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Literature summary extracted from

  • Sanishvili, R.; Yakunin, A.F.; Laskowski, R.A.; Skarina, T.; Evdokimova, E.; Doherty-Kirby, A.; Lajoie, G.A.; Thornton, J.M.; Arrowsmith, C.H.; Savchenko, A.; Joachimiak, A.; Edwards, A.M.
    Integrating structure, bioinformatics, and enzymology to discover function. BioH, a new carboxylesterase from Escherichia coli (2003), J. Biol. Chem., 278, 26039-26045.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.1.1
-
 Escherichia coli
3.1.1.1 expression of the selenomethionine enriched enzyme in Escherichia coli methionine auxotroph strain B834 (DE3) in supplemented M9 medium Escherichia coli
3.1.1.85 expressed in the Escherichia coli auxotroph strain B834 (DE3) Escherichia coli

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.1.1.1
-
 Escherichia coli
3.1.1.1 purified recombinant enzyme, by hanging drop vapour diffusion method, 0.002 ml of each, protein solution and precipitant solution, equilibration against reservoir solution containing 1.2 M sodium citrate trihydrate and 0.1 M Tris-HCl, pH 8.0, 21°C, 2-5 days, X-ray diffraction structure determination at 1.7 A resolution, structure analysis Escherichia coli
3.1.1.85 hanging drop vapor diffusion method, using 1.2 M sodium citrate trihydrate and 0.1 M Tris-HCl (pH 8.0), at 21°C Escherichia coli

General Stability

EC Number General Stability Organism
3.1.1.1 stable Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.1.1 Phenylmethylsulfonylfluoride
-
 Escherichia coli
3.1.1.85 phenylmethylsulfonyl fluoride 10.5% residual activity after 10 min of incubation with 2 mM Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.1.1 0.25
-
 4-nitrophenyl caproate pH 7.5, 37°C Escherichia coli
3.1.1.1 0.25
-
 p-nitrophenyl caproate +/- 0.02 Escherichia coli
3.1.1.1 0.29
-
 4-nitrophenyl acetate pH 7.5, 37°C Escherichia coli
3.1.1.1 0.29
-
 p-nitrophenyl acetate +/- 0.04 Escherichia coli
3.1.1.1 0.33
-
 4-nitrophenyl butyrate pH 7.5, 37°C Escherichia coli
3.1.1.1 0.33
-
 p-nitrophenyl butyrate +/- 0.06 Escherichia coli
3.1.1.1 0.35
-
 4-nitrophenyl propionate pH 7.5, 37°C Escherichia coli
3.1.1.1 0.35
-
 p-nitrophenyl propionate +/- 0.08 Escherichia coli
3.1.1.1 0.6
-
 4-nitrophenyl laurate pH 7.5, 37°C Escherichia coli
3.1.1.1 0.6
-
 p-nitrophenyl laurate +/- 0.13 Escherichia coli
3.1.1.85 0.25
-
 4-nitrophenyl caproate in 50 mM HEPES-K (pH 7.5) buffer, at 37°C Escherichia coli
3.1.1.85 0.29
-
 4-nitrophenyl acetate in 50 mM HEPES-K (pH 7.5) buffer, at 37°C Escherichia coli
3.1.1.85 0.33
-
 4-nitrophenyl butyrate in 50 mM HEPES-K (pH 7.5) buffer, at 37°C Escherichia coli
3.1.1.85 0.35
-
 4-nitrophenyl propionate in 50 mM HEPES-K (pH 7.5) buffer, at 37°C Escherichia coli
3.1.1.85 0.6
-
 4-nitrophenyl laurate in 50 mM HEPES-K (pH 7.5) buffer, at 37°C Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.1.1.1 29152
-
 x * 29152, mass spectrometry Escherichia coli

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 the enzyme BioH is involved in biotin biosynthesis ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.1 Escherichia coli
-
 enzyme BioH, selenomethionine enriched protein, contains 2 Gly-Xaa-Ser-Xaa-Gly motifs
-
3.1.1.1 Escherichia coli P13001
-
-
3.1.1.85 Escherichia coli P13001
-
-
3.1.1.85 Escherichia coli DH5-alpha P13001
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.1.85 Ni-NTA column chromatography Escherichia coli

Reaction

EC Number Reaction Comment Organism Reaction ID
3.1.1.1 a carboxylic ester + H2O = an alcohol + a carboxylate active site structure, catalytic triad consists of residues Ser82, His235, and Asp207 Escherichia coli
a

