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Literature summary extracted from

  • Kwon, M.A.; Kim, H.S.; Oh, J.Y.; Song, B.K.; Song, J.K.
    Gene cloning, expression, and characterization of a new carboxylesterase from Serratia sp. SES-01: comparison with Escherichia coli BioHe enzyme (2009), J. Microbiol. Biotechnol., 19, 147-154.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.1.1.1 Co2+ 10% activation of recombinant BioHs at 10 mM Serratia sp.
3.1.1.1 Co2+ 150% activation of recombinant BioHe at 5-10 mM Escherichia coli
3.1.1.1 Mn2+ 10% activation of recombinant BioHs at 10 mM Serratia sp.

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.1.1 gene bioHe, DNA and amino acid sequence determination and analysis, sequence compariosns, overview Escherichia coli
3.1.1.1 gene bioHs, cloned from the genomic DNA library, DNA and amino acid sequence determination and analysis, expression of the HIs-tagged enzyme in Escherichia coli strain JM109 Serratia sp.

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.1.1 1-butanol 62% inhibition of BioHe at 30% Escherichia coli
3.1.1.1 1-butanol 95% inhibition of BioHs at 30% Serratia sp.
3.1.1.1 acetone 15% inhibition of BioHe at 30% Escherichia coli
3.1.1.1 acetone 96% inhibition of BioHs at 30% Serratia sp.
3.1.1.1 acetonitrile 89% inhibition of BioHe at 30% Escherichia coli
3.1.1.1 acetonitrile 97% inhibition of BioHs at 30% Serratia sp.
3.1.1.1 Cu2+ 30% inhibition of recombinant BioHe at 5-10 mM Escherichia coli
3.1.1.1 DMSO 22% inhibition of BioHs at 30% Serratia sp.
3.1.1.1 ethanol 16% inhibition of BioHe at 30% Escherichia coli
3.1.1.1 ethanol 95% inhibition of BioHs at 30% Serratia sp.
3.1.1.1 Isopropanol 70% inhibition of BioHe at 30% Escherichia coli
3.1.1.1 Isopropanol 96% inhibition of BioHs at 30% Serratia sp.
3.1.1.1 methanol 7% inhibition of BioHe at 30% Escherichia coli
3.1.1.1 methanol 98% inhibition of BioHs at 30% Serratia sp.
3.1.1.1 additional information no inhibition by DMSO at 10-30% Escherichia coli
3.1.1.1 SDS 52% inhibition of recombinant BioHe at 0.2% Escherichia coli
3.1.1.1 SDS almost complete inhibition of recombinant BioHs at 0.2% Serratia sp.

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.1.1 additional information no effects by EDTA, and 0.2% to 5% Triton X-100, Tween 20, and Tween 80. BioHe is no metalloenzyme Escherichia coli
3.1.1.1 additional information no effects by EDTA, and 0.2% to 5% Triton X-100, Tween 20, and Tween 80. BioHs is no metalloenzyme Serratia sp.

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.1.1.1 28300
-
x * 28300, SDS-PAGE Serratia sp.

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.1.1.1 additional information Escherichia coli BioHe shows carboxylesterase activity with a preference for short chain fatty acid esters with acyl chain length of up to C6. BioHe BioH also shows low enzymatic activities for thioesterase, lipase, and aminopeptidase, but shows no detectable enzymatic activity for phosphatase, trypsin-like endopeptidase, or perhydrolase ?
-
?
3.1.1.1 additional information Serratia sp. BioHs shows carboxylesterase activity with a preference for short chain fatty acid esters with acyl chain length of up to C6. BioHs also displays a weak thioesterase activity. Can form a complex with CoA, and may be involved in the condensation of CoA and pimelic acid into pimeloyl-CoA, a precursor in biotin biosynthesis ?
-
?
3.1.1.1 additional information Serratia sp. SES-01 BioHs shows carboxylesterase activity with a preference for short chain fatty acid esters with acyl chain length of up to C6. BioHs also displays a weak thioesterase activity. Can form a complex with CoA, and may be involved in the condensation of CoA and pimelic acid into pimeloyl-CoA, a precursor in biotin biosynthesis ?
-
?

