Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.2.1.23 extracted from

  • Chilaka, F.C.; Nwamba, C.O.
    Kinetic analysis of urea-inactivation of beta-galactosidase in the presence of galactose (2008), J. Enzyme Inhib. Med. Chem., 23, 7-15.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Kestingiella geocarpa
-
-
-

Renatured (Commentary)

Renatured (Comment) Organism
investigation of the denaturation of purified beta-galactosidase in 5 M urea at 50°C and pH 4.5. The presence of galactose protects the free enzyme and not the enzyme-substrate complex against urea inactivation via a noncompetitive mechanism at low galactose concentrations and a competitive mechanism at high galactose concentrations Kestingiella geocarpa

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-nitrophenyl beta-D-galactopyranoside + H2O
-
Kestingiella geocarpa 4-nitrophenol + beta-D-galactose
-
?