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Literature summary for 3.2.1.23 extracted from

  • Nichols, E.R.; Gavina, J.M.; McLeod, R.G.; Craig, D.B.
    Single molecule assays of beta-galactosidase from two wild-type strains of E. coli: effects of protease inhibitors on microheterogeneity and different relative activities with differing substrates (2007), Protein J., 26, 95-105.
    View publication on PubMed
Search for more literature for 3.2.1.23

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ activates Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
 strains ATCC 8677 and ATCC 35321
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
 beta-galactosidase from strains 8677 and 35321 demonstrate that the relative activities of the enzyme for the different substrates differ between the strains, assay method optimizationusing different substrates, overview 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
-
 ?
7-O-beta-D-galactosylresorufin + H2O
-
 Escherichia coli resorufin + beta-D-galactose
-
 ?
9H-(1,3-dichloro-9,9-dimethylacridin-2-one-7-yl) beta-D-galactopyranoside + H2O
-
 Escherichia coli 9H-(1,3-dichloro-9,9-dimethylacridin-2-one-7-ol) + beta-D-galactose
-
 ?
fluorescein-beta-D-digalactopyranoside + H2O
-
 Escherichia coli fluorescein + beta-D-galactose
-
 ?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.3
-
 assay at Escherichia coli