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Literature summary for 3.2.1.58 extracted from

  • Kumagai, Y.; Ojima, T.
    Isolation and characterization of two types of beta-1,3-glucanases from the common sea hare Aplysia kurodai (2010), Comp. Biochem. Physiol. B, 155, 138-144.
    View publication on PubMed
Search for more literature for 3.2.1.58

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information kinetics, overview Aplysia kurodai

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
33000
-
 x * 33000, SDS-PAGE Aplysia kurodai

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
laminarin + H2O Aplysia kurodai AkLam33 exhibits exolytic beta-1,3-hydrolytic activity releasing D-glucose, it is highly active with high activity toward smaller substrates such as laminaritetraose and laminaritriose, and hydrolyzes highly branched beta-1,3-glucans such as Eisenia bicyclis laminarin, but it is also active toward beta-1,3-glucans with a few beta-1,6-linked glucose branches such as Laminaria digitata laminarin ?
-
 ?
additional information Aplysia kurodai no direct degradation activity with laminaribiose as a sole substrate, but the enzyme is capable of degrading it via transglycosylation reaction with laminaritriose ?
-
 ?

Organism

Organism UniProt Comment Textmining
Aplysia kurodai
-
-
-

Purification (Commentary)

Purification (Comment) Organism
native enzyme 28fold by ammonium sulfate fractionation, and several steps of cation exchange chromatography Aplysia kurodai

Source Tissue

Source Tissue Comment Organism Textmining

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3 8 purified enzyme Aplysia kurodai

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
laminarin + H2O AkLam33 exhibits exolytic beta-1,3-hydrolytic activity releasing D-glucose, it is highly active with high activity toward smaller substrates such as laminaritetraose and laminaritriose, and hydrolyzes highly branched beta-1,3-glucans such as Eisenia bicyclis laminarin, but it is also active toward beta-1,3-glucans with a few beta-1,6-linked glucose branches such as Laminaria digitata laminarin Aplysia kurodai ?
-
 ?
laminaritetraose + H2O preferred substrate Aplysia kurodai ?
-
 ?
laminaritriose + H2O
-
 Aplysia kurodai ?
-
 ?
additional information no direct degradation activity with laminaribiose as a sole substrate, but the enzyme is capable of degrading it via transglycosylation reaction with laminaritriose Aplysia kurodai ?
-
 ?
additional information sAkLam33 substrate specificity amd mode of action, overview. The enzyme is inactive toward laminaribiose, starch, carboxymethylcellulose, agar, beta-1,4-mannan, beta-1,4-xylan, and alginic acid, and it is specific to beta-1,3-glucosyl linkages Aplysia kurodai ?
-
 ?

Subunits

Subunits Comment Organism
? x * 33000, SDS-PAGE Aplysia kurodai

Synonyms

Synonyms Comment Organism
AkLam33
-
 Aplysia kurodai

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
40
-
-
 Aplysia kurodai

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
45
-
 50% inactivation Aplysia kurodai

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.05
-
 Laminarin pH 6.0, 30°C Aplysia kurodai
4.79
-
 laminaritetraose pH 6.0, 30°C Aplysia kurodai

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.7
-
-
 Aplysia kurodai