Literature summary for 3.2.1.89 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.

Search for more literature for 3.2.1.89

Crystallization (Commentary)

Crystallization (Comment)	Organism
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

Protein Variants	Comment	Organism
E263A	inactive nucleophile mutant	Bacillus licheniformis

Molecular Weight [Da]

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

Organism

Organism	UniProt	Comment	Textmining
Bacillus licheniformis	-	-	-

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

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

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)