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Literature summary for 3.2.1.23 extracted from

  • Pollard, H.B.; Steers, E.
    Bacillus megaterium, KM beta-galactosidase: purification by affinity chromatography and characterization of the active species (1973), Arch. Biochem. Biophys., 158, 650-661.
    View publication on PubMed
Search for more literature for 3.2.1.23

Inhibitors

Inhibitors Comment Organism Structure
4-aminophenyl beta-D-thiogalactopyranoside
-
 Priestia megaterium

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
120000
-
 2 * 120000, SDS-PAGE Priestia megaterium

Organism

Organism UniProt Comment Textmining
Priestia megaterium
-
-
-
Priestia megaterium KM / ATCC 13632
-
-
-

Purification (Commentary)

Purification (Comment) Organism
native enzyme to homogeneity by 4-aminophenyl beta-D-thiogalactopyranoside affinity chromatography Priestia megaterium

Renatured (Commentary)

Renatured (Comment) Organism
denatured protein from 8 M urea is renatured by dialysis and addition of free and active monomer Priestia megaterium

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-nitrophenyl beta-D-galactopyranoside + H2O
-
 Priestia megaterium 2-nitrophenol + beta-D-galactose
-
 ?
2-nitrophenyl beta-D-galactopyranoside + H2O
-
 Priestia megaterium KM / ATCC 13632 2-nitrophenol + beta-D-galactose
-
 ?

Subunits

Subunits Comment Organism
dimer 2 * 120000, SDS-PAGE Priestia megaterium

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
31
-
 assay at Priestia megaterium

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.2
-
 assay at Priestia megaterium