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Literature summary for 3.2.1.23 extracted from

  • Komp, M.; Hess, D.
    Multiple beta-galactosidase activities in Petunia hybrida: separation and characterization (1981), Phytochemistry, 20, 973-976.
No PubMed abstract available

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.182
-
o-nitrophenyl-beta-D-galactoside enzyme form H4 Petunia x hybrida
0.95
-
o-nitrophenyl-beta-D-galactoside enzyme form H3 Petunia x hybrida
1.05
-
o-nitrophenyl-beta-D-galactoside enzyme form H1 Petunia x hybrida
1.33
-
o-nitrophenyl-beta-D-galactoside enzyme form H2 Petunia x hybrida

Organism

Organism UniProt Comment Textmining
Petunia x hybrida
-
multiple forms: H1, H2, H3 and H4
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
o-nitrophenyl-beta-D-galactoside + H2O
-
Petunia x hybrida o-nitrophenol + beta-D-galactose
-
?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
55
-
-
Petunia x hybrida

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
4.3
-
-
Petunia x hybrida