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Literature summary for 3.2.1.132 extracted from

  • Honda, Y.; Fukamizo, T.; Okajima, T.; Goto, S.; Boucher, I.; Brzezinski, R.
    Thermal unfolding of chitosanase from Streptomyces sp. N174: role of tryptophan residues in the protein structure stabilization (1999), Biochim. Biophys. Acta, 1429, 365-376.
    View publication on PubMed
Search for more literature for 3.2.1.132

Cloned(Commentary)

Cloned (Comment) Organism
expression in Streptomyces lividans TK24 Streptomyces sp.

Protein Variants

Protein Variants Comment Organism
W101F decreased midpoint temperature by about 7°C Streptomyces sp.
W227F decreased midpoint temperature by about 7°C Streptomyces sp.
W28F decreased midpoint temperature by about 7°C Streptomyces sp.
W28F/W101F decreased midpoint temperature by about 11°C Streptomyces sp.

Organism

Organism UniProt Comment Textmining
Streptomyces sp. P33665 N174
-

Purification (Commentary)

Purification (Comment) Organism
recombinant protein Streptomyces sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
30% N-acetylated chitosan + H2O
-
 Streptomyces sp. ?
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
38.4
-
 30% N-acetylated chitosan 40°C, pH 5.5, W227F Streptomyces sp.
42.1
-
 30% N-acetylated chitosan 40°C, pH 5.5, W28F/W101F Streptomyces sp.
45.1
-
 30% N-acetylated chitosan 40°C, pH 5.5, W101F Streptomyces sp.
50.1
-
 30% N-acetylated chitosan 40°C, pH 5.5, W28F Streptomyces sp.
71.4
-
 30% N-acetylated chitosan 40°C, pH 5.5, wild-type Streptomyces sp.