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Literature summary for 3.1.1.79 extracted from

  • Ascione, G.; de Pascale, D.; De Santi, C.; Pedone, C.; Dathan, N.A.; Monti, S.M.
    Native expression and purification of hormone-sensitive lipase from Psychrobacter sp. TA144 enhances protein stability and activity (2012), Biochem. Biophys. Res. Commun., 420, 542-546.
    View publication on PubMed
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Application

Application Comment Organism
synthesis the enzyme catalyzes the hydrolysis of fatty acid esters at very low temperature and is therefore of great potential industrial and pharmaceutical interest Psychrobacter sp.

Cloned(Commentary)

Cloned (Comment) Organism
expression of the entire enzyme, N-terminally and C-terminally His6-tagged, as a fully soluble protein in Escherichia coli in the presence of either the osmolyte trehalose, plus high salt concentration, or the membrane fluidizer benzyl alcohol. Addition of these compounds proves to be decisive in procuring a high expression level of stable, soluble, full-length recombinant protein Psychrobacter sp.

General Stability

General Stability Organism
the entire enzyme recombinantly expressed as a fully soluble protein is more stable than its previously expressed recombinant counterpart, an insoluble form of the entire enzyme, cloned and expressed in Escherichia coli, and subsequently refolded to the active form, circular dichroism Psychrobacter sp.

Organism

Organism UniProt Comment Textmining
Psychrobacter sp.
-
 originally isolated from Antarctic sea water
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Psychrobacter sp. TA144
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 originally isolated from Antarctic sea water
-

Purification (Commentary)

Purification (Comment) Organism
recombinant N- and C-terminally His6-tagged soluble full-length enzyme from Escherichia coli by nickel affinity chromatography and gel filtration Psychrobacter sp.

Subunits

Subunits Comment Organism
monomer entire enzyme recombinantly expressed as a fully soluble protein, purified from benzyl alcohol treatment, light scattering analysis, the enzyme contains 29% alpha-helix and 18% beta-sheet Psychrobacter sp.

Synonyms

Synonyms Comment Organism
13-HSL
-
 Psychrobacter sp.
HSL
-
 Psychrobacter sp.

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
25 40 the entire enzyme recombinantly expressed as a fully soluble protein is more stable at 40°C than its previously expressed recombinant counterpart, an insoluble form of the entire enzyme, cloned and expressed in Escherichia coli, and subsequently refolded to the active form Psychrobacter sp.
49
-
 melting temperature of the purified recombinant fully soluble full-length enzyme, irreversible inactivation. The thermally denatured HSL at 75°C still contains a substantial amount of secondary structure Psychrobacter sp.

General Information

General Information Comment Organism
additional information the hormone-sensitive lipase catalyzes the hydrolysis of fatty acid esters at very low temperature and is extremely active Psychrobacter sp.