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3.2.1.22: alpha-galactosidase

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

Word Map on EC 3.2.1.22

Reaction

alpha-D-galactosyl-(1->4)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide
+
H2O
=
D-galactose
 +
beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide

Synonyms

1,6-alpha-D-galactoside galactohydrolase, a-galactosidase, Ag-I, Ag-II, Aga-F78, Aga-Y, AgaA, agaAJB13, AgaB, AgaI, AGal, AgalB, Agalsidase alfa, AglA, AglC, AkalphaGal, alkaline alpha-gal form 1, alkaline alpha-galactosidase, alkaline alpha-galactosidase form 1, alpha-D-galactopyranoside galactohydrolase, alpha-D-galactosidase, Alpha-D-galactoside galactohydrolase, alpha-Gal, alpha-Gal A, alpha-Gal II, alpha-Gal III, alpha-gal1, alpha-galactosidase, alpha-galactosidase 1, alpha-galactosidase 2, alpha-galactosidase 3, alpha-galactosidase A, alpha-galactosidase AgaA A355E, alpha-galactosidase AgaB, alpha-galactosidase I, alpha-galactosidase II, alpha-galactosidase III, alpha-galactoside galactohydrolase, alphaGal1, ATSIP2, blAga3, BLGA_00330, ceramidase, galactosylgalactosylglucosyl-, ceramide trihexosidase, ceramidetrihexosidase, ceramidetrihexoside-alpha-galactosidase, E1 alpha-galactosidase, E2 alpha-galactosidase, E3 alpha-galactosidase, EC 3.2.1.47, Fabrazyme, Gal36, GALA, galA17, GalS, Genzyme, GH36 alpha-galactosidase, GH97b, GLA, LaMel36A, MEL1, Mel4A, MelA, melibiase, retaining alpha-galactosidase, ScAGal, Tm GalA, TM1192, TmGalA, TnGalA, trihexosyl ceramide galactosidase, trihexosylceramide alpha-galactosidase, trihexosylceramidealpha-galactosidase

ECTree

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

General Stability

General Stability on EC 3.2.1.22 - alpha-galactosidase

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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
0.01% bovine serum albumin stabilizes enzyme stability
-
enzyme displays remarkable resistance to proteases
enzyme immobilization in a cellulose film preserves 97% of the initial enzyme activity. The enzyme maintains above 80% of its original activity after 10 consecutive reuses of the film
-
human serum albumin stabilizes
-
Mn2+ and reducing agents stabilizes activity in cell free extract
-
the enzyme is protease-resistant, when combined with trypsin, the enzyme retained over 90% degradability to soybean meal
the enzyme shows strong resistance to trypsin and proteinase K digestion. After treatment at 37°C for 1 h with trypsin and proteinase K, the enzyme retained 102.1% and 114% of its initial activity, respectively
the enzyme unfolds at 2.7 M urea in the absence of 2,6-dithiopurine, and at 3 M urea in the presence of 2,6-dithiopurine. 2,6-dithiopurine is able to stabilize the enzyme against thermal and urea-induced denaturation