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Information on EC 3.2.1.22 - alpha-galactosidase and Organism(s) Homo sapiens

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IUBMB Comments
Also hydrolyses alpha-D-fucosides.
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This record set is specific for:
Homo sapiens
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
alpha-galactosidase, alpha-galactosidase a, alpha-gal, alpha-gal a, agalsidase alfa, genzyme, alpha-d-galactosidase, a-galactosidase, fabrazyme, alpha-galactosidase i, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Agalsidase alfa
alpha-D-galactosidase
-
-
-
-
Alpha-D-galactoside galactohydrolase
-
-
-
-
alpha-Gal
-
alpha-Gal A
alpha-galactosidase
-
-
alpha-galactosidase A
alpha-galactoside galactohydrolase
-
-
-
-
ceramidase, galactosylgalactosylglucosyl-
-
-
-
-
ceramide trihexosidase
-
-
-
-
ceramidetrihexosidase
-
-
-
-
ceramidetrihexoside-alpha-galactosidase
-
-
-
-
Fabrazyme
commercial preparation
Genzyme
commercial preparation
melibiase
-
-
-
-
trihexosyl ceramide galactosidase
-
-
-
-
trihexosylceramide alpha-galactosidase
-
-
-
-
trihexosylceramidealpha-galactosidase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
alpha-D-galactoside galactohydrolase
Also hydrolyses alpha-D-fucosides.
CAS REGISTRY NUMBER
COMMENTARY hide
9023-01-2
-
9025-35-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-methylumbelliferyl alpha-D-galactopyranoside + H2O
4-methylumbelliferone + alpha-D-galactopyranose
show the reaction diagram
-
-
-
?
4-methylumbelliferyl alpha-D-galactoside + H2O
4-methylumbelliferone + alpha-D-galactose
show the reaction diagram
4-methylumbelliferyl alpha-D-galactoside + H2O
4-methylumbelliferone + D-galactose
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl alpha-D-galactoside + H2O
alpha-D-galactose + 4-methylumbelliferone
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl-alpha-D-galactopyranoside + H2O
?
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl-alpha-D-galactoside + H2O
4-methylumbelliferol + alpha-D-galactose
show the reaction diagram
-
-
-
-
?
4-nitrophenyl alpha-D-galactoside + H2O
4-nitrophenol + alpha-D-galactose
show the reaction diagram
-
-
-
?
ceramide trihexoside + H2O
?
show the reaction diagram
-
-
-
-
?
D-galactosyl-D-galactosyl-D-glucosyl-N-acylsphingosine + H2O
lactosyl-N-acylsphingosine + D-galactose
show the reaction diagram
-
-
-
-
?
digalactosylceramide + H2O
galactose + galactosylceramide
show the reaction diagram
-
-
-
-
?
galactobisylceramide + H2O
?
show the reaction diagram
-
-
-
-
?
globopentaose + H2O
?
show the reaction diagram
-
-
-
-
?
globotriaosylceramide + H2O
?
show the reaction diagram
-
-
-
-
?
globotriaosylceramide + H2O
D-Galalpha(1,4)D-Glu-ceramide + D-galactose
show the reaction diagram
-
i.e. D-Galalpha(1,4)D-Galalpha(1,4)D-Glu-ceramide
-
-
?
globotriose + H2O
?
show the reaction diagram
-
-
-
-
?
globtriglycosylceramide + H2O
?
show the reaction diagram
-
-
-
-
?
melibiose + H2O
D-galactose + D-glucose
show the reaction diagram
-
-
-
?
o-nitrophenyl alpha-D-fucopyranoside + H2O
o-nitrophenol + D-fucose
show the reaction diagram
-
-
-
-
?
o-nitrophenyl-alpha-N-acetyl-galactosaminide + H2O
?
show the reaction diagram
-
-
-
-
?
p-nitrophenyl-alpha-galactoside + H2O
p-nitrophenol + galactose
show the reaction diagram
-
-
-
-
?
