Cloned (Comment) | Organism |
---|---|
recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) Star | Bifidobacterium bifidum |
Protein Variants | Comment | Organism |
---|---|---|
additional information | generation of different truncated forms of the enzyme, structure-function analysis in comparison to the wild-type, overview. The large Bifidobacterium bifidum lacto-N-biosidase and its truncated mutants are used as a model proteins to evaluate the minimal functional unit due to its interest and structural complexity | Bifidobacterium bifidum |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
lacto-N-tetraose + H2O | Bifidobacterium bifidum | - |
lacto-N-biose + lactose | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bifidobacterium bifidum | B3TLD6 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) Star by nickel affinity chromatography, gel filtration, and ultrafiltration | Bifidobacterium bifidum |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
lacto-N-tetraose + H2O | - |
Bifidobacterium bifidum | lacto-N-biose + lactose | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | three-dimensional enzyme structure analysis, overview | Bifidobacterium bifidum |
Synonyms | Comment | Organism |
---|---|---|
LnbB | - |
Bifidobacterium bifidum |
General Information | Comment | Organism |
---|---|---|
evolution | the enzyme belongs to the glycosyl hydrolase family 20, GH20. Domain organization of GH20 beta-N-acetylhexosaminidases, overview | Bifidobacterium bifidum |
additional information | the large Bifidobacterium bifidum lacto-N-biosidase and its truncated mutants are used as model proteins to evaluate the minimal functional unit due to its interest and structural complexity. Structure-function analysis of the wild-type in comparison to different truncated enzyme mutants, and comparisons of enzyme structure models, overview. The lacto-N-biosidase requires GH20b and the lectin-like domain at the N- and C-termini of the catalytic GH20 domain to be fully soluble and functional. The lectin domain provides this remote element to the active site. Restoration of activity of the inactive GH20beta-GH20-alpha construct (model A architecture) by a complementation assay with the lectin-like domain | Bifidobacterium bifidum |