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Literature summary extracted from

  • Ay, F.; Karaoglu, H.; Inan, K.; Canakci, S.; Belduz, A.O.
    Cloning, purification and characterization of a thermostable carboxylesterase from Anoxybacillus sp. PDF1 (2011), Protein Expr. Purif., 80, 74-79.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.1.1.1 beta-mercaptoethanol 1% (v/v) activates carboxylesterase in a range of 136% and 244% after 0 and 30 min of incubation Anoxybacillus sp.
3.1.1.1 dithiothreitol 5 mM dithiothreitol increases the activity at 171% after the incubation of the enzyme for 30 min Anoxybacillus sp.

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.1.1 expressed in Escherichia coli BL21(DE3) cells Anoxybacillus sp.

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.1.1 Co2+ about 42% residual activity at 5 mM Co2+ after 1 h of incubation Anoxybacillus sp.
3.1.1.1 EDTA 95% residual activity at 5 mM Anoxybacillus sp.
3.1.1.1 phenylmethylsulfonyl fluoride complete inhibition at 5 mM Anoxybacillus sp.
3.1.1.1 SDS 36% residual activity at 0.1% (w/v) after 30 min of incubation Anoxybacillus sp.
3.1.1.1 Zn2+ about 10% residual activity at 5 mM Zn2+ after 1 h of incubation Anoxybacillus sp.

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.1.1 0.348
-
4-nitrophenyl butyrate apparent value, pH 8.0, 60°C Anoxybacillus sp.

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.1.1 Ca2+ 1 mM Ca2+ leads to some activation after 15 min Anoxybacillus sp.
3.1.1.1 K+ 1 mM K+ leads to some activation after 15 min Anoxybacillus sp.
3.1.1.1 Li+ 1 mM Li+ leads to some activation after 15 min Anoxybacillus sp.
3.1.1.1 additional information not influenced by Mg2+ Anoxybacillus sp.

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.1.1.1 26000
-
x * 26000, SDS-PAGE Anoxybacillus sp.

Organic Solvent Stability

EC Number Organic Solvent Comment Organism
3.1.1.1 DMSO 97% residual activity at 1% (v/v) after 30 min of incubation Anoxybacillus sp.
3.1.1.1 Ethanol 92% residual activity at 1% (v/v) after 30 min of incubation Anoxybacillus sp.
3.1.1.1 isopropanol 99% residual activity at 1% (v/v) after 30 min of incubation Anoxybacillus sp.

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.1 Anoxybacillus sp.
-
-
-
3.1.1.1 Anoxybacillus sp. PDF1
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.1.1 heat shock precipitation and Q-Sepharose column chromatography Anoxybacillus sp.

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.1 4-nitrophenyl butyrate + H2O high level of activity with 4-nitrophenyl butyrate (100%) Anoxybacillus sp. 4-nitrophenol + butyrate
-
?
3.1.1.1 4-nitrophenyl butyrate + H2O high level of activity with 4-nitrophenyl butyrate (100%) Anoxybacillus sp. PDF1 4-nitrophenol + butyrate
-
?
3.1.1.1 4-nitrophenyl laurate + H2O 37% activity compared to 4-nitrophenyl butyrate Anoxybacillus sp. 4-nitrophenol + laurate
-
?
3.1.1.1 4-nitrophenyl laurate + H2O 37% activity compared to 4-nitrophenyl butyrate Anoxybacillus sp. PDF1 4-nitrophenol + laurate
-
?
3.1.1.1 4-nitrophenyl palmitate + H2O 5% activity compared to 4-nitrophenyl butyrate Anoxybacillus sp. 4-nitrophenol + palmitate
-
?
3.1.1.1 4-nitrophenyl palmitate + H2O 5% activity compared to 4-nitrophenyl butyrate Anoxybacillus sp. PDF1 4-nitrophenol + palmitate
-
?
3.1.1.1 additional information carboxylesterase has serine residue in active site and -SH groups in specific sites which are required for its activity Anoxybacillus sp. ?
-
?
3.1.1.1 additional information carboxylesterase has serine residue in active site and -SH groups in specific sites which are required for its activity Anoxybacillus sp. PDF1 ?
-
?

Subunits

EC Number Subunits Comment Organism
3.1.1.1 ? x * 26000, SDS-PAGE Anoxybacillus sp.

Synonyms

EC Number Synonyms Comment Organism
3.1.1.1 Carboxylic-ester hydrolase
-
Anoxybacillus sp.
3.1.1.1 EST
-
Anoxybacillus sp.

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.1.1 60 65
-
Anoxybacillus sp.

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.1.1.1 25 90 the enzymatic activity decreases significantly at temperatures below 25°C and above 90°C Anoxybacillus sp.

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.1.1.1 60 75 at 60 and 65°C, the enzyme is stable for half an hour; whereas incubation at 70°C for half an h leads to a 50% loss of activity. At 65°C, the stability of carboxylesterase decreases to 70% of the total. After 70°C, a sharp decline in the enzyme activity is observed Anoxybacillus sp.

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.1.1.1 1500
-
4-nitrophenyl butyrate apparent value, pH 8.0, 60°C Anoxybacillus sp.

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.1.1 8
-
-
Anoxybacillus sp.

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.1.1.1 5 10
-
Anoxybacillus sp.