Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Sulaiman, S.; You, D.J.; Kanaya, E.; Koga, Y.; Kanaya, S.
    Crystal structure and thermodynamic and kinetic stability of metagenome-derived LC-cutinase (2014), Biochemistry, 53, 1858-1869.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.1.74 recombinant expression of extracellular wild-type and mutant enzymes in Escherichia coli uncultured bacterium

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.1.1.74 purified recombinant C275A/C292A mutant enzyme, sitting drop vapor diffusion method, from 20% w/v PEG 3350 and 0.2 M sodium thiocyanate, 20°C, 2 weeks, X-ray diffraction structure determination and analysis at 1.5 A resolution uncultured bacterium

Protein Variants

EC Number Protein Variants Comment Organism
3.1.1.74 C275A/C292A site-directed mutagenesis, the mutant lacks the disulfide bond formed by Cys275 and Cys292, resulting in increased instability uncultured bacterium

General Stability

EC Number General Stability Organism
3.1.1.74 the disulfide bond formed by Cys275 and Cys292 contributes not only to the thermodynamic stability but also to the kinetic stability of LC-cutinase uncultured bacterium

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.1.74 guanidine hydrochloride GdnHCl-induced unfolding of LC-cutinase is analyzed at pH 8.0 by circular dichroism spectroscopy, overview uncultured bacterium

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.1.74 0.18
-
 4-nitrophenyl butyrate pH 8.0, 50°C, recombinant mutant C275A/C292A, absence of 1% PEG uncultured bacterium
3.1.1.74 0.19
-
 4-nitrophenyl butyrate pH 8.0, 70°C, recombinant mutant C275A/C292A, absence of 1% PEG uncultured bacterium
3.1.1.74 0.21
-
 4-nitrophenyl butyrate pH 8.0, 50°C, recombinant wild-type enzyme, absence of 1% PEG uncultured bacterium
3.1.1.74 0.22
-
 4-nitrophenyl butyrate pH 8.0, 30°C, recombinant wild-type enzyme, absence of 1% PEG uncultured bacterium
3.1.1.74 0.24
-
 4-nitrophenyl butyrate pH 8.0, 70°C, recombinant wild-type enzyme, absence of 1% PEG uncultured bacterium
3.1.1.74 0.25
-
 4-nitrophenyl butyrate pH 8.0, 30°C, recombinant mutant C275A/C292A, absence of 1% PEG uncultured bacterium
3.1.1.74 0.25
-
 4-nitrophenyl butyrate pH 8.0, 70°C, recombinant wild-type enzyme, absence of 1% PEG uncultured bacterium
3.1.1.74 0.27
-
 4-nitrophenyl butyrate pH 8.0, 30°C, recombinant wild-type enzyme, presence of 1% PEG uncultured bacterium
3.1.1.74 0.27
-
 4-nitrophenyl butyrate pH 8.0, 50°C, recombinant wild-type enzyme, presence of 1% PEG uncultured bacterium

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.1.1.74 extracellular
-
 uncultured bacterium
-
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.1.1.74 additional information uncultured bacterium the enzyme shows polyethylene terephthalate-degrading activity ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.74 uncultured bacterium
-
 metagenome-derived LC-cutinase
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.1.74 recombinant extracellular wild-type and mutant enzymes without a putative N-terminal signal peptide (Met1-Ala34) and Gln35 from Escherichia coli uncultured bacterium

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.74 4-nitrophenyl butyrate + H2O
-
 uncultured bacterium 4-nitrophenol + butyrate
-
 ?
3.1.1.74 additional information the enzyme shows polyethylene terephthalate-degrading activity uncultured bacterium ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.1.1.74 LC-cutinase
-
 uncultured bacterium

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.1.74 50
-
-
 uncultured bacterium

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.1.1.74 30 70 activity range uncultured bacterium

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.1.1.74 additional information
-
 thermal denaturation-induced unfolding of LC-cutinase is analyzed at pH 8.0 by circular dichroism spectroscopy, kinetics of transition of the thermal denaturation, overview. The disulfide bond formed by Cys275 and Cys292 contributes not only to the thermodynamic stability but also to the kinetic stability of LC-cutinase uncultured bacterium

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.1.1.74 49
-
 4-nitrophenyl butyrate pH 8.0, 70°C, recombinant mutant C275A/C292A, absence of 1% PEG uncultured bacterium
3.1.1.74 196
-
 4-nitrophenyl butyrate pH 8.0, 50°C, recombinant mutant C275A/C292A, absence of 1% PEG uncultured bacterium
3.1.1.74 213
-
 4-nitrophenyl butyrate pH 8.0, 70°C, recombinant wild-type enzyme, absence of 1% PEG uncultured bacterium
3.1.1.74 232
-
 4-nitrophenyl butyrate pH 8.0, 30°C, recombinant wild-type enzyme, absence of 1% PEG uncultured bacterium
3.1.1.74 278
-
 4-nitrophenyl butyrate pH 8.0, 30°C, recombinant wild-type enzyme, presence of 1% PEG uncultured bacterium
3.1.1.74 318
-
 4-nitrophenyl butyrate pH 8.0, 70°C, recombinant wild-type enzyme, absence of 1% PEG uncultured bacterium
3.1.1.74 342
-
 4-nitrophenyl butyrate pH 8.0, 30°C, recombinant mutant C275A/C292A, absence of 1% PEG uncultured bacterium
3.1.1.74 343
-
 4-nitrophenyl butyrate pH 8.0, 50°C, recombinant wild-type enzyme, absence of 1% PEG uncultured bacterium
3.1.1.74 359
-
 4-nitrophenyl butyrate pH 8.0, 50°C, recombinant wild-type enzyme, presence of 1% PEG uncultured bacterium

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.1.74 8
-
 assay at uncultured bacterium

General Information

EC Number General Information Comment Organism
3.1.1.74 additional information residues Ser165, Asp210, and His242 form the catalytic triad. The disulfide bond formed by Cys275 and Cys292 contributes not only to the thermodynamic stability but also to the kinetic stability of LC-cutinase uncultured bacterium

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
3.1.1.74 258
-
 4-nitrophenyl butyrate pH 8.0, 70°C, recombinant mutant C275A/C292A, absence of 1% PEG uncultured bacterium
3.1.1.74 888
-
 4-nitrophenyl butyrate pH 8.0, 70°C, recombinant wild-type enzyme, absence of 1% PEG uncultured bacterium
3.1.1.74 1046
-
 4-nitrophenyl butyrate pH 8.0, 30°C, recombinant wild-type enzyme, presence of 1% PEG uncultured bacterium
3.1.1.74 1050
-
 4-nitrophenyl butyrate pH 8.0, 30°C, recombinant wild-type enzyme, absence of 1% PEG uncultured bacterium
3.1.1.74 1090
-
 4-nitrophenyl butyrate pH 8.0, 50°C, recombinant mutant C275A/C292A, absence of 1% PEG uncultured bacterium
3.1.1.74 1295
-
 4-nitrophenyl butyrate pH 8.0, 70°C, recombinant wild-type enzyme, absence of 1% PEG uncultured bacterium
3.1.1.74 1311
-
 4-nitrophenyl butyrate pH 8.0, 50°C, recombinant wild-type enzyme, presence of 1% PEG uncultured bacterium
3.1.1.74 1370
-
 4-nitrophenyl butyrate pH 8.0, 30°C, recombinant mutant C275A/C292A, absence of 1% PEG uncultured bacterium
3.1.1.74 1630
-
 4-nitrophenyl butyrate pH 8.0, 50°C, recombinant wild-type enzyme, absence of 1% PEG uncultured bacterium