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Literature summary for 3.2.1.23 extracted from

  • Pessela, B.C.; Dellamora-Ortiz, G.; Betancor, L.; Fuentes, M.; Guisan, J.M.; Fernandez-Lafuente, R.
    Modulation of the catalytic properties of multimeric beta-galactosidase from E. coli by using different immobilization protocols (2007), Enzyme Microb. Technol., 40, 310-315.
No PubMed abstract available
Search for more literature for 3.2.1.23

Protein Variants

Protein Variants Comment Organism
additional information modulation of the catalytic properties of the enzyme using different supports and immobilization strategies, e.g. bearing glyoxyl, epoxy, or BrCN groups or by glutaraldehyde crosslinking on matrices containing primary amino groups, different derivatives exhibit very different synthetic activity/hydrolytic activity ratios in transglycosylation reactions strongly depending on the experimental conditions, overview Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ activates Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
lactose + H2O Escherichia coli
-
 D-glucose + D-galactose
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-nitrophenyl beta-D-galactopyranoside + H2O
-
 Escherichia coli 2-nitrophenol + beta-D-galactose
-
 ?
lactose + H2O
-
 Escherichia coli D-glucose + D-galactose
-
 ?
additional information the enzyme also exhibits transglycosylation activity with lactose as acceptor Escherichia coli ?
-
 ?

Subunits

Subunits Comment Organism
oligomer
-
 Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5
-
 transglycosylation assay at Escherichia coli
7
-
 assay at Escherichia coli