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Literature summary for 3.2.1.39 extracted from

  • Pesentseva, M.S.; Kusaykin, M.I.; Anastyuk, S.D.; Sova, V.V.; Zvyagintseva, T.N.
    Catalytic properties and mode of action of endo-(1-->3)-beta-D-glucanase and beta-D-glucosidase from the marine mollusk Littorina kurila (2008), Carbohydr. Res., 343, 2393-2400.
    View publication on PubMed
Search for more literature for 3.2.1.39

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
32000
-
 gel filtration Littorina kurila
40000
-
 1 * 40000, SDS-PAGE Littorina kurila

Organism

Organism UniProt Comment Textmining
Littorina kurila
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Littorina kurila

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
 Littorina kurila
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.285
-
-
 Littorina kurila

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
laminaran + H2O
-
 Littorina kurila ?
-
 ?
additional information narrow substrate specificity, hydrolyzes only the (1-3)-beta-D-glucosidic bonds in the mixed (1-3),(1-6)- and (1-3),(1-4)-beta-D-glucans down to glucose and glucooligosaccharides. Enzyme acts with retention of the anomeric configuration and additionally catalyzes transglycosylation reactions Littorina kurila ?
-
 ?
periodate-oxidized laminaran + H2O 95% of the rate with laminaran Littorina kurila ?
-
 ?
translam + H2O 86% of the rate with laminaran Littorina kurila ?
-
 ?

Subunits

Subunits Comment Organism
monomer 1 * 40000, SDS-PAGE Littorina kurila

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.4
-
-
 Littorina kurila

pH Range

pH Minimum pH Maximum Comment Organism
4.5 7.5
-
 Littorina kurila