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.1 Escherichia coli
-
gene bioHe
-
3.1.1.1 Serratia sp. B0M0H6 gene bioHs
-
3.1.1.1 Serratia sp. SES-01 B0M0H6 gene bioHs
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.1.1 recombinant His-tagged BioHs from Escherichia coli strain JM109 by metal affinity chromatography Serratia sp.

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.1 4-nitrophenyl acetate + H2O
-
Escherichia coli 4-nitrophenol + acetate
-
?
3.1.1.1 4-nitrophenyl acetate + H2O
-
Serratia sp. 4-nitrophenol + acetate
-
?
3.1.1.1 4-nitrophenyl acetate + H2O
-
Serratia sp. SES-01 4-nitrophenol + acetate
-
?
3.1.1.1 4-nitrophenyl butyrate + H2O
-
Escherichia coli 4-nitrophenol + butyrate
-
?
3.1.1.1 4-nitrophenyl butyrate + H2O
-
Serratia sp. 4-nitrophenol + butyrate
-
?
3.1.1.1 4-nitrophenyl butyrate + H2O
-
Serratia sp. SES-01 4-nitrophenol + butyrate
-
?
3.1.1.1 additional information BioHe shows carboxylesterase activity with a preference for short chain fatty acid esters with acyl chain length of up to C6. BioHe BioH also shows low enzymatic activities for thioesterase, lipase, and aminopeptidase, but shows no detectable enzymatic activity for phosphatase, trypsin-like endopeptidase, or perhydrolase Escherichia coli ?
-
?
3.1.1.1 additional information BioHs shows carboxylesterase activity with a preference for short chain fatty acid esters with acyl chain length of up to C6. BioHs also displays a weak thioesterase activity. Can form a complex with CoA, and may be involved in the condensation of CoA and pimelic acid into pimeloyl-CoA, a precursor in biotin biosynthesis Serratia sp. ?
-
?
3.1.1.1 additional information BioHs shows carboxylesterase activity with a preference for short chain fatty acid esters with acyl chain length of up to C6. BioHs also displays a weak thioesterase activity. Can form a complex with CoA, and may be involved in the condensation of CoA and pimelic acid into pimeloyl-CoA, a precursor in biotin biosynthesis Serratia sp. SES-01 ?
-
?

Subunits

EC Number Subunits Comment Organism
3.1.1.1 ? x * 28300, SDS-PAGE Serratia sp.

Synonyms

EC Number Synonyms Comment Organism
3.1.1.1 BioHe
-
Escherichia coli
3.1.1.1 BioHs
-
Serratia sp.
3.1.1.1 More the enzyme belongs to the BioH enzyme family Escherichia coli

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.1.1 20 30
-
Escherichia coli
3.1.1.1 30 40
-
Serratia sp.

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.1.1.1 15 60 activity profile, overview Escherichia coli
3.1.1.1 15 60 activity profile, overview Serratia sp.

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.1.1.1 50
-
inactivation of BioHs after 30 min Serratia sp.
3.1.1.1 55
-
30 min, purified recombinant enzyme, more than 95% activity of BioHe remaining at 55°C Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.1.1 7 9 90% of maximal activity within this range Escherichia coli
3.1.1.1 7 9 90% of maximal activity within this range Serratia sp.

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.1.1.1 4 10 activity profile, inactive at pH 3.0, overview Escherichia coli
3.1.1.1 4 10 activity profile, inactive at pH 3.0, overview Serratia sp.

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.1.1.1 3
-
inactivation after 1 h Escherichia coli
3.1.1.1 3
-
inactivation after 1 h Serratia sp.
3.1.1.1 3.5
-
50% activity remaining after 1 h Escherichia coli
3.1.1.1 4.5
-
50% activity remaining after 1 h Serratia sp.
3.1.1.1 5 10 completely stable after 1 h Escherichia coli
3.1.1.1 5 10 completely stable after 1 h Serratia sp.

General Information

EC Number General Information Comment Organism
3.1.1.1 additional information BioHe also functions as a pimeloyl-CoA thioesterase/acyltransferase for the biotin synthetic pathway Escherichia coli
3.1.1.1 additional information BioHs also functions as a pimeloyl-CoA thioesterase/acyltransferase for the biotin synthetic pathway Serratia sp.