Any feedback?
Literature summary for 4.2.2.3 extracted from
- Isolation and characterization of two alginate lyase isozymes, AkAly28 and AkAly33, from the common sea hare Aplysia kurodai (2010), Comp. Biochem. Physiol. B, 157, 317-325.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| NaCl | about 20% of maximal activity in the absence of NaCl, maximal activity at around 0.1 M NaCl | Aplysia kurodai |  |
| NaCl | absolutely required, maximal activity above 0.2 M | Aplysia kurodai | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| NaCl | AkAly28 shows practically no activity in the absence of NaCl and the maximal activity at NaCl concentrations higher than 0.2 M, whereas AkAly33 shows about 20% of maximal activity despite the absence of NaCl and the maximal activity at around 0.1 M NaCl | Aplysia kurodai | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 28000 | - |
x * 28000, SDS-PAGE | Aplysia kurodai |
| 28000 | - |
x * 33000, isozyme AkAly33, SDS-PAGE, x * 28000, isozyme AkAly28, SDS-PAGE | Aplysia kurodai |
| 33000 | - |
x * 33000, SDS-PAGE | Aplysia kurodai |
| 33000 | - |
x * 33000, isozyme AkAly33, SDS-PAGE, x * 28000, isozyme AkAly28, SDS-PAGE | Aplysia kurodai |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Aplysia kurodai | AkAly28 hardly degrades oligosaccharides smaller than tetrasaccharide, while AkAly33 degrades oligosaccharides larger than disaccharide producing disaccharide and 2-keto-3-deoxy-gluconaldehyde, substrate specificities, production of oligosaccharides, analysis by anion-exchange chromatography, overview | ? | - |
? | |
| additional information | Aplysia kurodai | preferably degrades poly(M)-rich substrate and rapidly decreases the viscosity of sodium alginate solution in the initial phase of degradation. Aly33 degrades poly(M)-rich substrate into various sizes of oligosaccharides in the reaction time up to 1 h and further degrades the thus formed oligosaccharides to disaccharide and monosaccharide such as alpha-keto acid in the reaction time 2-6 h | ? | - |
? | |
| additional information | Aplysia kurodai | preferably degrades poly(M)-rich substrate producing unsaturated tri- and disaccharides and rapidly decreases the viscosity of sodium alginate solution in the initial phase of degradation | ? | major reaction products are tri- and disaccharide along with various sizes of intermediary oligosaccharides | ? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Aplysia kurodai | - |
enzyme belongs to polysaccharide lyase family 14 | - |
| Aplysia kurodai | - |
two alginate lyase isozymes, AkAly28 and AkAly33 | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Aplysia kurodai |
| native isozyme AkAly28 72.6fold and isozyme isozyme AkAly33 26fold by ammonium sulfate fractionation and cation exchange chromatography | Aplysia kurodai |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| digestive juice | - |
Aplysia kurodai | - |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 2057 | - |
pH 7.0, 30°C | Aplysia kurodai |
| 2057 | - |
purified isozyme AkAly33, pH 8.0, 37°C | Aplysia kurodai |
| 5740 | - |
pH 7.0, 30°C | Aplysia kurodai |
| 5741 | - |
purified isozyme AkAly28, pH 8.0, 37°C | Aplysia kurodai |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| alginate | highest activity toward poly(M)-rich substrate, moderate activity toward sodium alginate and weak activity toward poly(MG)-rich substrate, no activity toward poly (G)-rich substrate | Aplysia kurodai | ? | major reaction products are tri- and disaccharide along with various sizes of intermediary oligosaccharides | ? | |
| additional information | AkAly28 hardly degrades oligosaccharides smaller than tetrasaccharide, while AkAly33 degrades oligosaccharides larger than disaccharide producing disaccharide and 2-keto-3-deoxy-gluconaldehyde, substrate specificities, production of oligosaccharides, analysis by anion-exchange chromatography, overview | Aplysia kurodai | ? | - |
? | |
| additional information | preferably degrades poly(M)-rich substrate and rapidly decreases the viscosity of sodium alginate solution in the initial phase of degradation. Aly33 degrades poly(M)-rich substrate into various sizes of oligosaccharides in the reaction time up to 1 h and further degrades the thus formed oligosaccharides to disaccharide and monosaccharide such as alpha-keto acid in the reaction time 2-6 h | Aplysia kurodai | ? | - |
? | |
| additional information | preferably degrades poly(M)-rich substrate producing unsaturated tri- and disaccharides and rapidly decreases the viscosity of sodium alginate solution in the initial phase of degradation | Aplysia kurodai | ? | major reaction products are tri- and disaccharide along with various sizes of intermediary oligosaccharides | ? | |
| additional information | preferably degrades poly(M)-rich substrate producing unsaturated tri- and disaccharides and rapidly decreases the viscosity of sodium alginate solution in the initial phase of degradation. Aly28 hardly degrades oligosaccharides smaller than tetrasaccharide | Aplysia kurodai | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 28000, SDS-PAGE | Aplysia kurodai |
| ? | x * 33000, SDS-PAGE | Aplysia kurodai |
| ? | x * 33000, isozyme AkAly33, SDS-PAGE, x * 28000, isozyme AkAly28, SDS-PAGE | Aplysia kurodai |
| More | tryptic peptide mapping, mass spectrometric analysis, overview | Aplysia kurodai |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| alginate lyase | - |
Aplysia kurodai |
| Aly28 | - |
Aplysia kurodai |
| Aly33 | - |
Aplysia kurodai |
| endolytic poly(M) lyase | - |
Aplysia kurodai |
| endolytic polymannuronate lyase | - |
Aplysia kurodai |
| More | AkAly28 and AkAly33 belong to polysaccharide lyase family 14 | Aplysia kurodai |
| poly(M) lyase | - |
Aplysia kurodai |
| polymannuronate lyase | - |
Aplysia kurodai |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 40 | - |
- |
Aplysia kurodai |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 10 | 60 | activity range | Aplysia kurodai |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 38 | - |
half inactivation after 20 min | Aplysia kurodai |
| 38 | - |
half-life of isozymes AkAly28 and AkAly33 is 20 min | Aplysia kurodai |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 6.7 | - |
- |
Aplysia kurodai |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 4 | 11 | activity range | Aplysia kurodai |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | AkAly28 and AkAly33 belong to polysaccharide lyase family 14, N-terminal and internal amino-acid sequences analysis, overview | Aplysia kurodai |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
