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Literature summary for 3.2.1.39 extracted from

  • Zakharenko, A.M.; Kusaykin, M.I.; Kovalchuk, S.N.; Anastyuk, S.D.; Ly, B.M.; Sova, V.V.; Rasskazov, V.A.; Zvyagintseva, T.N.
    Enzymatic and molecular characterization of an endo-1,3-beta-D-glucanase from the crystalline styles of the mussel Perna viridis (2011), Carbohydr. Res., 346, 243-252.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
Laminarin KM value 0.3 mg/ml, pH 6.2, 37°C Perna viridis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
33000
-
x * 33000, SDS-PAGE Perna viridis

Organism

Organism UniProt Comment Textmining
Perna viridis
-
member of glycosyl hydrolase family 16
-

Purification (Commentary)

Purification (Comment) Organism
-
Perna viridis

Source Tissue

Source Tissue Comment Organism Textmining
crystalline style
-
Perna viridis
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
laminarin + H2O
-
Perna viridis D-glucose + laminarioligosaccharides if the degree of cleavage of laminarin under exhaustive hydrolysis reaches 74%, the major products are glucose and di-, tri-, and tetrasaccharides ?
additional information poor substrates: yeast glucan, pachyman, amylopectin, carboxymethy cellulose, and pustulan Perna viridis ?
-
?
periodate-oxidized laminarin + H2O 100% of the activity with laminarin Perna viridis ?
-
?
translam + H2O 32.1% of the activity with laminarin Perna viridis ?
-
?

Subunits

Subunits Comment Organism
? x * 33000, SDS-PAGE Perna viridis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
45
-
-
Perna viridis

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
45
-
half-life 180 min Perna viridis
50
-
half-life 20 min Perna viridis

pH Range

pH Minimum pH Maximum Comment Organism
4 6.5
-
Perna viridis