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Literature summary for 3.2.1.140 extracted from

  • Val-Cid, C.; Biarnes, X.; Faijes, M.; Planas, A.
    Structural-functional analysis reveals a specific domain organization in family GH20 hexosaminidases (2015), PLoS ONE, 10, e0128075 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.2.1.140

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) Star Bifidobacterium bifidum

Protein Variants

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/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
lacto-N-tetraose + H2O Bifidobacterium bifidum
-
 lacto-N-biose + lactose
-
 ?

Organism

Organism UniProt Comment Textmining
Bifidobacterium bifidum B3TLD6
-
-

Purification (Commentary)

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 and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
lacto-N-tetraose + H2O
-
 Bifidobacterium bifidum lacto-N-biose + lactose
-
 ?

Subunits

Subunits Comment Organism
More three-dimensional enzyme structure analysis, overview Bifidobacterium bifidum

Synonyms

Synonyms Comment Organism
LnbB
-
 Bifidobacterium bifidum

General Information

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