The crystal structure of bovine bile salt activated lipase: insights into the bile salt activation mechanism - Wang_1997_Structure_5_1209 |
Author(s) : Wang X , Wang CS , Tang J , Dyda F , Zhang XC |
Ref : Structure , 5 :1209 , 1997 |
Abstract : Wang_1997_Structure_5_1209 |
ESTHER : Wang_1997_Structure_5_1209 |
PubMedSearch : Wang_1997_Structure_5_1209 |
PubMedID: 9331420 |
Gene_locus related to this paper: bovin-balip |