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Literature summary extracted from

  • Nishimoto, M.; Hidaka, M.; Nakajima, M.; Fushinobu, S.; Kitaoka, M.
    Identification of amino acid residues that determine the substrate preference of 1,3-beta-galactosyl-N-acetylhexosamine phosphorylase (2012), J. Mol. Catal. B, 74, 97-102.
No PubMed abstract available

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.4.1.211 DNA and amino acid sequence determination and analysis, sequence comparisons, phylogenetic analysis, exxpression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21 (DE3) Bifidobacterium longum

Protein Variants

EC Number Protein Variants Comment Organism
2.4.1.211 P161S site-directed mutagenesis, the mutation leads to an increase in the selectivity on lacto-N-biose I Bifidobacterium longum
2.4.1.211 P161S/S336A site-directed mutagenesis Bifidobacterium longum
2.4.1.211 S336A site-directed mutagenesis, the mutation leads to an increase in the selectivity on lacto-N-biose I Bifidobacterium longum
2.4.1.211 V162T site-directed mutagenesis, the mutation leads to an increase in the selectivity on galacto-N-biose Bifidobacterium longum

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.4.1.211 2.8
-
 lacto-N-biose I pH 7.5, 30°C, wild-type enzyme Bifidobacterium longum
2.4.1.211 6.7
-
 galacto-N-biose pH 7.5, 30°C, mutant V162T Bifidobacterium longum
2.4.1.211 7.7
-
 galacto-N-biose pH 7.5, 30°C, wild-type enzyme Bifidobacterium longum
2.4.1.211 8.4
-
 lacto-N-biose I pH 7.5, 30°C, mutant P161S Bifidobacterium longum
2.4.1.211 13
-
 lacto-N-biose I pH 7.5, 30°C, mutant S336A Bifidobacterium longum
2.4.1.211 20
-
 galacto-N-biose pH 7.5, 30°C, mutant S336A Bifidobacterium longum
2.4.1.211 22
-
 lacto-N-biose I pH 7.5, 30°C, mutant V162T Bifidobacterium longum
2.4.1.211 27
-
 galacto-N-biose pH 7.5, 30°C, mutant P161S Bifidobacterium longum
2.4.1.211 46
-
 lacto-N-biose I pH 7.5, 30°C, mutant P161S/S336A Bifidobacterium longum
2.4.1.211 120
-
 galacto-N-biose pH 7.5, 30°C, mutant P161S/S336A Bifidobacterium longum

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.211 Bifidobacterium longum E8MF13
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.4.1.211 recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography Bifidobacterium longum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.211 galacto-N-biose + phosphate
-
 Bifidobacterium longum alpha-D-galactose 1-phosphate + N-acetyl-D-galactosamine
-
 ?
2.4.1.211 lacto-N-biose I + phosphate
-
 Bifidobacterium longum alpha-D-galactose 1-phosphate + N-acetyl-D-glucosamine
-
 ?
2.4.1.211 additional information substrate specificity, overview. Structurally determined substrate preference for galacto-N-biose and lacto-N-biose I Bifidobacterium longum ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.4.1.211 GalHexNAcP
-
 Bifidobacterium longum

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.4.1.211 30
-
 assay at Bifidobacterium longum

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.4.1.211 3.5
-
 galacto-N-biose pH 7.5, 30°C, mutant S336A Bifidobacterium longum
2.4.1.211 3.7
-
 galacto-N-biose pH 7.5, 30°C, mutant P161S/S336A Bifidobacterium longum
2.4.1.211 15
-
 lacto-N-biose I pH 7.5, 30°C, mutants S336A and Bifidobacterium longum
2.4.1.211 27
-
 lacto-N-biose I pH 7.5, 30°C, wild-type enzyme Bifidobacterium longum
2.4.1.211 27
-
 galacto-N-biose pH 7.5, 30°C, mutant V162T Bifidobacterium longum
2.4.1.211 33
-
 galacto-N-biose pH 7.5, 30°C, mutant P161S Bifidobacterium longum
2.4.1.211 33
-
 lacto-N-biose I pH 7.5, 30°C, mutant V162T Bifidobacterium longum
2.4.1.211 39
-
 lacto-N-biose I pH 7.5, 30°C, mutant P161S Bifidobacterium longum
2.4.1.211 65
-
 galacto-N-biose pH 7.5, 30°C, wild-type enzyme Bifidobacterium longum

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.4.1.211 7.5
-
 assay at Bifidobacterium longum

General Information

EC Number General Information Comment Organism
2.4.1.211 evolution the GalHexNAcP belongs to the glycoside hydrolase family 112, GH112 Bifidobacterium longum
2.4.1.211 additional information the residues at positions 162, 161, and 336 determine the substrate specificity, structure-function relationship, molecular docking, and specificity prediction, overview. The side-chain hydroxyl group of S336 forms a hydrogen bond with the side-chain nitrogen atom of R358, which plays a significant role in catalysis Bifidobacterium longum

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.4.1.211 0.031
-
 galacto-N-biose pH 7.5, 30°C, mutant P161S/S336A Bifidobacterium longum
2.4.1.211 0.17
-
 galacto-N-biose pH 7.5, 30°C, mutant S336A Bifidobacterium longum
2.4.1.211 0.34
-
 lacto-N-biose I pH 7.5, 30°C, mutant P161S/S336A Bifidobacterium longum
2.4.1.211 1.1
-
 lacto-N-biose I pH 7.5, 30°C, mutant S336A Bifidobacterium longum
2.4.1.211 1.2
-
 galacto-N-biose pH 7.5, 30°C, mutant P161S Bifidobacterium longum
2.4.1.211 1.5
-
 lacto-N-biose I pH 7.5, 30°C, mutant V162T Bifidobacterium longum
2.4.1.211 4
-
 galacto-N-biose pH 7.5, 30°C, mutant V162T Bifidobacterium longum
2.4.1.211 4.6
-
 lacto-N-biose I pH 7.5, 30°C, mutant P161S Bifidobacterium longum
2.4.1.211 8.5
-
 galacto-N-biose pH 7.5, 30°C, wild-type enzyme Bifidobacterium longum
2.4.1.211 9.3
-
 lacto-N-biose I pH 7.5, 30°C, wild-type enzyme Bifidobacterium longum