trihexosylceramide + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-galactosyl-D-galactosyl-D-glucosyl-N-acylsphingosine + H2O
lactosyl-N-acylsphingosine + D-galactose
show the reaction diagram
-
-
-
-
?
globotriaosylceramide + H2O
?
show the reaction diagram
-
-
-
-
?
globotriaosylceramide + H2O
D-Galalpha(1,4)D-Glu-ceramide + D-galactose
show the reaction diagram
-
i.e. D-Galalpha(1,4)D-Galalpha(1,4)D-Glu-ceramide
-
-
?
melibiose + H2O
D-galactose + D-glucose
show the reaction diagram
-
-
-
?
trihexosylceramide + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
NaCl
-
activation
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-deoxy-L-altronojirimycin hydrochloride
1000fold less effective than 1-deoxygalactonojirimycin
1-deoxygalactonojirimycin
Ceramide lactoside
-
-
ceramide trihexoside
D-myo-inositol
-
weak competitive inhibitor
digalactosylceramide
EDTA
-
-
galactose
galactostatin bisulfite
Human serum albumin
-
-
-
myo-inositol
-
-
N-acetyl-D-galactosamine
-
-
n-butyldeoxygalactonojirimycin
2000fold less effective than 1-deoxygalactonojirimycin
NaCl
-
-
sodium taurocholate
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-deoxygalactonojirimycin
digalactosylceramide
-
in absence of sodium taurocholate and sodium chloride at low substrate concentrations
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.9 - 6.8
4-methylumbelliferyl alpha-D-galactopyranoside
2.2 - 4.5
4-methylumbelliferyl alpha-D-galactoside
1.55
4-methylumbelliferyl-alpha-D-galactopyranoside
-
-
1.8 - 16.3
4-methylumbelliferyl-alpha-D-galactoside
0.05 - 0.15
ceramide trihexoside
0.28
digalactosylceramide
-
-
3.7
globopentaose
-
-
9.1
globotriose
-
-
0.18
globtriglycosylceramide
-
-
-
8.8
o-nitrophenyl alpha-D-fucopyranoside
-
-
1.3
o-nitrophenyl-alpha-N-acetyl-galactosaminide
-
alpha-galactosidase B
6.7 - 9.3
p-nitrophenyl-alpha-galactoside
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.038 - 0.047
1-deoxygalactonojirimycin
0.095 - 0.122
galactostatin bisulfite
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000048 - 0.000063
1-deoxygalactonojirimycin
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0396
-
-
0.052
-
-
0.076
-
-
17.6
-
-
2060000
-
placental alpha-galactosidase A
229000
-
plasma alpha-galactosidase A
4.02
-
-
4070000
-
spleen alpha-galactosidase A
6.56
-
-
74.62
-
purified recombinant enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.5
-
ceramide trihexoside
4 - 4.5
-
-
4.1
-
D-galactosyl-D-galactosyl-D-glucosyl-N-acylsphingosine
4.2
-
wild-type and mutant enzymes S65T, S65A and S65D
4.3
-
4-methylumbelliferyl-alpha-D-galactopyranoside as substrate
4.5
-
methylumbelliferyl alpha-galactoside
4.8
-
o-nitrophenyl-alpha-N-acetyl-galactosaminide as substrate
5.4
-
form A
7.2
-
form B
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 7.5
-
wild type enzyme
3.5 - 5.5
-
pH 3.5 about 60% of maximal activity, pH 5.5 about 10% of maximal activity
3.5 - 6.5
-
mutant enzymes
3.6 - 5.4
-
pH 3.6: about 75% of maximal activity, pH 5.4: about 40% of maximal activity, wild-type enzyme and mutant enzymes S65T, S65A and E66D
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
enzyme activity is detected in unstimulated whole saliva and mainly due to isoform A activity. Activity is higher in unclarified samples than in clarified ones and shows wide daily variations. Activity in whole salivea is significantly higher than in glandular saliva
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
AGAL_HUMAN
429
0
48767
Swiss-Prot
Secretory Pathway (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
101000
-
gel filtration
103000
117000
-
gel filtration, alpha-galactosidase B
150000
-
gel filtration
24000
-
4 * 24000, SDS-PAGE
46000
46620
46850
49800
-
alpha-galactosidase A, 2 * 49800, SDS-PAGE
50000
-
ER and Golgi enzyme forms, SDS-PAGE
95000
-
sucrose density gradient centrifugation, gel filtration
96600
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
homodimer
x-ray crystallography
tetramer
-
4 * 24000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
