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Literature summary for 3.1.1.6 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
Search for more literature for 3.1.1.6

Application

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

Cloned(Commentary)

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

Crystallization (Commentary)

Crystallization (Comment) Organism
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

Protein Variants Comment Organism
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

Inhibitors Comment Organism Structure
dimethylarsinic acid binding mechanism Rhodococcus sp.

KM Value [mM]

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

Organism

Organism UniProt Comment Textmining
Rhodococcus sp.
-
-
-
Rhodococcus sp. H1
-
-
-

Purification (Commentary)

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

Reaction

Reaction Comment Organism Reaction ID
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)

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

Synonyms

Synonyms Comment Organism
HerE
-
 Rhodococcus sp.

Turnover Number [1/s]

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

Ki Value [mM]

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