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Literature summary for 3.1.1.45 extracted from

  • Kim, H.K.; Liu, J.W.; Carr, P.D.; Ollis, D.L.
    Following directed evolution with crystallography: structural changes observed in changing the substrate specificity of dienelactone hydrolase (2005), Acta Crystallogr. Sect. D, 61, 920-931.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
-
Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging drop vapor diffusion method Escherichia coli

Protein Variants

Protein Variants Comment Organism
C123S 100% activity towards alpha-naphthyl acetate compared with the wild type enzyme Escherichia coli
C123S/R206A 65% activity towards alpha-naphthyl acetate compared with the wild type enzyme Escherichia coli
E36A/C123S no activity activity towards alpha-naphthyl acetate Escherichia coli
E36D 104% activity towards alpha-naphthyl acetate compared with the wild type enzyme Escherichia coli
E36D/C123S 183% activity towards alpha-naphthyl acetate compared with the wild type enzyme Escherichia coli
E36D/C123S/A134S/S208G/A229V/K234R 256% activity towards alpha-naphthyl acetate compared with the wild type enzyme Escherichia coli
E36D/C123S/A134T/A229V 164% activity towards alpha-naphthyl acetate compared with the wild type enzyme Escherichia coli
E36D/C123S/A205D 217% activity towards alpha-naphthyl acetate compared with the wild type enzyme Escherichia coli
E36D/C123S/A205D/A229V 222% activity towards alpha-naphthyl acetate compared with the wild type enzyme Escherichia coli
E36D/C123S/A205D/A229V 224% activity towards alpha-naphthyl acetate compared with the wild type enzyme Escherichia coli
E36D/C123S/A205D/A229V 230% activity towards alpha-naphthyl acetate compared with the wild type enzyme Escherichia coli
E36D/C123S/A229V 187% activity towards alpha-naphthyl acetate compared with the wild type enzyme Escherichia coli
E36D/C123S/F173A no activity activity towards alpha-naphthyl acetate Escherichia coli
E36D/C123S/G211D/A229V 172% activity towards alpha-naphthyl acetate compared with the wild type enzyme Escherichia coli
E36D/C123S/G211D/K234N 205% activity towards alpha-naphthyl acetate compared with the wild type enzyme Escherichia coli
E36D/C123S/R206T/A229V 122% activity towards alpha-naphthyl acetate compared with the wild type enzyme Escherichia coli
E36D/R105H/C123S/G211D/K234N 233% activity towards alpha-naphthyl acetate compared with the wild type enzyme Escherichia coli
E36D/R45Q/C123S 172% activity towards alpha-naphthyl acetate compared with the wild type enzyme Escherichia coli
E36D/R45Q/C123S/A205D/A229V 148% activity towards alpha-naphthyl acetate compared with the wild type enzyme Escherichia coli
E36D/R81A/C123S/R206A 114% activity towards alpha-naphthyl acetate compared with the wild type enzyme Escherichia coli
E36N/C123S 140% activity towards alpha-naphthyl acetate compared with the wild type enzyme Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
phenylmethylsulfonyl fluoride PMSF, mimics the transition state of the reaction Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.007
-
p-nitrophenyl acetate E36D,C123S,A134S,S208G,A229V,K234R mutant enzyme, pH 7.0 Escherichia coli
0.008
-
p-nitrophenyl acetate E36D,C123S mutant enzyme, pH 7.0 Escherichia coli
0.008
-
p-nitrophenyl acetate E36D,R105H,C123S,G211D,K234N mutant enzyme, pH 7.0 Escherichia coli
0.02
-
Alpha-naphthyl acetate E36D,C123S,A134S,S208G,A229V,K234R mutant enzyme, pH 7.0 Escherichia coli
0.021
-
p-nitrophenyl acetate C123S mutant enzyme, pH 7.0 Escherichia coli
0.023
-
Alpha-naphthyl acetate E36D,C123S mutant enzyme, pH 7.0 Escherichia coli
0.032
-
Alpha-naphthyl acetate E36D,R105H,C123S,G211D,K234N mutant enzyme, pH 7.0 Escherichia coli
0.074
-
Alpha-naphthyl acetate C123S mutant enzyme, pH 7.0 Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4-carboxymethylene-but-2-ene-4-olide + H2O Escherichia coli third enzyme of the halocatechol branch of the beta-ketoadipate pathway, catalyses the hydrolysis of both, (E) and (Z) dienelactone to maleyl acetate (2E)-4-oxohex-2-enedioic acid
-
?
4-carboxymethylene-but-2-ene-4-olide + H2O Escherichia coli DH5-alpha third enzyme of the halocatechol branch of the beta-ketoadipate pathway, catalyses the hydrolysis of both, (E) and (Z) dienelactone to maleyl acetate (2E)-4-oxohex-2-enedioic acid
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
strain DH5alpha
-
Escherichia coli DH5-alpha
-
strain DH5alpha
-