construction of structural models of mutant enzyme responsible for Fabry disease and calculation of indexes. Structural changes in the classic Fabry disease group are generally large and tend to be in the core region of a protein or located in the functionally important region, including the active-site pocket. Structural changes in the variant Fabry disease group are small or localized on the surface of the molecule far away from the activte site. Structural changes due to amino acid substitutions for which substrate analogues are effective for improving the stability or transportation are small or localized on the molecular surface
-
hanging drop vapor diffusion method, using 25% (w/v) PEG 4000, 200 mM (NH4)2SO4, and 100 mM NaCH3COO, pH 4.6, at 20°C
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A156V
-
reduced activity
A20P
-
reduced activity
A230T
6 mM 2,6-dithiopurine promotes the maturation of the mutant enzyme
A37T
2,6-dithiopurine has no effect on this mutant enzyme
A97V
-
reduced activity
C142W
-
mutation isolated in patient with Fabry disease. 1-Deoxygalactonojirimycin has no significant effect on catalytic activity
C172G
2,6-dithiopurine has no effect on this mutant enzyme
D170A
the mutant protein lacks the active site nucleophile
D231G
-
mutation isolated in patient with Fabry disease. Protein expression is similar to wild-type, but mutant has no catalytic activity. 1-Deoxygalactonojirimycin has no significant effect on catalytic activity
D246N
the mutant shows about 37% activity compared to the wild type enzyme
D266N
-
mutation isolated in patient with Fabry disease. 1-Deoxygalactonojirimycin has no significant effect on catalytic activity
E59K
-
reduced activity
E66D
-
KM-value and maximal velocity with 4-methylumbelliferyl alpha-D-galactoside as substrate are similar to the wild-type values. The stability of the mutant enzyme at neutral pH is reduced to 54% of the wild-type enzyme. The intracellular activity in COS1 cells is 68% of the wild-type activity. Intracellular activity in COS1 cells is enhanced to 80% of wild-type activity by cultivation of cells with 1-deoxygalactonojirimycin
F113L
G360C
2,6-dithiopurine has no effect on this mutant enzyme
L166V
-
reduced activity
L300F
2,6-dithiopurine has no effect on this mutant enzyme
M296I
-
reduced activity
M296V
-
reduced activity
M42T
2,6-dithiopurine has no effect on this mutant enzyme
M51I
-
enzymological parameter values are almost the same as those of the wild-type GLA. Km (4-methylumbelliferyl alpha-D-galactoside) similar to wild-type. Mutant enzyme is unstable under neutral pH conditions and acidic ones. The effect of imino sugars including 1-deoxygalactonojirimycin and galactostatin bisulfite on the purified mutant enzyme is examined. The imino sugars improve the stability of the mutant enzyme under both neutral and acidic pH conditions. The results of surface plasmon resonance biosensor assaying suggests that the imino sugars retain their binding activity as to the mutant enzyme under both neutral and acidic pH conditions
M72V
-
reduced activity
N215S
-
reduced activity
P40S
2,6-dithiopurine has no effect on this mutant enzyme
Q279E
Q280K
2,6-dithiopurine has no effect on this mutant enzyme
R112C
-
mutation isolated in patient with Fabry disease. 1-Deoxygalactonojirimycin enhances mutant catalytic activity
R112H
-
reduced activity
R118C
R118G
the mutant shows about 38% activity compared to the wild type enzyme
R118H
the mutant shows about 68% activity compared to the wild type enzyme
R118L
the mutant shows about 52% activity compared to the wild type enzyme
R118P
the mutant shows about 48% activity compared to the wild type enzyme
R118S
the mutant shows about 78% activity compared to the wild type enzyme
R301Q
R356W
-
reduced activity
S126C
S126G
the mutant shows about 52% activity compared to the wild type enzyme
S126I
the mutant shows about 38% activity compared to the wild type enzyme
S126N
the mutant shows about 17% activity compared to the wild type enzyme
S126R
the mutant shows about 20% activity compared to the wild type enzyme
S126T
the mutant shows about 48% activity compared to the wild type enzyme
S297F
-
mutation isolated in patient with Fabry disease. 1-Deoxygalactonojirimycin has no significant effect on catalytic activity
