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Literature summary for 3.2.1.11 extracted from

  • Ko, J.A.; Nam, S.H.; Kim, D.; Lee, J.H.; Kim, Y.M.
    Identification of catalytic amino acid residues by chemical modification in dextranase (2016), J. Microbiol. Biotechnol., 26, 837-845.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
D1252N about 40% of wild-type activtiy Paenibacillus sp.
D189N complete loss of activity Paenibacillus sp.
D340N complete loss of activity Paenibacillus sp.
E412Q complete loss of activity Paenibacillus sp.

Organism

Organism UniProt Comment Textmining
Paenibacillus sp.
-
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.3
-
mutant D1252N, pH 5.5, 35°C Paenibacillus sp.
11.9
-
truncated enzyme bearing only the A domain region, pH 5.5, 35°C Paenibacillus sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dextran + H2O
-
Paenibacillus sp. isomaltotetraose plus small amounts of cycloisomaltooligosaccharides with a degree of polymerization of 7–14 ?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
35
-
-
Paenibacillus sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.5
-
-
Paenibacillus sp.