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Literature summary for 3.1.1.1 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)

Cloned (Comment) Organism
expressed in Escherichia coli Haloarcula marismortui

General Stability

General Stability Organism
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

Inhibitors Comment Organism Structure
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
E600 half-inactivation times of 20 s, at an inhibitor:enzyme molar ratio is 10:1 Haloarcula marismortui
phenylmethylsulfonyl fluoride half-inactivation times is 10 s, at an inhibitor:enzyme molar ratio of 10:1 Haloarcula marismortui

Metals/Ions

Metals/Ions Comment Organism Structure
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

Organism UniProt Comment Textmining
Haloarcula marismortui Q5V5N6
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Haloarcula marismortui

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 ?
-
?
vinyl acetate + H2O 30.5% of the activity with vinyl butyrate Haloarcula marismortui vinyl alcohol + acetate
-
?
vinyl butyrate + H2O
-
Haloarcula marismortui vinyl alcohol + butyrate
-
?
vinyl hexanoate + H2O 68% of the activity with vinyl butyrate Haloarcula marismortui vinyl alcohol + hexanoate
-
?
vinyl propionate + H2O 55% of the activity with vinyl butyrate Haloarcula marismortui vinyl alcohol + propionate
-
?

Synonyms

Synonyms Comment Organism
LipC
-
Haloarcula marismortui

Temperature Stability [°C]

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

pH Optimum

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

pH Range

pH Minimum pH Maximum Comment Organism
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

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