S65A
-
KM-value and maximal velocity with 4-methylumbelliferyl alpha-D-galactoside as substrate are similar to the wild-type values. The stability of the mutant enzyme at neutral pH is reduced to 29% of the wild-type enzyme. The intracellular activity in COS1 cells is 26% of the wild-type activity. Intracellular activity in COS1 cells is enhanced to 44% of wild-type activity by cultivation of cells with 1-deoxygalactonojirimycin
S65T
-
KM-value and maximal velocity with 4-methylumbelliferyl alpha-D-galactoside as substrate are similar to the wild-type values. The stability of the mutant enzyme at neutral pH is reduced to 4% of the wild-type enzyme. The intracellular activity in COS1 cells is 9% of the wild-type activity. Intracellular activity in COS1 cells is enhanced to 34% of wild-type activity by cultivation of cells with 1-deoxygalactonojirimycin
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 6
-
37°C, 20 min, mutant enzymes S65T, S65A and E66D are stable
654330
4 - 7
-
37°C, 20 min, wild-type enzyme is stable
654330
6.1
-
mutant enzyme S65T, more than 50% loss of activity after 20 min above
654330
6.5
-
mutant enzyme S65A, more than 50% loss of activity after 20 min above
654330
6.9
-
mutant enzyme S66D, more than 50% loss of activity after 20 min above
654330
7
-
20 min,mutant enzyme S65T shows 3% residual activity, mutant enzyme S65A shows 24% residual activity, mutant enzyme S66D shows 45% residual activity
654330
7.4
-
above no activity
136495
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100
-
A-1 75% loss of activity after boiling, A-2 100% loss of activity after boiling
50
-
mutant enzymes Q279E and R301Q are almost completely inactivated after 30 min at 50°C, while the wild-type enzyme retains 43% of its original activity even after 60 min
52
-
1 h, 90% loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Butanol
-
A1 retains enzymatic activity in 100% butanol, A2 retains activity in 20% butanol
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, pH 6, 1 mg/ml human serum albumin or 5% polyvinylpyrolidone, less than 3% per month loss in activity
-
5°C, at least 3 days, dialysed (NH4)2SO4 precipitates, at least 1 month
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
efficient and rapid purification procedure for recombinant alpha-galactosidase A by sequential Concanavalin A-Sepharose and immobilized thio-alpha-galactoside agarose column chromatography. This procedure is especially useful for the purification of mutant forms of alpha-galactosidase A, which are not stable under conventional purification techniques. Purification of the intracellular mutant enzyme M279I, expressed in COS-7 cells within 6 h at 62% overall yield
-
Ni2+-Sepharose column chromatography
recombinant enzyme
-
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
-
Cos-cells
-
expressed in Escherichia coli and in Methylotrophic yeast Ogataea minuta TK5-3/Ura cells
-
expressed in Trichoplusia ni insect cells
expression in COS-7 cell
-
expression in murine fibroblast
-
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
-
expression of mutant enzyme S65T, S65A and E66D by using an expression system with baculovirus/insect cells, expression in COS cells
-
expression with Autographa californica nuclear polyhedrosis virus
-
highly expression in transgenic mice
-
mutant enzymes Q279E and R301Q are expressed in Sf9 cells
-
mutants expressed in COS-7 cells
-
overexpression in CHO cells
-
overexpression in Sf9 cells infected with recombinant baculovirus, expression in COS-7 cells
-
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
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme activity in Fabry disease patients is significantly lower than values measured for healthy controls
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
determinantion of alpha-galactosidase A activity in samples from patients with Fabry disease and healthy controls. Average enzyme activity in dried blood spot samples prepared using EDTA tubes is higher compared to those spotted directly irrespective of disease status
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kusiak, J.W.; Quirk, J.M.; Brady, R.O.
