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Literature summary extracted from

  • Zeuner, B.; Nyffenegger, C.; Mikkelsen, J.D.; Meyer, A.S.
    Thermostable beta-galactosidases for the synthesis of human milk oligosaccharides (2016), N. Biotechnol., 33, 355-60.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.21 expression in Escherichia coli Thermus thermophilus
3.2.1.21 expression in Escherichia coli Niallia circulans
3.2.1.B28 expression in Escherichia coli Pyrococcus furiosus

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.21 Niallia circulans E5RWQ2
-
-
3.2.1.21 Thermus thermophilus Q9RA61
-
-
3.2.1.B28 Pyrococcus furiosus Q51723
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.21 lactose + N,N'-diacetylchitobiose
-
Thermus thermophilus Gal-beta-(1->4)-GlcNAc-beta-(1->3)-Gal-beta-(1->4)-Glc + H2O
-
?
3.2.1.21 lactose + N,N'-diacetylchitobiose
-
Niallia circulans Gal-beta-(1->4)-GlcNAc-beta-(1->3)-Gal-beta-(1->4)-Glc + H2O
-
?
3.2.1.21 additional information enzyme is able to catalyze formation of lacto-N-neotetraose, i.e. Gal-beta(1,4)-GlcNAc-beta(1,3)-Gal-beta(1,4)-Glc, from lactose and N,N'-diacetylchitobiose and of N-acetyllactosamine, i.e Gal-beta(1,4)-GlcNAc from N-acetylglucosamine and lactose. When compared with truncated beta-galactosidase BgaD-D from Bacillus circulans, and beta-glycosidase CelB from Pyrococcus furiosus, BgaD is the most potent transgalactosidase, but both BglT and CelB can catalyze formation of LNnT and LacNAc, with BglT giving higher yields than CelB Thermus thermophilus ?
-
?
3.2.1.21 additional information enzyme is able to catalyze formation of lacto-N-neotetraose, i.e. Gal-beta-(1->4)-GlcNAc-beta-(1->3)-Gal-beta (1->4)-Glc, from lactose and N,N'-diacetylchitobiose and of N-acetyllactosamine, i.e Gal-beta-(1->4)-GlcNAc from N-acetylglucosamine and lactose. When compared with beta-glycosidase BglT from Thermus thermophilus, and beta-glycosidase CelB from Pyrococcus furiosus, BgaD is the most potent transgalactosidase, but both BglT and CelB can catalyze formation of LNnT and LacNAc, with BglT giving higher yields than CelB Niallia circulans ?
-
?
3.2.1.21 N-acetyl-D-glucosamine + lactose
-
Niallia circulans 4-O-beta-D-galactopyranosyl-N-acetyl-D-glucosamine + D-glucose transgalactosylation reaction ?
3.2.1.21 N-acetylglucosamine + lactose
-
Thermus thermophilus Gal-beta-(1->4)-GlcNAc + D-glucose transgalactosylation reaction ?
3.2.1.B28 lactose + N,N'-diacetylchitobiose
-
Pyrococcus furiosus Gal-beta(1,4)-GlcNAc-beta(1,3)-Gal-beta(1,4)-Glc + H2O
-
?
3.2.1.B28 additional information enzyme is able to catalyze formation of lacto-N-neotetraose, i.e. Gal-beta(1,4)-GlcNAc-beta(1,3)-Gal-beta(1,4)-Glc, from lactose and N,N'-diacetylchitobiose and of N-acetyllactosamine, i.e Gal-beta(1,4)-GlcNAc from N-acetylglucosamine and lactose. When compared with beta-glycosidase BglT from Thermus thermophilus, and beta-galactosidase BgaD-D from Bacillus circulans, BgaD is the most potent transgalactosidase, but both BglT and CelB can catalyze formation of LNnT and LacNAc, with BglT giving higher yields than CelB Pyrococcus furiosus ?
-
?
3.2.1.B28 N-acetyl-D-glucosamine + lactose
-
Pyrococcus furiosus 4-O-beta-D-galactopyranosyl-N-acetyl-D-glucosamine + D-glucose transgalactosylation reaction ?

Synonyms

EC Number Synonyms Comment Organism
3.2.1.21 BGA
-
Niallia circulans
3.2.1.21 BglT
-
Thermus thermophilus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.21 80
-
half-life 280 min Thermus thermophilus
3.2.1.21 80
-
half-life 280 min Niallia circulans
3.2.1.21 90
-
half-life 205 min Thermus thermophilus
3.2.1.21 90
-
half-life 205 min Niallia circulans
3.2.1.21 95
-
half-life 11 min Thermus thermophilus
3.2.1.21 95
-
half-life 11 min Niallia circulans
3.2.1.B28 80
-
half-life 280 min Pyrococcus furiosus
3.2.1.B28 90
-
half-life 205 min Pyrococcus furiosus
3.2.1.B28 95
-
half-life 11 min Pyrococcus furiosus