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Literature summary for 3.1.1.1 extracted from

  • Camacho, R.M.; Mateos, J.C.; Gonzalez-Reynoso, O.; Prado, L.A.; Cordova, J.
    Production and characterization of esterase and lipase from Haloarcula marismortui (2009), J. Ind. Microbiol. Biotechnol., 36, 901-909.
    View publication on PubMed

Localization

Localization Comment Organism GeneOntology No. Textmining
intracellular
-
Haloarcula marismortui 5622
-

Metals/Ions

Metals/Ions Comment Organism Structure
NaCl presence of two esterase activities, one of them more active at low salt concentrations, and the second one is more active at high salt concentrations Haloarcula marismortui

Organism

Organism UniProt Comment Textmining
Haloarcula marismortui
-
-
-
Haloarcula marismortui DSM 3752
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-nitrophenyl pentanoate + H2O
-
Haloarcula marismortui 4-nitrophenol + pentanoate
-
?
4-nitrophenyl pentanoate + H2O
-
Haloarcula marismortui DSM 3752 4-nitrophenol + pentanoate
-
?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
45
-
-
Haloarcula marismortui

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
25 70 25°C: esterase shows 55.9% relative activity, 70°C: 23.3% of maximal activity Haloarcula marismortui