Ceramide trihexosidase from human placenta
Methods Enzymol.
50
533-537
1978
Homo sapiens
Manually annotated by BRENDA team
Mapes, C.A.; Suelter, C.H.; Sweeley, C.C.
Isolation and characterization of ceramide trihexosidases (form A) from human plasma
J. Biol. Chem.
248
2471-2479
1973
Homo sapiens
Manually annotated by BRENDA team
Mae Wan Ho
Hydrolysis of ceramide trihexoside by a specific alpha-galactosidase from human liver
Biochem. J.
133
1-10
1973
Homo sapiens
Manually annotated by BRENDA team
Mapes, C.A.; Sweeley, C.C.
Interconversion of the A and B forms of ceramide trihexosidase from human plasma
Arch. Biochem. Biophys.
158
297-304
1973
Homo sapiens
Manually annotated by BRENDA team
Mapes, C.A.; Sweeley, C.C.
Substrate specificity of ceramide trihexosidase
FEBS Lett.
25
279-281
1972
Homo sapiens
Manually annotated by BRENDA team
Rietra, P.J.G.M.; Tager, J.M.; Borst, P.
Detection and properties of an acid alpha-galactosidase (ceramidetrihexosidase) in normal human urine
Biochim. Biophys. Acta
279
436-445
1972
Homo sapiens
Manually annotated by BRENDA team
Poulos, A.; Beckman, K.
Trihexosylceramide alpha-galactosidase of human leucocytes
Clin. Chim. Acta
89
35-45
1978
Homo sapiens
Manually annotated by BRENDA team
Scram, A.W.; Tager, J.M.
The specificity of lysosomal hydrolases: human alpha-Galactosidas isoenzymes
Trends Biochem. Sci.
6
328-330
1981
Homo sapiens
-
Manually annotated by BRENDA team
Bishop, D.F.; Desnick, R.F.
Affinity purification of alpha-galactosidase A from human spleen, placenta, and plasma with elemination of pyrogene contamination
J. Biol. Chem.
256
1307-1316
1981
Homo sapiens
Manually annotated by BRENDA team
Dean, K.J.; Sweeley, C.C.
Studies on human liver alpha-galactosidase. I Purification of alpha-Galactosidas A and its enzymatic properties with glycolipid and oligosaccharide substrates
J. Biol. Chem.
254
9994-10000
1979
Homo sapiens
Manually annotated by BRENDA team
Dean, K.J.; Sweeley, C.C.
Studies on human liver alpha-galactosidase. II Purification and enzymatic properties of alpha-Galactosidas B (alpha-N-acetylgalactosaminidase)
J. Biol. Chem.
254
10001-10005
1979
Homo sapiens
Manually annotated by BRENDA team
Dean, K.J.; Sweeley, C.C.
Studies on human liver alpha-galactosidases. III. Partial characterization of carbohydrate-binding specificities
J. Biol. Chem.
254
10006-10010
1979
Homo sapiens
Manually annotated by BRENDA team
Salvayre, R.; Maret, A.; Negre, A.; Douste-Blazy, L.
