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Literature summary 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

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.6 additional information
-
 additional information kinetics, overview Aplysia kurodai
3.2.1.39 additional information
-
 additional information kinetics Aplysia kurodai
3.2.1.58 additional information
-
 additional information kinetics, overview Aplysia kurodai

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.2.1.39 extracellular
-
 Aplysia kurodai
-
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.6 36000
-
 x * 36000, SDS-PAGE Aplysia kurodai
3.2.1.39 36000
-
 x * 36000, SDS-PAGE Aplysia kurodai
3.2.1.58 33000
-
 x * 33000, SDS-PAGE Aplysia kurodai

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.2.1.6 laminarin + H2O Aplysia kurodai AkLam36 exhibits exolytic beta-1,3-hydrolytic activity releasing D-glucose preferring beta-1,3-glucans with a few beta-1,6-linked glucose branches such as Laminaria digitata laminarin ?
-
 ?
3.2.1.6 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 ?
-
 ?
3.2.1.58 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 ?
-
 ?
3.2.1.58 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

EC Number Organism UniProt Comment Textmining
3.2.1.6 Aplysia kurodai
-
-
-
3.2.1.39 Aplysia kurodai
-
-
-
3.2.1.58 Aplysia kurodai
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.6 native enzyme 126fold by ammonium sulfate fractionation, several steps of cation exchange chromatography, and gel filtration Aplysia kurodai
3.2.1.39 native enzyme 126fold from digestive fluid by ammonium sulfate fractionation, three steps of cation exchange chromatography, ultrafiltration and gel filtration Aplysia kurodai
3.2.1.58 native enzyme 28fold by ammonium sulfate fractionation, and several steps of cation exchange chromatography Aplysia kurodai

Reaction

EC Number Reaction Comment Organism Reaction ID
3.2.1.39 laminariheptaose + 3 H2O = laminaritriose + 2 laminaribiose AkLam36 mode of action, overview Aplysia kurodai
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.2.1.39 digestive juice
-
 Aplysia kurodai
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.2.1.6 172
-
 purified enzyme Aplysia kurodai
3.2.1.39 172
-
 purified native enzyme Aplysia kurodai
3.2.1.58 3 8 purified enzyme Aplysia kurodai

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.6 laminarin + H2O AkLam36 exhibits exolytic beta-1,3-hydrolytic activity releasing D-glucose preferring beta-1,3-glucans with a few beta-1,6-linked glucose branches such as Laminaria digitata laminarin Aplysia kurodai ?
-
 ?
3.2.1.6 laminarin + H2O AkLam36 exhibits exolytic beta-1,3-hydrolytic activity with released D-glucose, preferring beta-1,3-glucans with a few beta-1,6-linked glucose branches such as Laminaria digitata laminarin, best substrate is barley beta-D-glucan Aplysia kurodai ?
-
 ?
3.2.1.6 laminaritetraose + H2O
-
 Aplysia kurodai ?
-
 ?
3.2.1.6 laminaritriose + H2O
-
 Aplysia kurodai ?
-
 ?
3.2.1.6 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 ?
-
 ?
3.2.1.6 additional information sAkLam36 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 ?
-
 ?
3.2.1.39 laminarin + H2O
-
 Aplysia kurodai laminaribiose + beta-D-glucose
-
 ?
3.2.1.39 laminarioligosaccharide + H2O e.g. laminaritetraose Aplysia kurodai laminaribiose + beta-D-glucose
-
 ?
3.2.1.39 laminaritetraose + H2O
-
 Aplysia kurodai ?
-
 ?
3.2.1.39 additional information AkLam36 specific for beta-1,3-glucosyl linkages. AkLam36 is an endolytic enzyme degrading laminarin and laminarioligosaccharides to laminaritriose, laminaribiose, and D-glucose. AkLam36 shows higher activity toward beta-1,3-glucans with a few beta-1,6-linked glucose branches such as Laminaria digitata laminarin than highly branched beta-1,3-glucans such as Eisenia bicyclis laminarin Aplysia kurodai ?
-
 ?
3.2.1.58 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 ?
-
 ?
3.2.1.58 laminaritetraose + H2O preferred substrate Aplysia kurodai ?
-
 ?
3.2.1.58 laminaritriose + H2O
-
 Aplysia kurodai ?
-
 ?
3.2.1.58 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 ?
-
 ?
3.2.1.58 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

EC Number Subunits Comment Organism
3.2.1.6 ? x * 36000, SDS-PAGE Aplysia kurodai
3.2.1.39 ? x * 36000, SDS-PAGE Aplysia kurodai
3.2.1.58 ? x * 33000, SDS-PAGE Aplysia kurodai

Synonyms

EC Number Synonyms Comment Organism
3.2.1.6 AkLam36
-
 Aplysia kurodai
3.2.1.39 AkLam36
-
 Aplysia kurodai
3.2.1.39 beta-1,3-glucanase
-
 Aplysia kurodai
3.2.1.58 AkLam33
-
 Aplysia kurodai

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.6 50
-
-
 Aplysia kurodai
3.2.1.58 40
-
-
 Aplysia kurodai

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.6 42
-
 50% inactivation Aplysia kurodai
3.2.1.58 45
-
 50% inactivation Aplysia kurodai

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.2.1.6 0.21
-
 laminaritetraose pH 6.0, 30°C Aplysia kurodai
3.2.1.6 23.1
-
 Laminarin pH 6.0, 30°C Aplysia kurodai
3.2.1.39 0.19
-
 laminaritetraose
-
 Aplysia kurodai
3.2.1.39 23.01
-
 Laminarin
-
 Aplysia kurodai
3.2.1.58 0.05
-
 Laminarin pH 6.0, 30°C Aplysia kurodai
3.2.1.58 4.79
-
 laminaritetraose pH 6.0, 30°C Aplysia kurodai

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.6 6
-
-
 Aplysia kurodai
3.2.1.58 5.7
-
-
 Aplysia kurodai