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Literature summary extracted from

  • Yu, P.; Xu, M.
    Enhancing the enzymatic activity of the endochitinase by the directed evolution and its enzymatic property evaluation (2012), Process Biochem., 47, 1089-1094.
No PubMed abstract available

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.14 DNA and amino acid sequence determination and analysis, expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) Trichoderma viride

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.14 Y185F/S226P site-directed mutagenesis Trichoderma viride

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.14 Co2+ inhibits at 13% at 0.5 mM, 14% at 2 mM Trichoderma viride
3.2.1.14 Cu2+ inhibits at 12% at 0.5 mM, 25% at 2 mM Trichoderma viride
3.2.1.14 Zn2+ inhibits at 18% at 0.5 mM, 21% at 2 mM Trichoderma viride

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.14 0.25
-
 4-nitrophenyl N-acetyl-beta-D-glucosamine mutant enzyme, pH 7.0, 37°C Trichoderma viride
3.2.1.14 0.54
-
 4-nitrophenyl N-acetyl-beta-D-glucosamine wild-type enzyme, pH 7.0, 37°C Trichoderma viride

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.2.1.14 Ba2+ activates at 0.5-2 mM Trichoderma viride
3.2.1.14 Ca2+ activates slightly at 2 mM Trichoderma viride
3.2.1.14 Mg2+ activates at 0.5-2 mM Trichoderma viride
3.2.1.14 Mn2+ activates at 0.5-2 mM Trichoderma viride
3.2.1.14 additional information poor effects by Na+ and K+ at 0.5-2 mM Trichoderma viride

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.14 46000
-
 x * 46000, SDS-PAGE Trichoderma viride

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.14 Trichoderma viride
-
-
-
3.2.1.14 Trichoderma viride MECH
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.14 mutant enzyme 9.7fold from Escherichia coli by ammonium sulfate precipitation, anion exchange chromatography, concentration by PEG 20000, and gel filtration Trichoderma viride

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.14 4-nitrophenyl N-acetyl-beta-D-glucosamine + H2O
-
 Trichoderma viride 4-nitrophenol + N-acetyl-beta-D-glucosamine
-
 ?
3.2.1.14 4-nitrophenyl N-acetyl-beta-D-glucosamine + H2O
-
 Trichoderma viride MECH 4-nitrophenol + N-acetyl-beta-D-glucosamine
-
 ?

Subunits

EC Number Subunits Comment Organism
3.2.1.14 ? x * 46000, SDS-PAGE Trichoderma viride

Synonyms

EC Number Synonyms Comment Organism
3.2.1.14 Ech42
-
 Trichoderma viride
3.2.1.14 endochitinase
-
 Trichoderma viride

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.14 50
-
 wild-type and mutant enzymes Trichoderma viride

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.2.1.14 20 70 activity range, wild-type and mutant enzymes, profile overview Trichoderma viride

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.14 20 50 pH 7.0, 10 min, purified mutant enzyme, stable at, over 90% activity within this range Trichoderma viride
3.2.1.14 20 70 pH 7.0, 10 min, purified wild-type enzyme, stable at, over 90% activity within this range Trichoderma viride
3.2.1.14 80
-
 pH 7.0, 10 min, purified mutant enzyme, loss of 50% activity Trichoderma viride

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.14 7.5
-
 wild-type and mutant enzymes Trichoderma viride

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.2.1.14 3 8 activity range, wild-type and mutant enzymes, profile overview Trichoderma viride

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.2.1.14 4 8 37°C, the purified wild-type enzyme shows over 80% activity within this range, the purified mutant shows over 90% activity Trichoderma viride