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Literature summary extracted from

  • Yoon, H.J.; Hashimoto, W.; Miyake, O.; Murata, K.; Mikami, B.
    Crystal structure of alginate lyase A1-III complexed with trisaccharide product at 2.0 A resolution (2001), J. Mol. Biol., 307, 9-16.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.2.2.3 overexpression of isozyme A1-III in Bacillus subtilis Sphingomonas sp.

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.2.2.3 8 mg/ml purified isozyme A1-III complexed with trisaccharide product 4-deoxy-L-erythro-hex-4-enepyranosyluronate-mannuronate-mannuronic acid, hanging drop vapour diffusion method, 0.1 M HEPES, pH 7.5, containg 48% PEG w/v saturated ammonium sulfate, 290 mM trisaccharide, 20°C, X-ray diffraction structure determination and analysis at 2.0 A resolution Sphingomonas sp.

Organism

EC Number Organism UniProt Comment Textmining
4.2.2.3 Sphingomonas sp.
-
isozyme A1-III
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.2.2.3 recombinant isozyme A1-III from Bacillus subtilis Sphingomonas sp.

Reaction

EC Number Reaction Comment Organism Reaction ID
4.2.2.3 R2-beta-D-mannuronic acid-R1 = R2-OH + 4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl-R1 substrate binding site structure, active site cleft, catalytic mechanism Sphingomonas sp.

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.2.3 poly-beta-1,4-D-mannuronate
-
Sphingomonas sp. 4-deoxy-L-erythro-hex-4-enepyranosyluronate-mannuronate-mannuronic acid
-
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Synonyms

EC Number Synonyms Comment Organism
4.2.2.3 alginate lyase
-
Sphingomonas sp.