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-carboxymethylene-but-2-ene-4-olide + H2O third enzyme of the halocatechol branch of the beta-ketoadipate pathway, catalyses the hydrolysis of both, (E) and (Z) dienelactone to maleyl acetate Escherichia coli (2E)-4-oxohex-2-enedioic acid
-
?
4-carboxymethylene-but-2-ene-4-olide + H2O third enzyme of the halocatechol branch of the beta-ketoadipate pathway, catalyses the hydrolysis of both, (E) and (Z) dienelactone to maleyl acetate Escherichia coli DH5-alpha (2E)-4-oxohex-2-enedioic acid
-
?
alpha-naphthyl acetate + H2O
-
Escherichia coli 1-naphthol + acetate
-
?
alpha-naphthyl acetate + H2O
-
Escherichia coli DH5-alpha 1-naphthol + acetate
-
?
p-nitrophenyl acetate + H2O
-
Escherichia coli p-nitrophenol + acetate
-
?
p-nitrophenyl acetate + H2O
-
Escherichia coli DH5-alpha p-nitrophenol + acetate
-
?

Synonyms

Synonyms Comment Organism
dienelactone hydrolase
-
Escherichia coli
DLH
-
Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.24
-
p-nitrophenyl acetate E36D,C123S mutant enzyme, pH 7.0 Escherichia coli
0.24
-
Alpha-naphthyl acetate E36D,C123S,A134S,S208G,A229V,K234R mutant enzyme, pH 7.0 Escherichia coli
1.6
-
Alpha-naphthyl acetate E36D,C123S mutant enzyme, pH 7.0 Escherichia coli
2.05
-
Alpha-naphthyl acetate E36D,R105H,C123S,G211D,K234N mutant enzyme, pH 7.0 Escherichia coli
2.9
-
p-nitrophenyl acetate C123S mutant enzyme, pH 7.0 Escherichia coli
63.4
-
Alpha-naphthyl acetate C123S mutant enzyme, pH 7.0 Escherichia coli
71.2
-
Alpha-naphthyl acetate E36D,C123S mutant enzyme, pH 7.0 Escherichia coli
86.2
-
Alpha-naphthyl acetate E36D,R105H,C123S,G211D,K234N mutant enzyme, pH 7.0 Escherichia coli
97.9
-
p-nitrophenyl acetate E36D,C123S mutant enzyme, pH 7.0 Escherichia coli
98.1
-
Alpha-naphthyl acetate E36D,C123S,A134S,S208G,A229V,K234R mutant enzyme, pH 7.0 Escherichia coli
107.7
-
p-nitrophenyl acetate C123S mutant enzyme, pH 7.0 Escherichia coli
120
-
Alpha-naphthyl acetate C123S mutant enzyme, pH 7.0 Escherichia coli
123
-
p-nitrophenyl acetate E36D,R105H,C123S,G211D,K234N mutant enzyme, pH 7.0 Escherichia coli
126.8
-
p-nitrophenyl acetate E36D,C123S,A134S,S208G,A229V,K234R mutant enzyme, pH 7.0 Escherichia coli
138
-
p-nitrophenyl acetate E36D,C123S,A134S,S208G,A229V,K234R mutant enzyme, pH 7.0 Escherichia coli