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Literature summary for 4.2.2.3 extracted from

  • Wolfram, F.; Arora, K.; Robinson, H.; Neculai, A.M.; Yip, P.; Howell, P.L.
    Expression, purification, crystallization and preliminary X-ray analysis of Pseudomonas aeruginosa AlgL (2012), Acta Crystallogr. Sect. F, 68, 584-587.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
gene algL, expression from pNMAlgL28–362 expression vector as His-tagged enzyme in Escherichia coli strain Origami 2 (DE3) Pseudomonas aeruginosa

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant His-tagged AlgL28-362 protein, hanging drop vapour diffusion method, mixing of 0.002 ml of 8 mg/ml protein in 20 mM Tris-HCl, pH 7.5, 150 mM NaCl, with 0.002 ml of reservoir solution containing 0.2 M ammonium acetate, 0.1 M sodium citrate tribasic dihydrate, pH 4.6, 28% w/v PEG 4000, 0.3 M PIPES, method optimization, 4 days, 20°C, X-ray diffraction structure determination and analysis at 1.64 A resolution Pseudomonas aeruginosa

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
40000
-
x * 40000 Pseudomonas aeruginosa

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Pseudomonas aeruginosa AlgL is a poly-(beta-D-mannuronate) lyase that preferentially degrades deacetylated polymannuronate via a beta-elimination reaction, resulting in an unsaturated uronic acid at the nonreducing end of the molecule ?
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?

Organism

Organism UniProt Comment Textmining
Pseudomonas aeruginosa Q06749 gene algL, encoded on the algD operon, AlgD/8/44/K/E/G/X/L/I/J/F/A
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Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged AlgL28-362 protein from Escherichia coli strain Origami 2 (DE3) by nickel affinity chrmatography, ultrafiltration, and gel filtration Pseudomonas aeruginosa

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information AlgL is a poly-(beta-D-mannuronate) lyase that preferentially degrades deacetylated polymannuronate via a beta-elimination reaction, resulting in an unsaturated uronic acid at the nonreducing end of the molecule Pseudomonas aeruginosa ?
-
?
additional information AlgL is an endolytic enzyme that cleaves the 1-4 glycosidic linkage, resulting in disaccharides and trisaccharides as its major products. Several residues, including His202 and Tyr256, play a role in AlgL activity Pseudomonas aeruginosa ?
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?

Subunits

Subunits Comment Organism
? x * 40000 Pseudomonas aeruginosa
More AlgL has an alpha6/alpha5-barrel fold Pseudomonas aeruginosa

Synonyms

Synonyms Comment Organism
AlgL
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Pseudomonas aeruginosa

General Information

General Information Comment Organism
evolution AlgL belong to the polysaccharide family 5 Pseudomonas aeruginosa
metabolism the enzyme is involved in the biosynthesis of alginate Pseudomonas aeruginosa