Family: Cholesterol_esterase

Block: C

Parent Family: Carboxylesterase


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 :


Peptide in Fasta
Nucleotide in Fasta
Alignment with Multalin Text only
Seed alignment with MAFFT No colour
Alignment with MAFFT No colour
Dendrogram The dnd file

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)

References (6)

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
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
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
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
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
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
PubMedID: 9331420
Gene_locus related to this paper: bovin-balip