Properties of multiple molecular forms of alpha-galactosidase and alpha-N-acetylgalactosaminidase from normal and fabry leukocytes
Eur. J. Biochem.
100
377-383
1979
Homo sapiens
Manually annotated by BRENDA team
Bishop.D.F.; Sweely, C.C.
Plasma alpha-galactosidase A: properties and comparisons with tissue alpha-Galactosidas
Biochim. Biophys. Acta
525
399-409
1978
Homo sapiens
Manually annotated by BRENDA team
Kusiak, J.W.; Quirk, J.M.; Brady, R.O.
Purification and properties of the two major isozymes of alpha-galactosidase from human placenta
J. Biol. Chem.
253
184-190
1978
Homo sapiens
Manually annotated by BRENDA team
Beutler, E.; Kuhl, W.
Purification and properties of human alpha-galactosidases
J. Biol. Chem.
247
7195-7200
1972
Homo sapiens
Manually annotated by BRENDA team
Kase, R.; Shimmoto, M.; Itoh, K.; Utsumi, K.; Kotani, M.; Taya, C.; Yonekawa, H.; Sakuraba, H.
Immunohistochemical characterization of transgenic mice highly expressing human lysosomal alpha-Galactosidas
Biochim. Biophys. Acta
1406
260-266
1998
Homo sapiens
Manually annotated by BRENDA team
Ishii, S.; Kase, R.; Sakuraba, H.; Suzuki, Y.
Characterization of a mutant alpha-Galactosidas gene product for the late-onset cardiac form of fabry disease
Biochem. Biophys. Res. Commun.
197
1585-1589
1993
Homo sapiens
Manually annotated by BRENDA team
Coppola, G.; Yan, Y.; Hantzopoulos, P.; Segura, E.; Stroh, J.G.; Calhoun, D.H.
Characterization of glycosylated and catalytically active recombinant human alpha-galactosidase A using baculovirus vector
Gene
14
197-203
1994
Homo sapiens
Manually annotated by BRENDA team
Ioannou,Y.A.; Bishop, D.F.; Desnick, R.J.
Overexpression of human alpha-galactosidase A results in its intracellular aggregation, crystallization in lysosomes, and selective secretion
J. Cell Biol.
119
1137-1150
1992
Homo sapiens
Manually annotated by BRENDA team
Ishii, S.; Suzuki, Y.; Fan, J.Q.
Role of Ser-65 in the activity of alpha-galactosidase A: characterization of a point mutation (S65T) detected in a patient with Fabry disease
Arch. Biochem. Biophys.
377
228-233
2000
Homo sapiens
Manually annotated by BRENDA team
Kase, R.; Bierfreund, U.; Klein, A.; Kolter, T.; Utsumi, K.; Itoh, K.; Sandhoff, K.; Sakuraba, H.
Characterization of two alpha-galactosidase mutants (Q279E and R301Q) found in an atypical variant of fabry disease
Biochim. Biophys. Acta
1501
227-235
2000
Homo sapiens
Manually annotated by BRENDA team
Chen, Y.; Jin, M.; Goodrich, L.; Smith, G.; Coppola, G.; Calhoun, D.H.
Purification and characterization of human alpha-galactosidase A expressed in insect cells using a baculovirus vector
Protein Expr. Purif.
20
228-236
2000
Homo sapiens
Manually annotated by BRENDA team
Chen, Y.; Jin, M.; Egborge, T.; Coppola, G.; Andre, J.; Calhoun, D.H.
Expression and characterization of glycosylated and catalytically active recombinant human alpha-galactosidase A produced in Pichia pastoris
Protein Expr. Purif.
20
472-484
2000
Homo sapiens
Manually annotated by BRENDA team
Ishii, S.; Yoshioka, H.; Mannen, K.; Kulkarni, A.B.; Fan, J.Q.
