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Literature summary for 3.1.1.1 extracted from

  • Lombardo, D.; Guy, O.; Figarella, C.
    Purification and characterization of a carboxyl ester hydrolase from human pancreatic juice (1978), Biochim. Biophys. Acta, 527, 142-149.
    View publication on PubMed
Search for more literature for 3.1.1.1

General Stability

General Stability Organism
50% loss of activity upon lyophilization Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
DFP
-
 Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.44
-
 4-nitrophenyl acetate
-
 Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
biliary salts activates Homo sapiens

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
100000
-
 x * 100000, SDS-PAGE Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
side-chain modification glycoprotein Homo sapiens
side-chain modification contains 5.2% neutral carbohydrate, 4.3 mol glucosamine and 17 mol of galactosamine per mol of enzyme Homo sapiens

Purification (Commentary)

Purification (Comment) Organism
-
 Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
pancreatic juice
-
 Homo sapiens
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
40
-
-
 Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-nitrophenyl acetate + H2O
-
 Homo sapiens 4-nitrophenol + acetate
-
 ?

Subunits

Subunits Comment Organism
? x * 100000, SDS-PAGE Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 hydrolysis of p-nitrophenyl acetate Homo sapiens