Literature summary extracted from
Yoon, H.J.; Hashimoto, W.; Katsuya, Y.; Mezaki, Y.; Murata, K.; Mikami, B.
Crystallization and preliminary X-ray crystallographic analysis of alginate lyase A1-II from Sphingomonas species A1 (2000), Biochim. Biophys. Acta, 1476, 382-385.
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
4.2.2.3 |
overexpression of isozyme A1-II in Escherichia coli |
Sphingomonas sp. |
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
4.2.2.3 |
purified isozyme A1-II, hanging drop vapour diffusion method, 0.003 ml protein solution: 38 mg/ml protein, 50 mM Tris-HCl, pH 7.5, + 0.003 ml bottom solution: 0.1 M Tris-HCl, pH 8.5, 43% saturated ammonium sulfate, 8% PEG 4000, 0.2 M Li2SO4, 20°C, 1 month, X-ray diffraction structure determination and analysis at 2.8 A resolution |
Sphingomonas sp. |
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
4.2.2.3 |
Sphingomonas sp. |
- |
isozyme A1-II |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
4.2.2.3 |
recombinant isozyme A1-II from Escherichia coli, 52.9fold |
Sphingomonas sp. |
Specific Activity [micromol/min/mg]
EC Number |
Specific Activity Minimum [µmol/min/mg] |
Specific Activity Maximum [µmol/min/mg] |
Comment |
Organism |
---|
4.2.2.3 |
34.4 |
- |
purified enzyme |
Sphingomonas sp. |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
4.2.2.3 |
alginate |
isozyme A1-II performs endolytic cleavage of the glycosidic bonds, beta-elimination reaction, and shows a preference for polyguluronate instead of polymannuronate |
Sphingomonas sp. |
unsaturated algino-oligosaccharides |
isozyme A1-II produces mainly tri- and tetrasaccharides |
? |
|
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
4.2.2.3 |
alginate lyase |
- |
Sphingomonas sp. |