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Literature summary extracted from

  • Müller-Santos, M.; de Souza, E.M.; Pedrosa, Fde O.; Mitchell, D.A., Longhi, S.; Carrière, F.; Canaan, S.; Krieger, N.
    First evidence for the salt-dependent folding and activity of an esterase from the halophilic archaea Haloarcula marismortui (2009), Biochim. Biophys. Acta, 1791, 719-729.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.1.1 expressed in Escherichia coli Haloarcula marismortui

General Stability

EC Number General Stability Organism
3.1.1.1 the enzyme is totally unfolded in salt-free medium and secondary structure appears in the presence of 0.25–0.5 M KCl. After salt depletion, the protein is able to recover 60% of its initial activity when 2 M KCl is added Haloarcula marismortui

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.1.1 5-methoxy-3-(4-phenoxyphenyl)-3H-[1,3,4]oxadiazol-2-one half-inactivation time is 15 min, at an inhibitor:enzyme molar ratio of 100:1 Haloarcula marismortui
3.1.1.1 E600 half-inactivation times of 20 s, at an inhibitor:enzyme molar ratio is 10:1 Haloarcula marismortui
3.1.1.1 phenylmethylsulfonyl fluoride half-inactivation times is 10 s, at an inhibitor:enzyme molar ratio of 10:1 Haloarcula marismortui

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.1.1 KCl activity is optimal in the presence of 3 M KCl and no activity is detected in the absence of salts. The enzyme is totally unfolded in salt-free medium and secondary structure appears in the presence of 0.25-0.5 M KCl. After salt depletion, the protein is able to recover 60% of its initial activity when 2 M KCl is added Haloarcula marismortui

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.1 Haloarcula marismortui Q5V5N6
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.1.1
-
Haloarcula marismortui

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.1.1.1 590
-
pH 8.5, temperature not specified in the publication, substrate: vinyl butyrate Haloarcula marismortui

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.1 additional information specific activities on tri-, di- and monoacylglycerols are much lower than those measured with the shorter-chain vinyl esters and decreases with increasing acyl chain length. No detectable activity of the enzyme on vinyl esters and glycerol esters that have acyl chains longer than 12 carbon atoms Haloarcula marismortui ?
-
?
3.1.1.1 vinyl acetate + H2O 30.5% of the activity with vinyl butyrate Haloarcula marismortui vinyl alcohol + acetate
-
?
3.1.1.1 vinyl butyrate + H2O
-
Haloarcula marismortui vinyl alcohol + butyrate
-
?
3.1.1.1 vinyl hexanoate + H2O 68% of the activity with vinyl butyrate Haloarcula marismortui vinyl alcohol + hexanoate
-
?
3.1.1.1 vinyl propionate + H2O 55% of the activity with vinyl butyrate Haloarcula marismortui vinyl alcohol + propionate
-
?

Synonyms

EC Number Synonyms Comment Organism
3.1.1.1 LipC
-
Haloarcula marismortui

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.1.1.1 40
-
2 h, no loss of activity Haloarcula marismortui
3.1.1.1 50
-
2 h, 4.5% loss of activity Haloarcula marismortui
3.1.1.1 60
-
5 min, complete loss of activity Haloarcula marismortui

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.1.1 8.5
-
substrate: vinyl butyrate Haloarcula marismortui

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.1.1.1 5 9 not active on vinyl butyrate at pH values below 5.0, above pH 5.0 the specific activity increases with pH, reaching a maximum of 590 U/mg at pH 8.5, pH 9.0: 78% of the maximum activity, substrate: vinyl butyrate Haloarcula marismortui

pI Value

EC Number Organism Comment pI Value Maximum pI Value
3.1.1.1 Haloarcula marismortui calculated from sequence
-
4.2