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3.2.1.23: beta-galactosidase

This is an abbreviated version!
For detailed information about beta-galactosidase, go to the full flat file.

Word Map on EC 3.2.1.23

Reaction

beta-D-galactopyranosyl-(1-4)-beta-D-galactopyranosyl-(1-6)-beta-D-galactopyranosyl-(1-3)-beta-D-galactopyranose
+ 3 H2O = 4 beta-D-galactopyranose

Synonyms

Aabeta-gal, Acid beta-galactosidase, B-GAL, BbgI, BbgII, BbgIII, BbgIV, beta galactosidase, beta-D-galactohydrolase, beta-D-galactosidase, beta-D-galactoside galactohydrolase, beta-D-glactanase, beta-D-lactosidase, beta-gal, beta-Gal 1, beta-Gal 2, beta-Gal II, beta-galactosidase, beta-galactosidase I, beta-galactosidase II, beta-galactosidase III, beta-galactosidase IV, beta-galase, beta-lactosidase, betagal, betaGly4, betaGS, BGA, BgaB, BgaBM, bgaD, BgaH, BGAL, BGAL1, BGAL10, BGAL11, BGAL12, BGAL13, BGAL14, BGAL15, BGAL16, BGAL17, BGAL2, BGAL3, BGAL4, BGAL5, BGAL6, BGAL7, BGAL8, BGAL9, BgalA, BgAP, BgaS, BgaX, BGL1, BglAp, BGT I, BGT II, cold-active beta-galactosidase, CTP-beta-gal, driselase, EABase, endo-beta-galactosidase, Exo-(1-->4)-beta-D-galactanase, exo-beta-(1->3)-D-galactanase, Gal-2, Gal-5, GAL1, Gal2, Gal3, Gal4, GALA, galactanase, galactosidase, galactosidase, beta, GALB, gherkin lactase, H-BgaS, hcbetagal, Hlac_2868, Hydrolact, LacA, LACS, lactase, lactase phlorizin hydrolase, lactosylceramidase II, Lactozym, Lactozym 3000L, LPH, Maxilact, Maxilact-L/2000, MeBglD2, More, ONPGase, Oryzatym, p-nitrophenyl beta-galactosidase, PF1208, PRGH1, S 2107, SA-beta-GAL, SA-betagal, senescence-associated beta-galactosidase, SPD_0065 protein, SR12 protein, Ss beta-gal, SSO3019, SSU0587, Sumiklat, Trilactase, XC1214, XG-specific beta-galactosidase, YesZ, YH4502, ZD410

ECTree

     3 Hydrolases
         3.2 Glycosylases
             3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
                3.2.1.23 beta-galactosidase

Renatured

Renatured on EC 3.2.1.23 - beta-galactosidase

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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
beta-galactosidase activity in 80% v/v buffer tetraglyme after 11 h is 9% of the initial activity of the enzyme in 50 mM imidazole/HCl buffer containing 1 mM MgCl2, 145 mM NaCl and 4 mM dithiothreitol at pH 7.0. The recovered activity of the enzyme, measured after dialysis is approximately 45% of the initial activity
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denatured protein from 8 M urea is renatured by dialysis and addition of free and active monomer
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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
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refolding buffer (pH 8.0) contains 10 mM MgCl2, 0.01% Tween 20, 2.5 mM dithiothreitol, and 100 mM Tris-HCl. In a binary system using only L-Arg-HCl the refolding yield of beta-gal increases with increasing concentration up to 0.2 M, in a ternary system using both 0.2 M L-Arg-HCl and another salt, the refolding yield increases up to 1.5fold higher than that in the binary system
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renaturation of the urea-denatured heavy isoenzymes results in the formation of tetramers but not the heavier forms
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