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.1.1.1 0.19
-
 +/- 0.02, palmitoyl-CoA Escherichia coli
3.1.1.1 3.17
-
 +/- 0.34, p-nitrophenyl laurate Escherichia coli
3.1.1.1 8.4
-
 +/- 0.27, p-nitrophenyl caproate Escherichia coli
3.1.1.1 12.7
-
 +/- 1.5, p-nitrophenyl butyrate Escherichia coli
3.1.1.1 27.5
-
 +/- 2.5, p-nitrophenyl propionate Escherichia coli
3.1.1.1 38.9
-
 +/- 3.6, p-nitrophenyl acetate Escherichia coli

Storage Stability

EC Number Storage Stability Organism
3.1.1.1 4°C, 5% glycerol, 0.5 M NaCl, no loss in activity after several months Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.1 4-nitrophenyl acetate + H2O best substrate Escherichia coli 4-nitrophenol + acetate
-
 ?
3.1.1.1 4-nitrophenyl butyrate + H2O
-
 Escherichia coli 4-nitrophenol + butyrate
-
 ?
3.1.1.1 4-nitrophenyl caproate + H2O
-
 Escherichia coli 4-nitrophenol + caproate
-
 ?
3.1.1.1 4-nitrophenyl caproate + H2O
-
 Escherichia coli DH5-alpha 4-nitrophenol + caproate
-
 ?
3.1.1.1 4-nitrophenyl laurate + H2O
-
 Escherichia coli 4-nitrophenol + laurate
-
 ?
3.1.1.1 4-nitrophenyl laurate + H2O
-
 Escherichia coli DH5-alpha 4-nitrophenol + laurate
-
 ?
3.1.1.1 4-nitrophenyl propionate + H2O
-
 Escherichia coli 4-nitrophenol + propionate
-
 ?
3.1.1.1 additional information enzyme shows low thioesterase activity, it cannot use free pimelic acid for pimeloyl-CoA synthesis, enzyme shows a broad substrate specificity with a preference for short chain substrates Escherichia coli ?
-
 ?
3.1.1.1 additional information the enzyme BioH is involved in biotin biosynthesis Escherichia coli ?
-
 ?
3.1.1.1 p-nitrophenyl acetate + H2O
-
 Escherichia coli p-nitrophenol + acetate
-
 ?
3.1.1.1 p-nitrophenyl acetate + H2O
-
 Escherichia coli DH5-alpha p-nitrophenol + acetate
-
 ?
3.1.1.1 p-nitrophenyl butyrate
-
 Escherichia coli p-nitrophenol + butyrate
-
 ?
3.1.1.1 p-nitrophenyl butyrate
-
 Escherichia coli DH5-alpha p-nitrophenol + butyrate
-
 ?
3.1.1.1 p-nitrophenyl caprate
-
 Escherichia coli p-nitrophenol + caprate
-
 ?
3.1.1.1 p-nitrophenyl caprate
-
 Escherichia coli DH5-alpha p-nitrophenol + caprate
-
 ?
3.1.1.1 p-nitrophenyl caproate
-
 Escherichia coli p-nitrophenol + caproate
-
 ?
3.1.1.1 p-nitrophenyl laurate
-
 Escherichia coli p-nitrophenol + laurate
-
 ?
3.1.1.1 p-nitrophenyl palmitate + H2O
-
 Escherichia coli p-nitrophenol + palmitate
-
 ?
3.1.1.1 p-nitrophenyl propionate
-
 Escherichia coli p-nitrophenol + propionate
-
 ?
3.1.1.1 p-nitrophenyl stearate
-
 Escherichia coli p-nitrophenol + stearate
-
 ?
3.1.1.1 palmitoyl-CoA
-
 Escherichia coli CoA + palmitate
-
 ?
3.1.1.85 4-nitrophenyl acetate + H2O highest carboxylesterase activity Escherichia coli ?
-
 ?
3.1.1.85 4-nitrophenyl butyrate + H2O
-
 Escherichia coli ?
-
 ?
3.1.1.85 4-nitrophenyl caprate + H2O
-
 Escherichia coli ?
-
 ?
3.1.1.85 4-nitrophenyl caproate + H2O
-
 Escherichia coli ?
-
 ?
3.1.1.85 4-nitrophenyl laurate + H2O
-
 Escherichia coli ?
-
 ?
3.1.1.85 4-nitrophenyl palmitate + H2O
-
 Escherichia coli ?
-
 ?
3.1.1.85 4-nitrophenyl propionate + H2O
-
 Escherichia coli ?
-
 ?
3.1.1.85 4-nitrophenyl stearate + H2O very low carboxylesterase activity Escherichia coli ?
-
 ?
3.1.1.85 additional information purified BioH shows low enzymatic activities for thioesterase (using palmitoyl-CoA as a substrate), lipase (using olive oil as a substrate), and aminopeptidase (using leucine-4-anilide as a substrate) and shows no detectable enzymatic activity for phosphatase (using 4-nitrophenyl phosphate as a substrate), trypsin-like endopeptidase (using benzoyl-arginine-4-nitroanilide as a substrate), or bromoperoxidase (phenol red and monochlorodimedone as potential substrates) Escherichia coli ?
-
 ?
3.1.1.85 pimelyl-[acyl-carrier protein] methyl ester + H2O
-
 Escherichia coli pimelyl-[acyl-carrier protein] + methanol
-
 ?

