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Literature summary extracted from

  • Zhu, X.; Larsen, N.A.; Basran, A.; Bruce, N.C.; Wilson, I.A.
    Observation of an arsenic adduct in an acetyl esterase crystal structure (2003), J. Biol. Chem., 278, 2008-2014.
    View publication on PubMed

Application

EC Number Application Comment Organism
3.1.1.6 analysis development of a heroin biosensor with high sensitivity Rhodococcus sp.

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.1.6 expression of the N-terminally His-tagged enzyme in Escherichia coli BL21(DE3) Rhodococcus sp.

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.1.1.6 purified selenomethionine enzyme, 6-7 mg/ml, pure or complexed with the inhibitor dimethylarsinic acid, crystal growth in 1.8 M ammonium sulfate, 0.1 M NaCl, 0.1 M cacodylate, pH 6.5, for crystallization of native methionine enzyme 1.7 M ammonium sulfate, 0.1 M NaCl, 0.1 M BES, pH 6.4, is used, X-ray structure determination and analysis at 1.3 A and 1.45 A resolution Rhodococcus sp.

Protein Variants

EC Number Protein Variants Comment Organism
3.1.1.6 additional information construction of selenomethionine enzyme by growth of the recombinant methionine auxotroph Escherichia coli strain B834-(DE3) expressing the enzyme in minimal medium containing selenomethionine Rhodococcus sp.

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.1.6 dimethylarsinic acid binding mechanism Rhodococcus sp.

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.1.6 0.07
-
 phenyl acetate recombinant enzyme, pH 6.4 Rhodococcus sp.
3.1.1.6 0.5
-
 6-acetylmorphine recombinant enzyme, pH 8.0 Rhodococcus sp.

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.6 Rhodococcus sp.
-
-
-
3.1.1.6 Rhodococcus sp. H1
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.1.6 recombinant from Escherichia coli as N-terminally His-tagged selenomethionine or methionine enzyme, removal of the His-tag Rhodococcus sp.

Reaction

EC Number Reaction Comment Organism Reaction ID
3.1.1.6 an acetic ester + H2O = an alcohol + acetate active site serine, active site structure, reaction and ligand binding mechanism Rhodococcus sp.
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.6 3,6-diacetylmorphine + H2O i.e. heroin, rapid spontaneous hydrolysis of the instable 3-acetyl group Rhodococcus sp. morphine + acetate
-
 ?
3.1.1.6 3,6-diacetylmorphine + H2O i.e. heroin, rapid spontaneous hydrolysis of the instable 3-acetyl group Rhodococcus sp. H1 morphine + acetate
-
 ?
3.1.1.6 6-acetylmorphine + H2O substrate specificity Rhodococcus sp. morphine + acetate
-
 ?
3.1.1.6 6-acetylmorphine + H2O substrate specificity Rhodococcus sp. H1 morphine + acetate
-
 ?
3.1.1.6 phenyl acetate + H2O
-
 Rhodococcus sp. phenol + acetate
-
 ?
3.1.1.6 phenyl acetate + H2O
-
 Rhodococcus sp. H1 phenol + acetate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.1.1.6 HerE
-
 Rhodococcus sp.

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.1.1.6 3
-
 phenyl acetate recombinant enzyme, pH 6.4 Rhodococcus sp.
3.1.1.6 12.6
-
 6-acetylmorphine recombinant enzyme, pH 8.0 Rhodococcus sp.

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.1.1.6 12
-
 dimethylarsinic acid recombinant enzyme, pH 6.4 Rhodococcus sp.