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Literature summary for 3.2.1.14 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
Search for more literature for 3.2.1.14

Cloned(Commentary)

Cloned (Comment) Organism
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

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

Inhibitors

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

KM Value [mM]

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

Metals/Ions

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

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Trichoderma viride
-
-
-
Trichoderma viride MECH
-
-
-

Purification (Commentary)

Purification (Comment) Organism
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)

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

Subunits

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

Synonyms

Synonyms Comment Organism
Ech42
-
 Trichoderma viride
endochitinase
-
 Trichoderma viride

Temperature Optimum [°C]

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

Temperature Range [°C]

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

Temperature Stability [°C]

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

pH Optimum

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

pH Range

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

pH Stability

pH Stability pH Stability Maximum Comment Organism
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