Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.1.1.79 extracted from

  • Choi, Y.H.; Lee, Y.N.; Park, Y.J.; Yoon, S.J.; Lee, H.B.
    Identification of amino acids related to catalytic function of Sulfolobus solfataricus P1 carboxylesterase by site-directed mutagenesis and molecular modeling (2016), BMB Rep., 49, 349-354 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
sequence comparisons, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21 (DE3), subcloning in Escherichia coli strain DH5alpha Saccharolobus solfataricus

Protein Variants

Protein Variants Comment Organism
A152F site-directed mutagenesis, the mutant shows 12.83% activity compared to wild-type Saccharolobus solfataricus
C101S site-directed mutagenesis, the mutant shows 31.55% activity compared to wild-type Saccharolobus solfataricus
C103S site-directed mutagenesis, the mutant shows 17.95% activity compared to wild-type Saccharolobus solfataricus
C184S site-directed mutagenesis, the mutant shows 16.93% activity compared to wild-type Saccharolobus solfataricus
C94S site-directed mutagenesis, the mutant shows 11.90% activity compared to wild-type Saccharolobus solfataricus
D244N site-directed mutagenesis, the mutant shows 1.55% activity compared to wild-type Saccharolobus solfataricus
G80E site-directed mutagenesis, the mutant shows 14.09% activity compared to wild-type Saccharolobus solfataricus
G81E site-directed mutagenesis, the mutant shows 16.94% activity compared to wild-type Saccharolobus solfataricus
H274N site-directed mutagenesis, almost inactive mutant Saccharolobus solfataricus
additional information the cysteine residues are located near the active site or at the positions inducing any conformational changes of the enzyme by their replacement with serine residues Saccharolobus solfataricus
S151A site-directed mutagenesis, inactive mutant Saccharolobus solfataricus

Inhibitors

Inhibitors Comment Organism Structure
4-chloromercuribenzoate
-
Saccharolobus solfataricus
diethyl dicarbonate
-
Saccharolobus solfataricus
diisopropylfluorophosphate
-
Saccharolobus solfataricus
HgCl2
-
Saccharolobus solfataricus
PMSF
-
Saccharolobus solfataricus

Organism

Organism UniProt Comment Textmining
Saccharolobus solfataricus A0A0E3GVY6
-
-
Saccharolobus solfataricus DSM1616 A0A0E3GVY6
-
-
Saccharolobus solfataricus P1 A0A0E3GVY6
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type 19.35fold to homogeneity and of mutant enzymes, from Escherichia coli strain BL21 (DE3), by heat treatment and hydrophobic interaction chromatography Saccharolobus solfataricus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-nitrophenol caprylate + H2O
-
Saccharolobus solfataricus 4-nitrophenol + caprylate
-
?
4-nitrophenol caprylate + H2O
-
Saccharolobus solfataricus P1 4-nitrophenol + caprylate
-
?
4-nitrophenol caprylate + H2O
-
Saccharolobus solfataricus DSM1616 4-nitrophenol + caprylate
-
?
tributyrin + H2O
-
Saccharolobus solfataricus dibutyrin + butyrate
-
?
tributyrin + H2O
-
Saccharolobus solfataricus P1 dibutyrin + butyrate
-
?
tributyrin + H2O
-
Saccharolobus solfataricus DSM1616 dibutyrin + butyrate
-
?

Subunits

Subunits Comment Organism
? x * 33500, about, sequence calculation, x * 34000, recombinant wild-type and mutant enzymes, SDS-PAGE Saccharolobus solfataricus

Synonyms

Synonyms Comment Organism
alpha/beta hydrolase UniProt Saccharolobus solfataricus
HSL-like carboxylesterase
-
Saccharolobus solfataricus
SsoP1Est
-
Saccharolobus solfataricus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
60
-
assay at Saccharolobus solfataricus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
assay at Saccharolobus solfataricus

General Information

General Information Comment Organism
evolution archaeon Sulfolobus solfataricus P1 carboxylesterase is a thermostable enzyme belonging to the mammalian hormone-sensitive lipase (HSL) family. Enzyme SsoP1Est belongs to the HSL family exhibiting a classic alpha/beta hydrolase fold by sequence alignment with homologous esterases, which were well characterized in the structure. Thus, it contains a typical catalytic triad of esterases, which is expected to be composed of Ser151, Asp244, and His274, and another typical oxyanion hole, which is presumed to be composed of Gly80, Gly81, and Ala152 Saccharolobus solfataricus
additional information residues Ser151, Asp244, and His274 form the catalytic triad of the native SsoP1Est, residues Gly80, Gly81, and Ala152 form the oxyanion hole. Enzyme structure homology modeling, overview Saccharolobus solfataricus