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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

Cloned

Cloned on EC 3.2.1.22 - alpha-galactosidase

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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloned to an improved baculovirus vector and expressed in insect cells at optimized growth conditions, the purified enzyme is taken up by Fabry fibroblasts in culture resulting in normal enzyme levels
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Cos-cells
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expressed in Escherichia coli and in Methylotrophic yeast Ogataea minuta TK5-3/Ura cells
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expressed in Escherichia coli as a His-tagged fusion protein
expressed in Escherichia coli BL-21(DE3) cells
O33835
expressed in Escherichia coli BL21 (DE3) cells
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(lambdaDE3) cells
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expressed in Escherichia coli MV1184 cells
expressed in Escherichia coli RM448 cells
expressed in Escherichia coli Rosetta (DE3) cells
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expressed in Escherichia coli Rosetta(DE3) cells
expressed in Escherichia coli strain BL21(DE3)-RIL
expressed in Escherichia coli strain Origami (DE)
expressed in Escherichia coli TOP10 or XL1 cells
expressed in Pichia pastoris
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expressed in Pichia pastoris as a His-tagged fusion protein
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expressed in Pseudomonas chlororaphis
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expressed in Saccharomyces cerevisiae BJ3505 cells
expressed in Sf9 insect cells
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expressed in Trichoplusia ni insect cells
expression in COS-7 cell
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expression in Escherichia coli
expression in murine fibroblast
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expression in Pichia pastoris
expression in Pichia pastoris. Purified recombinant enzyme is taken up by fibroblasts dericed from fabry disease patients and normal enzyme levels can be restored under theses conditions
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expression in Saccharomyces cerevisiae
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expression of mutant enzyme S65T, S65A and E66D by using an expression system with baculovirus/insect cells, expression in COS cells
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expression with Autographa californica nuclear polyhedrosis virus
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heterologous expression in Nicotiana tabacum var. Petite Havana using chloroplast transformation vector pLD-cut, modification of chloroplast ultrastructures in cutinase transplastomic lines, phenotype, overview
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highly expression in transgenic mice
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mutant enzymes Q279E and R301Q are expressed in Sf9 cells
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mutants expressed in COS-7 cells
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overexpression in CHO cells
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overexpression in Sf9 cells infected with recombinant baculovirus, expression in COS-7 cells
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overexpression of alpha-galactosidase AgaA A355E in Escherichia coli
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overexpression of alpha-galactosidase AgaB in Escherichia coli
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transgenic mouse expressing human mutant alpha-galactosidase R301Q in an endogenous enzyme deficient background is a biochemical animal model for studying active site specific chaperone therapy for Fabry disease. Oral administration of 1-deoxygalactonojirimycin, a competitive inhibitor of alpha-galactosidase A and an effective active-site specific chaperone for Fabry disease, at 0.05 mM in the drinking water of the mice for 2 weeks results in 13.8-, 3.3-, 3.9-, and 2.6fold increase in enzyme activities in the heart, kidney, spleen and liver, respectively
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