Transgenic mouse expressing human mutant alpha-galactosidase A in an endogenous enzyme deficient background: a biochemical animal model for studying active-site specific chaperone therapy for Fabry disease
Biochim. Biophys. Acta
1690
250-257
2004
Homo sapiens
Manually annotated by BRENDA team
Matsuzawa, F.; Aikawa, S.; Doi, H.; Okumiya, T.; Sakuraba, H.
Fabry disease: correlation between structural changes in alpha-galactosidase, and clinical and biochemical phenotypes
Hum. Genet.
117
317-328
2005
Homo sapiens (P06280)
Manually annotated by BRENDA team
Yasuda, K.; Chang, H.H.; Wu, H.L.; Ishii, S.; Fan, J.Q.
Efficient and rapid purification of recombinant human alpha-galactosidase A by affinity column chromatography
Protein Expr. Purif.
37
499-506
2004
Homo sapiens
Manually annotated by BRENDA team
Ishii, S.; Chang, H.H.; Kawasaki, K.; Yasuda, K.; Wu, H.L.; Garman, S.C.; Fan, J.Q.
Mutant alpha-galactosidase A enzymes identified in Fabry disease patients with residual enzyme activity: biochemical characterization and restoration of normal intracellular processing by 1-deoxygalactonojirimycin
Biochem. J.
406
285-295
2007
Homo sapiens
Manually annotated by BRENDA team
Oh, J.K.; Lee, J.Y.; Park, H.K.; Kho, H.S.
alpha-Galactosidase activity in human saliva
Arch. Oral Biol.
53
842-848
2008
Homo sapiens
Manually annotated by BRENDA team
Hamanaka, R.; Shinohara, T.; Yano, S.; Nakamura, M.; Yasuda, A.; Yokoyama, S.; Fan, J.Q.; Kawasaki, K.; Watanabe, M.; Ishii, S.
Rescue of mutant alpha-galactosidase A in the endoplasmic reticulum by 1-deoxygalactonojirimycin leads to trafficking to lysosomes
Biochim. Biophys. Acta
1782
408-413
2008
Homo sapiens
Manually annotated by BRENDA team
Olivova, P.; der Veen, K.V.; Cullen, E.; Rose, M.; Zhang, X.K.; Sims, K.B.; Keutzer, J.; Browning, M.F.
Effect of sample collection on alpha-galactosidase A enzyme activity measurements in dried blood spots on filter paper
Clin. Chim. Acta
403
159-162
2009
Homo sapiens
Manually annotated by BRENDA team
Park, J.Y.; Kim, G.H.; Kim, S.S.; Ko, J.M.; Lee, J.J.; Yoo, H.W.
Effects of a chemical chaperone on genetic mutations in alpha-galactosidase A in Korean patients with Fabry disease
Exp. Mol. Med.
41
1-7
2009
Homo sapiens
Manually annotated by BRENDA team
West, M.; Nicholls, K.; Mehta, A.; Clarke, J.T.; Steiner, R.; Beck, M.; Barshop, B.A.; Rhead, W.; Mensah, R.; Ries, M.; Schiffmann, R.
Agalsidase alfa and kidney dysfunction in Fabry disease
J. Am. Soc. Nephrol.
20
1132-1139
2009
Homo sapiens
Manually annotated by BRENDA team
Sugawara, K.; Ohno, K.; Saito, S.; Sakuraba, H.
Structural characterization of mutant alpha-galactosidases causing Fabry disease
J. Hum. Genet.
53
812-824
2008
Homo sapiens
Manually annotated by BRENDA team
Wu, G.; Yan, B.; Wang, X.; Feng, X.; Zhang, A.; Xu, X.; Dong, H.
Decreased activities of lysosomal acid alpha-D-galactosidase A in the leukocytes of sporadic Parkinsons disease
J. Neurol. Sci.
271
168-173
2008
Homo sapiens
Manually annotated by BRENDA team
Sugawara, K.; Tajima, Y.; Kawashima, I.; Tsukimura, T.; Saito, S.; Ohno, K.; Iwamoto, K.; Kobayashi, T.; Itoh, K.; Sakuraba, H.
