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Literature summary extracted from

  • Le Nours, J.; De Maria, L.; Welner, D.; Jorgensen, C.T.; Christensen, L.L.; Borchert, T.V.; Larsen, S.; Lo Leggio, L.
    Investigating the binding of beta-1,4-galactan to Bacillus licheniformis beta-1,4-galactanase by crystallography and computational modeling (2009), Proteins, 75, 977-989.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.2.1.89 wild-type and mutant E263A in complex with methyl-beta(1-4)-galactotetraoside, grown at room temperature in hanging drops with a resolution range of 30-2.3 A. Crystals of wild-type and mutant E263A both belong to the monoclinic space group P21, containing two molecules in the asymmetric unit Bacillus licheniformis

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.89 E263A inactive nucleophile mutant Bacillus licheniformis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.89 44000
-
 x * 44000, SDS-PAGE of mutant E263A Bacillus licheniformis

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.89 Bacillus licheniformis
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.89 AZCL-galactan + H2O the enzyme shows a conserved beta-turn, characteristic of GH53 enzymes, which contributes to subsites -2 to +3 Bacillus licheniformis ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.2.1.89 ? x * 44000, SDS-PAGE of mutant E263A Bacillus licheniformis

Synonyms

EC Number Synonyms Comment Organism
3.2.1.89 beta-1,4-galactanase
-
 Bacillus licheniformis
3.2.1.89 BLGAL
-
 Bacillus licheniformis