Subunits

EC Number Subunits Comment Organism
3.1.1.1 ? x * 29152, mass spectrometry Escherichia coli
3.1.1.1 monomer gel filtration Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
3.1.1.85 BioH
-
 Escherichia coli

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.1.1.1 0.1
-
 palmitoyl-CoA
-
 Escherichia coli
3.1.1.1 1.5
-
 4-nitrophenyl laurate pH 7.5, 37°C Escherichia coli
3.1.1.1 1.5
-
 p-nitrophenyl laurate +/- 0.2 Escherichia coli
3.1.1.1 4
-
 4-nitrophenyl caproate pH 7.5, 37°C Escherichia coli
3.1.1.1 4
-
 p-nitrophenyl caproate +/- 0.1 Escherichia coli
3.1.1.1 6.1
-
 4-nitrophenyl butyrate pH 7.5, 37°C Escherichia coli
3.1.1.1 6.1
-
 p-nitrophenyl butyrate +/- 0.7 Escherichia coli
3.1.1.1 13.1
-
 4-nitrophenyl propionate pH 7.5, 37°C Escherichia coli
3.1.1.1 13.1
-
 p-nitrophenyl propionate +/- 1.2 Escherichia coli
3.1.1.1 18.5
-
 4-nitrophenyl acetate pH 7.5, 37°C Escherichia coli
3.1.1.1 18.5
-
 p-nitrophenyl acetate +/- 1.7 Escherichia coli
3.1.1.85 1.5
-
 4-nitrophenyl laurate in 50 mM HEPES-K (pH 7.5) buffer, at 37°C Escherichia coli
3.1.1.85 4
-
 4-nitrophenyl caproate in 50 mM HEPES-K (pH 7.5) buffer, at 37°C Escherichia coli
3.1.1.85 6.1
-
 4-nitrophenyl butyrate in 50 mM HEPES-K (pH 7.5) buffer, at 37°C Escherichia coli
3.1.1.85 13.1
-
 4-nitrophenyl propionate in 50 mM HEPES-K (pH 7.5) buffer, at 37°C Escherichia coli
3.1.1.85 18.5
-
 4-nitrophenyl acetate in 50 mM HEPES-K (pH 7.5) buffer, at 37°C Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.1.1 8 8.5
-
 Escherichia coli
3.1.1.85 8 8.5
-
 Escherichia coli

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.1.1.1 6 10
-
 Escherichia coli

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.1.1.1 0.15
-
 Phenylmethylsulfonylfluoride
-
 Escherichia coli

General Information

EC Number General Information Comment Organism
3.1.1.85 metabolism BioH is involved in biotin biosynthesis Escherichia coli

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
3.1.1.85 2.5
-
 4-nitrophenyl laurate in 50 mM HEPES-K (pH 7.5) buffer, at 37°C Escherichia coli
3.1.1.85 16
-
 4-nitrophenyl caproate in 50 mM HEPES-K (pH 7.5) buffer, at 37°C Escherichia coli
3.1.1.85 18.5
-
 4-nitrophenyl butyrate in 50 mM HEPES-K (pH 7.5) buffer, at 37°C Escherichia coli
3.1.1.85 37.4
-
 4-nitrophenyl propionate in 50 mM HEPES-K (pH 7.5) buffer, at 37°C Escherichia coli
3.1.1.85 63.8
-
 4-nitrophenyl acetate in 50 mM HEPES-K (pH 7.5) buffer, at 37°C Escherichia coli