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Literature summary extracted from
- Characterization of a new alginate lyase from newly isolated Flavobacterium sp. S20 (2013), J. Ind. Microbiol. Biotechnol., 40, 113-122.
Application
| EC Number | Application | Comment | Organism |
|---|---|---|---|
| 4.2.2.11 | industry | alginate lyase is a promising biocatalyst because of its application in saccharification of alginate for the production of renewable biofuels | Flavobacterium sp. |
| 4.2.2.11 | synthesis | alginate lyase is a promising biocatalyst because of its application in saccharification of alginate for the production of biochemicals. Alg2A can be a good tool for the large-scale preparation of alginate oligosaccharides with high degree of polymerization | Flavobacterium sp. |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 4.2.2.11 | expression in Escherichia coli | Flavobacterium sp. |
| 4.2.2.11 | gene alg2A, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) | Flavobacterium sp. |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.2.2.11 | Ca2+ | 5 mM, 66% inhibition | Flavobacterium sp. |  |
| 4.2.2.11 | Co2+ | 5 mM, almost complete inhibition | Flavobacterium sp. | |
| 4.2.2.11 | Cu2+ | 5 mM, almost complete inhibition | Flavobacterium sp. | |
| 4.2.2.11 | Fe2+ | 5 mM, almost complete inhibition | Flavobacterium sp. | |
| 4.2.2.11 | Mg2+ | 5 mM, 66% inhibition | Flavobacterium sp. | |
| 4.2.2.11 | Mn2+ | 5 mM, almost complete inhibition | Flavobacterium sp. | |
| 4.2.2.11 | Zn2+ | 5 mM, almost complete inhibition | Flavobacterium sp. | |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 4.2.2.11 | additional information | - |
additional information | Michaelis-Menten kinetics, overview | Flavobacterium sp. | |
| 4.2.2.11 | additional information | - |
alginate | Km value 3.33 mg/ml, pH 8.5, 30°C | Flavobacterium sp. | |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.2.2.11 | K+ | activates | Flavobacterium sp. | |
| 4.2.2.11 | K+ | 5 mM, 148% of initial activity | Flavobacterium sp. | |
| 4.2.2.11 | Na+ | activates | Flavobacterium sp. | |
| 4.2.2.11 | Na+ | 5 mM, 119% of initial activity | Flavobacterium sp. | |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.2.2.11 | additional information | Flavobacterium sp. | Alg2A has a different endolytic reaction mode from both the two commercial alginate lyases and other alginate lyases from polysaccharide lyase family 7 owing to high yields of penta-, hex-, and hepta-saccharides in the hydrolysis products of Alg2A | ? | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 4.2.2.11 | Flavobacterium sp. | G9CHX6 | - |
- |
| 4.2.2.11 | Flavobacterium sp. | G9CHX6 | gene alg2A | - |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 4.2.2.11 | recombinant His-tagged enzyme 5.74fold from Escherichia coli strain BL21(DE3) by nickel affinity chromatography | Flavobacterium sp. |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 4.2.2.11 | 265.4 | - |
purified recombinant His-tagged enzyme, pH 8.5, 45°C | Flavobacterium sp. |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.2.2.11 | alginate | - |
Flavobacterium sp. | ? | high yields of penta-, hex-, and heptasaccharides in the hydrolysis products | ? | |
| 4.2.2.11 | additional information | Alg2A has a different endolytic reaction mode from both the two commercial alginate lyases and other alginate lyases from polysaccharide lyase family 7 owing to high yields of penta-, hex-, and hepta-saccharides in the hydrolysis products of Alg2A | Flavobacterium sp. | ? | - |
? | |
| 4.2.2.11 | additional information | the enzyme shows low activity with poly(beta-D-mannuronate), reaction of EC 4.2.2.3 | Flavobacterium sp. | ? | - |
? | |
| 4.2.2.11 | poly(alpha-(1->4)-L-guluronic acid) | preferred over poly-(beta1,4-D-mannuronan) | Flavobacterium sp. | ? | - |
? | |
| 4.2.2.11 | poly-(alpha-L-guluronate) | - |
Flavobacterium sp. | ? | - |
? | |
| 4.2.2.11 | poly-(beta-(1->4)-D-mannuronan) | - |
Flavobacterium sp. | ? | - |
? | |
| 4.2.2.11 | sodium alginate | Alg2A prefers poly-(alpha-L-guluronate) as a substrate over poly-(beta-D-mannuronate), substrate specificity, overview | Flavobacterium sp. | ? | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 4.2.2.11 | Alg2A | - |
Flavobacterium sp. |
| 4.2.2.11 | alginate lyase | - |
Flavobacterium sp. |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 4.2.2.11 | 45 | - |
- |
Flavobacterium sp. |
Temperature Range [°C]
| EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 4.2.2.11 | 20 | 70 | 40% of maximal activity at 20°C and 70°C, profile overview | Flavobacterium sp. |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 4.2.2.11 | 45 | - |
stable below | Flavobacterium sp. |
| 4.2.2.11 | 45 | - |
purified recombinant His-tagged enzyme, pH 8.5, 1 h, stable up to | Flavobacterium sp. |
| 4.2.2.11 | 50 | - |
purified recombinant His-tagged enzyme, pH 8.5, 1 h, inactivation | Flavobacterium sp. |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 4.2.2.11 | 872.8 | - |
sodium alginate | recombinant His-tagged enzyme, pH 8.5, 45°C | Flavobacterium sp. | |
| 4.2.2.11 | 873 | 999 | alginate | pH 8.5, 30°C | Flavobacterium sp. | |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 4.2.2.11 | 8.5 | - |
- |
Flavobacterium sp. |
pH Range
| EC Number | pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|---|
| 4.2.2.11 | 5 | 10 | more than 60% of maximum activity within | Flavobacterium sp. |
pH Stability
| EC Number | pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|---|
| 4.2.2.11 | 4 | - |
24 h, 20% residual activity | Flavobacterium sp. |
| 4.2.2.11 | 4 | 10 | purified recombinant His-tagged enzyme, 45°C, the enzyme retains over 60% activity after 24 h incubation at pH 5.0-10.0, but loses about 80% activity at pH 4.0 after 24 h | Flavobacterium sp. |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 4.2.2.11 | evolution | Alg2A belongs to the polysaccharide lyase family 7, but has a different endolytic reaction mode from other alginate lyases from polysaccharide lyase family 7 owing to high yields of penta-, hex-, and hepta-saccharides in the hydrolysis products of Alg2A, overview | Flavobacterium sp. |
kcat/KM [mM/s]
| EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 4.2.2.11 | additional information | - |
alginate | kcat/Km value 26 ml/mg/s, pH 8.5, 30°C | Flavobacterium sp. | |
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