KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | kinetics, overview | Aplysia kurodai |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
33000 | - |
x * 33000, SDS-PAGE | Aplysia kurodai |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Aplysia kurodai | - |
- |
- |
Purification (Comment) | Organism |
---|---|
native enzyme 28fold by ammonium sulfate fractionation, and several steps of cation exchange chromatography | Aplysia kurodai |
Source Tissue | Comment | Organism | Textmining |
---|
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
3 | 8 | purified enzyme | Aplysia kurodai |
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 | Comment | Organism |
---|---|---|
? | x * 33000, SDS-PAGE | Aplysia kurodai |
Synonyms | Comment | Organism |
---|---|---|
AkLam33 | - |
Aplysia kurodai |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
40 | - |
- |
Aplysia kurodai |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
45 | - |
50% inactivation | Aplysia kurodai |
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 Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
5.7 | - |
- |
Aplysia kurodai |