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Literature summary for 4.2.2.3 extracted from
- Functional characterization of AlgL, an alginate lyase from Pseudomonas aeruginosa (2012), Biochemistry, 51, 10259-10266.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene algL, algL is part of the alginate biosynthetic operon, expression of His-tagged enzyme in Escherichia coli strain C41(DE3) | Pseudomonas aeruginosa |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | steady-state kinetics, overview | Pseudomonas aeruginosa |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Pseudomonas aeruginosa | alginate lyase AlgL catalyzes the cleavage of the polysaccharide alginate through a beta-elimination reaction. AlgL operates preferentially on non-acetylated alginate or its precursor mannuronan. AlgL operates as an exopolysaccharide lyase | ? | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Pseudomonas aeruginosa | Q06749 | gene algL | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged enzyme from Escherichia coli strain C41(DE3) by nickel or cobalt affinity chromatography | Pseudomonas aeruginosa |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| alginate | AlgL lacks of stereospecificity, in that it is able to catalyze cleavage adjacent to either mannuronate or guluronate residues in alginate. The enzyme is able to remove the C5 proton from both mannuronate and guluronate, which are C5 epimers. Exhaustive digestion of alginate by AlgL generates dimeric and trimeric products, analysis by 1H NMR spectroscopy and mass spectrometry. AlgL operates as an exopolysaccharide lyase | Pseudomonas aeruginosa | ? | - |
? | |
| additional information | alginate lyase AlgL catalyzes the cleavage of the polysaccharide alginate through a beta-elimination reaction. AlgL operates preferentially on non-acetylated alginate or its precursor mannuronan. AlgL operates as an exopolysaccharide lyase | Pseudomonas aeruginosa | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| alginate lyase | - |
Pseudomonas aeruginosa |
| AlgL | - |
Pseudomonas aeruginosa |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
assay at | Pseudomonas aeruginosa |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.1 | - |
assay at | Pseudomonas aeruginosa |
General Information
| General Information | Comment | Organism |
|---|---|---|
| metabolism | AlgL is required for for alginate biosynthesis | Pseudomonas aeruginosa |
| physiological function | AlgL serves to degrade mislocalized alginate that is trapped in the periplasmic space | Pseudomonas aeruginosa |
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