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Literature summary extracted from

  • Ejima, K.; Liu, J.; Oshima, Y.; Hirooka, K.; Shimanuki, S.; Yokota, Y.; Hemmi, H.; Nakayama, T.; Nishino, T.
    Molecular cloning and characterization of a thermostable carboxylesterase from an archaeon, Sulfolobus shibatae DSM5389: non-linear kinetic behavior of a hormone-sensitive lipase family enzyme (2004), J. Biosci. Bioeng., 98, 445-451.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.1.1
-
Saccharolobus shibatae
3.1.1.1 overexpression in Escherichia coli as a soluble catalytically active protein Saccharolobus shibatae

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.1.1 HgCl2 1 mM, 11% residual activity; 1 mM, 89% inhibition Saccharolobus shibatae
3.1.1.1 additional information not inhibitory: EDTA, CaCl2, MgCl2, CuCl2, CoCl2, FeCl2, MnCl2, N-bromosuccinimide, diethylpyrocarbonate Saccharolobus shibatae
3.1.1.1 phenylmethylsulfonyl fluoride 1 mM, 4% inhibition; 1 mM, 4% residual activity Saccharolobus shibatae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.1.1 0.01
-
p-nitrophenyl butanoate
-
Saccharolobus shibatae
3.1.1.1 0.01
-
4-nitrophenyl butyrate pH 7.2, 37°C Saccharolobus shibatae
3.1.1.1 0.013
-
p-nitrophenyl acetate
-
Saccharolobus shibatae
3.1.1.1 0.013
-
4-nitrophenyl acetate pH 7.2, 37°C Saccharolobus shibatae
3.1.1.1 0.039
-
p-nitrophenyl valerate
-
Saccharolobus shibatae
3.1.1.1 0.039
-
4-nitrophenyl pentanoate pH 7.2, 37°C Saccharolobus shibatae

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.1.1.1 33000
-
and drimer, 3 *33000, calculated, 3 * 33000, SDS-PAGE Saccharolobus shibatae
3.1.1.1 33000
-
and trimer, 2 *33000, calculated, 2 * 33000, SDS-PAGE Saccharolobus shibatae
3.1.1.1 33000
-
2 * 33000, enzyme exists as a mixture of dimeric and trimeric forms, SDS-PAGE Saccharolobus shibatae
3.1.1.1 33000
-
3 * 33000, enzyme exists as a mixture of dimeric and trimeric forms, SDS-PAGE Saccharolobus shibatae
3.1.1.1 64000
-
dimer, gel filtration Saccharolobus shibatae
3.1.1.1 90000
-
trimer, gel filtration Saccharolobus shibatae

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.1 Saccharolobus shibatae
-
strain DSM5389, expression in Escherichia coli
-
3.1.1.1 Saccharolobus shibatae
-
DSM5389
-
3.1.1.1 Saccharolobus shibatae DSM 5389
-
strain DSM5389, expression in Escherichia coli
-
3.1.1.1 Saccharolobus shibatae DSM 5389
-
DSM5389
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.1.1 recombinant enzyme Saccharolobus shibatae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.1 4-nitrophenyl acetate + H2O 15% of the activity with 4-nitrophenyl butyrate Saccharolobus shibatae 4-nitrophenol + acetate
-
?
3.1.1.1 4-nitrophenyl acetate + H2O 15% of the activity with 4-nitrophenyl butyrate Saccharolobus shibatae DSM 5389 4-nitrophenol + acetate
-
?
3.1.1.1 4-nitrophenyl butyrate + H2O
-
Saccharolobus shibatae 4-nitrophenol + butyrate
-
?
3.1.1.1 4-nitrophenyl butyrate + H2O
-
Saccharolobus shibatae DSM 5389 4-nitrophenol + butyrate
-
?
3.1.1.1 4-nitrophenyl palmitate + H2O
-
Saccharolobus shibatae 4-nitrophenol + palmitate
-
?
3.1.1.1 4-nitrophenyl pentanoate + H2O 79% of the activity with 4-nitrophenyl butyrate Saccharolobus shibatae 4-nitrophenol + pentanoate
-
?
3.1.1.1 additional information no substrate: tributyrin, triolein Saccharolobus shibatae ?
-
?
3.1.1.1 additional information no hydrolysis of tributyrin and triolein Saccharolobus shibatae ?
-
?
3.1.1.1 additional information no substrate: tributyrin, triolein Saccharolobus shibatae DSM 5389 ?
-
?
3.1.1.1 additional information no hydrolysis of tributyrin and triolein Saccharolobus shibatae DSM 5389 ?
-
?
3.1.1.1 p-nitrophenyl acetate + H2O hydrolysis proceeds in linear manner, 15% of the reaction rate with p-nitrophenyl butyrate Saccharolobus shibatae p-nitrophenol + acetate
-
?
3.1.1.1 p-nitrophenyl acetate + H2O hydrolysis proceeds in linear manner, 15% of the reaction rate with p-nitrophenyl butyrate Saccharolobus shibatae DSM 5389 p-nitrophenol + acetate
-
?
3.1.1.1 p-nitrophenyl butanoate + H2O
-
Saccharolobus shibatae p-nitrophenol + butanoate
-
?
3.1.1.1 p-nitrophenyl pentanoate + H2O and substrates with longer acyl chains, hydrolysis proceeds in biophasic manner Saccharolobus shibatae p-nitrophenol + pentanoate
-
?
3.1.1.1 p-nitrophenyl valerate + H2O 79% of the reaction rate with p-nitrophenyl butyrate Saccharolobus shibatae p-nitrophenol + valeric acid
-
?

Subunits

EC Number Subunits Comment Organism
3.1.1.1 dimer and trimer, 2 *33000, calculated, 2 * 33000, SDS-PAGE Saccharolobus shibatae
3.1.1.1 dimer 2 * 33000, enzyme exists as a mixture of dimeric and trimeric forms, SDS-PAGE Saccharolobus shibatae
3.1.1.1 trimer and drimer, 3 *33000, calculated, 3 * 33000, SDS-PAGE Saccharolobus shibatae
3.1.1.1 trimer 3 * 33000, enzyme exists as a mixture of dimeric and trimeric forms, SDS-PAGE Saccharolobus shibatae

Synonyms

EC Number Synonyms Comment Organism
3.1.1.1 SshEstI esterase
-
Saccharolobus shibatae

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.1.1.1 60
-
60 min, pH 7.0, full activity Saccharolobus shibatae
3.1.1.1 90
-
30 min, pH 7.0, more than 70% residual activity Saccharolobus shibatae

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.1.1 7 8
-
Saccharolobus shibatae

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.1.1.1 2.5
-
30 min, 60% residual activity Saccharolobus shibatae

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.1.1.1 2.5
-
30 min, 60% residual activity Saccharolobus shibatae
3.1.1.1 2.5
-
60°C, 30 min, enzyme retains 60% of its initial activity Saccharolobus shibatae
3.1.1.1 6 8
-
Saccharolobus shibatae