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Literature summary for 4.2.2.3 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.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
overexpression of isozyme A1-II in Escherichia coli Sphingomonas sp.

Crystallization (Commentary)

Crystallization (Comment) Organism
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

Organism UniProt Comment Textmining
Sphingomonas sp.
-
isozyme A1-II
-

Purification (Commentary)

Purification (Comment) Organism
recombinant isozyme A1-II from Escherichia coli, 52.9fold Sphingomonas sp.

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
34.4
-
purified enzyme Sphingomonas sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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

Synonyms Comment Organism
alginate lyase
-
Sphingomonas sp.