Molecular interaction of imino sugars with human alpha-galactosidase: Insight into the mechanism of complex formation and pharmacological chaperone action in Fabry disease
Mol. Genet. Metab.
96
233-238
2009
Homo sapiens (P06280), Homo sapiens
Manually annotated by BRENDA team
Shin, S.H.; Kluepfel-Stahl, S.; Cooney, A.M.; Kaneski, C.R.; Quirk, J.M.; Schiffmann, R.; Brady, R.O.; Murray, G.J.
Prediction of response of mutated alpha-galactosidase A to a pharmacological chaperone
Pharmacogenet. Genomics
18
773-780
2008
Homo sapiens
Manually annotated by BRENDA team
Guce, A.I.; Clark, N.E.; Salgado, E.N.; Ivanen, D.R.; Kulminskaya, A.A.; Brumer, H.; Garman, S.C.
Catalytic mechanism of human alpha-galactosidase
J. Biol. Chem.
285
3625-3632
2010
Homo sapiens (P06280), Homo sapiens
Manually annotated by BRENDA team
Yan, S.; Wu, G.
Mutation patterns in human alpha-galactosidase A
Mol. Divers.
14
147-154
2010
Homo sapiens
Manually annotated by BRENDA team
Tsukimura, T.; Chiba, Y.; Ohno, K.; Saito, S.; Tajima, Y.; Sakuraba, H.
Molecular mechanism for stabilization of a mutant alpha-galactosidase A involving M51I amino acid substitution by imino sugars
Mol. Genet. Metab.
103
26-32
2011
Homo sapiens
Manually annotated by BRENDA team
Daitx, V.V.; Mezzalira, J.; Goldim, M.P.; Coelho, J.C.
Comparison between alpha-galactosidase A activity in blood samples collected on filter paper, leukocytes and plasma
Clin. Biochem.
45
1233-1238
2012
Homo sapiens
Manually annotated by BRENDA team
Lukas, J.; Giese, A.K.; Markoff, A.; Grittner, U.; Kolodny, E.; Mascher, H.; Lackner, K.J.; Meyer, W.; Wree, P.; Saviouk, V.; Rolfs, A.
Functional characterisation of alpha-galactosidase a mutations as a basis for a new classification system in Fabry disease
PLoS Genet.
9
e1003632
2013
Homo sapiens (P06280), Homo sapiens
Manually annotated by BRENDA team
Daitx, V.V.; Mezzalira, J.; Moraes, V.d.a. .C.; Breier, A.C.; Ce, J.; Coelho, J.C.
Comparing the alpha-galactosidase A biochemical properties from healthy individuals and Fabry disease patients
Clin. Chim. Acta
445
60-64
2015
Homo sapiens (P06280), Homo sapiens
Manually annotated by BRENDA team
Citro, V.; Pena-Garcia, J.; den-Haan, H.; Perez-Sanchez, H.; Del Prete, R.; Liguori, L.; Cimmaruta, C.; Lukas, J.; Cubellis, M.V.; Andreotti, G.
Identification of an allosteric binding site on human lysosomal alpha-galactosidase opens the way to new pharmacological chaperones for Fabry disease
PLoS ONE
11
e0165463
2016
Homo sapiens (P06280), Homo sapiens
Manually annotated by BRENDA team
Riera, C.; Lois, S.; Dominguez, C.; Fernandez-Cadenas, I.; Montaner, J.; Rodriguez-Sureda, V.; de la Cruz, X.
Molecular damage in Fabry disease Characterization and prediction of alpha-galactosidase A pathological mutations
Proteins Struct. Funct. Bioinform.
83
91-104
2015
Homo sapiens (P06280), Homo sapiens
Manually annotated by BRENDA team