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Literature summary for 3.1.1.1 extracted from

  • Espinosa-Luna, G.; Sanchez-Otero, M.G.; Quintana-Castro, R.; Matus-Toledo, R.E.; Oliart-Ros, R.M.
    Gene cloning and characterization of the Geobacillus thermoleovorans CCR11 carboxylesterase CaesCCR11, a new member of family XV (2016), Mol. Biotechnol., 58, 37-46 .
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
2-mercaptoethanol 1% v/v, 141.5% activity Geobacillus thermoleovorans
EDTA 1 mM, 143.2% activity Geobacillus thermoleovorans
Triton X-100 1% v/v, 136.9% activity Geobacillus thermoleovorans
Tween 20 1% v/v, 121.9% activity Geobacillus thermoleovorans

Cloned(Commentary)

Cloned (Comment) Organism
gene caesCCR11, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis and tree, recombinant expression in Escherichia coli strain BL21(DE3) Geobacillus thermoleovorans

Inhibitors

Inhibitors Comment Organism Structure
acetone
-
Geobacillus thermoleovorans
butanol
-
Geobacillus thermoleovorans
dioxane
-
Geobacillus thermoleovorans
ethanol
-
Geobacillus thermoleovorans
ethyl acetate
-
Geobacillus thermoleovorans
heptane
-
Geobacillus thermoleovorans
hexane
-
Geobacillus thermoleovorans
Hg2+ 90% inhibition Geobacillus thermoleovorans
K+ 10% inhibition Geobacillus thermoleovorans
methanol
-
Geobacillus thermoleovorans
PMSF 1 mM, 85% inhibition Geobacillus thermoleovorans
Propanol
-
Geobacillus thermoleovorans
SDS 0.1% w/v, 24.2% inhibition Geobacillus thermoleovorans

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
Geobacillus thermoleovorans
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Ba2+ activates slightly Geobacillus thermoleovorans
Li+ activates slightly Geobacillus thermoleovorans
Mg2+ activates slightly Geobacillus thermoleovorans
Na+ activates slightly Geobacillus thermoleovorans

Organic Solvent Stability

Organic Solvent Comment Organism
Acetone 21.8% residual activity after 1 h Geobacillus thermoleovorans
Butanol 22.9% residual activity after 1 h Geobacillus thermoleovorans
dioxane 13.2% residual activity after 1 h Geobacillus thermoleovorans
Ethanol 27.5% residual activity after 1 h Geobacillus thermoleovorans
Ethyl acetate 24.8% residual activity after 1 h Geobacillus thermoleovorans
heptane 74.6% residual activity after 1 h Geobacillus thermoleovorans
hexane 59.2% residual activity after 1 h Geobacillus thermoleovorans
Methanol 12.7% residual activity after 1 h Geobacillus thermoleovorans
propanol 13.1% residual activity after 1 h Geobacillus thermoleovorans

Organism

Organism UniProt Comment Textmining
Geobacillus thermoleovorans W8QMJ2 isolated from El Carrizal hot springs in Veracruz, Mexico
-
Geobacillus thermoleovorans CCR11 W8QMJ2 isolated from El Carrizal hot springs in Veracruz, Mexico
-

Purification (Commentary)

Purification (Comment) Organism
native extracellular enzyme and recombinant enzyme by ultrafiltration Geobacillus thermoleovorans

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1375.7
-
purified recombinant enzyme, pH 6.5, 30°C, substrate 4-nitrophenyl laurate Geobacillus thermoleovorans

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-nitrophenyl butyrate + H2O best substrate Geobacillus thermoleovorans 4-nitrophenol + butyrate
-
?
4-nitrophenyl butyrate + H2O best substrate Geobacillus thermoleovorans CCR11 4-nitrophenol + butyrate
-
?
4-nitrophenyl caprate + H2O
-
Geobacillus thermoleovorans 4-nitrophenol + caprate
-
?
4-nitrophenyl caprate + H2O
-
Geobacillus thermoleovorans CCR11 4-nitrophenol + caprate
-
?
4-nitrophenyl caproate + H2O
-
Geobacillus thermoleovorans 4-nitrophenol + caproate
-
?
4-nitrophenyl caproate + H2O
-
Geobacillus thermoleovorans CCR11 4-nitrophenol + caproate
-
?
additional information enzyme CaesCCR11 has a preference for C4 substrates. Activity toward 4-nitrophenyl esters with longer chain lengths is only slightly detected, suggesting that CaesCCR11 is an esterase Geobacillus thermoleovorans ?
-
?
additional information enzyme CaesCCR11 has a preference for C4 substrates. Activity toward 4-nitrophenyl esters with longer chain lengths is only slightly detected, suggesting that CaesCCR11 is an esterase Geobacillus thermoleovorans CCR11 ?
-
?

Subunits

Subunits Comment Organism
? x * 27300, about, sequence calculation Geobacillus thermoleovorans

Synonyms

Synonyms Comment Organism
CaesCCR11
-
Geobacillus thermoleovorans
More cf. EC 3.1.1.3 Geobacillus thermoleovorans

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
50
-
recombinant enzyme Geobacillus thermoleovorans

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
30 80 purified recombinant enzyme, at 30°C and 40°C, lipolytic activity is conserved after 30 and 20 min, respectively. When the enzyme is preincubated around the physiological temperature at 50-60°C for 30 min, lipolytic activity is increased by 80%, it is diminished by 50% at 70°C and completely lost at 80°C after 10 min Geobacillus thermoleovorans

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5 8 broad optimum, recombinant enzyme Geobacillus thermoleovorans

pH Stability

pH Stability pH Stability Maximum Comment Organism
6 8 purified recombinant enzyme, the activity is retained. Lipolytic activity is increased to 150% after a 28 h incubation at pH 9.0 and pH 10.0, while activity is lost by 50% at pH 5.0 and pH 11.0 Geobacillus thermoleovorans

General Information

General Information Comment Organism
evolution CaesCCR11 as a member of family XV of lipolytic enzymes, it has a canonical alpha/beta hydrolase fold composed of 7 beta-strands and 6 alpha-helices, the alpha/beta architecture of the cap domain, the GLSTG pentapeptide, and the formation of distinctive salt bridges Geobacillus thermoleovorans
additional information three-dimensional structure modeling of enzyme CaesCCR11 using the Bacillus sp. monoacyl glycerol lipase bMGL H-257 structure as template (PBD ID 3RM3) Geobacillus thermoleovorans