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Information on EC 3.2.1.22 - alpha-galactosidase and Organism(s) Thermotoga maritima and UniProt Accession O33835
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EC Tree
3.2.1.22 alpha-galactosidaseIUBMB Comments
Also hydrolyses alpha-D-fucosides.
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Word Map
- 3.2.1.22
- fabry
- lysosomal
-
x-linked
- glycosphingolipids
- cardiac
- globotriaosylceramide
- endothelial
- galactose
- epitope
- oligosaccharide
- pain
- raffinose
- hypertrophy
- ventricular
- proteinuria
- glycosidases
- glycolipids
- angiokeratomas
- alpha-glucosidase
- melibiose
- cerebrovascular
- galactomannans
- simplicifolia
-
multisystemic
-
corporation
-
xenotransplantation
- anaphylaxis
-
hemizygotes
-
cambridge
- alpha-l-fucosidase
- stachyose
- coffee
-
hyperacute
-
anti-gal
- beta-d-glucuronidase
- analysis
-
bandeiraea
- alpha-n-acetylgalactosaminidase
- guar
- beta-d-galactosidase
- biotechnology
-
sanofi
- nutrition
- griffonia
- beta-mannosidase
- imiglucerase
- degradation
- gaucher
- molecular biology
- beta-d-glucosidase
- medicine
- synthesis
-
verticillata
-
soymilk
- alpha-d-mannosidase
- arylamidase
-
flatulence
The taxonomic range for the selected organisms is: Thermotoga maritima
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
alpha-galactosidase, alpha-galactosidase a, alpha-gal, alpha-gal a, agalsidase alfa, genzyme, alpha-d-galactosidase, a-galactosidase, fabrazyme, alpha-galactosidase i, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Agalsidase alfa
-
-
-
-
alpha-D-galactosidase
-
-
-
-
Alpha-D-galactoside galactohydrolase
-
-
-
-
alpha-galactosidase A
-
-
-
-
alpha-galactoside galactohydrolase
-
-
-
-
ceramidase, galactosylgalactosylglucosyl-
-
-
-
-
ceramide trihexosidase
-
-
-
-
ceramidetrihexosidase
-
-
-
-
ceramidetrihexoside-alpha-galactosidase
-
-
-
-
melibiase
-
-
-
-
TmGalA
trihexosyl ceramide galactosidase
-
-
-
-
trihexosylceramide alpha-galactosidase
-
-
-
-
trihexosylceramidealpha-galactosidase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-, -
SYSTEMATIC NAME
IUBMB Comments
alpha-D-galactoside galactohydrolase
Also hydrolyses alpha-D-fucosides.
CAS REGISTRY NUMBER
COMMENTARY
9023-01-2
-
9025-35-8
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2,4-dinitrophenyl alpha-D-galactoside + H2O
2,4-dinitrophenol + alpha-D-galactose
O33835
-
-
-
?
2,5-dinitrophenyl alpha-D-galactoside + H2O
2,5-dinitrophenol + alpha-D-galactose
O33835
-
-
-
?
2-nitrophenyl alpha-D-galactoside + H2O
2-nitrophenol + alpha-D-galactose
O33835
-
-
-
?
3,4-dimethylphenyl alpha-D-galactoside + H2O
3,4-dimethylphenol + alpha-D-galactose
O33835
-
-
-
?
3-nitrophenyl alpha-D-galactoside + H2O
3-nitrophenol + alpha-D-galactose
O33835
-
-
-
?
4-bromophenyl alpha-D-galactoside + H2O
4-bromophenol + alpha-D-galactose
O33835
-
-
-
?
4-methoxyphenyl alpha-D-galactoside + H2O
4-methoxyphenol + alpha-D-galactose
O33835
-
-
-
?
4-nitrophenyl alpha-D-galactoside + H2O
4-nitrophenol + alpha-D-galactose
O33835
-
-
-
?
beta-naphthyl alpha-D-galactoside + H2O
beta-naphthol + alpha-D-galactose
O33835
-
-
-
?
phenyl alpha-D-galactoside + H2O
phenol + alpha-D-galactose
O33835
-
-
-
?
o-nitrophenyl alpha-D-galactopyranoside + H2O
o-nitrophenol + alpha-D-galactose
-
-
-
-
?
p-nitrophenyl alpha-D-galactopyranoside + H2O
p-nitrophenol + alpha-D-galactose
-
-
-
-
?
stachyose + 2 H2O
2 alpha-D-galactose + sucrose
-
20fold less active than with raffinose
-
-
?
verbascose + H2O
alpha-D-galactose + alpha-D-glucopyranosyl-(1,2)-beta-D-fructofuranoside
-
20fold less active than with raffinose
-
-
?
4-nitrophenyl alpha-D-galactopyranoside + H2O
4-nitrophenol + D-galactopyranose
-
-
-
?
4-nitrophenyl alpha-D-galactopyranoside + H2O
4-nitrophenol + D-galactopyranose
hydrolysis is accompanied by transglycosylation resulting in production of a mixture of (alpha1,2)-, (alpha1,3)-, and (alpha1,6)-4-nitrophenyl-digalactosides
-
-
?
additional information
?
-
O33835
no detectable enzymatic activity on xylo-, fuco-, manno-, or glucopyranosides
-
-
?
additional information
?
-
-
no detectable enzymatic activity on xylo-, fuco-, manno-, or glucopyranosides
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
microwave
O33835
microwave irradiation (300 W) significantly stimulates activity
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.037
2,4-dinitrophenyl alpha-D-galactoside
O33835
wild type enzyme, in 200 mM sodium citrate buffer (pH 5.0), at 37°C
0.135
2,4-dinitrophenyl alpha-D-galactoside
O33835
mutant enzyme D327G, in 200 mM sodium citrate buffer (pH 5.0), at 37°C
0.143
2,5-dinitrophenyl alpha-D-galactoside
O33835
wild type enzyme, in 200 mM sodium citrate buffer (pH 5.0), at 37°C
0.243
2,5-dinitrophenyl alpha-D-galactoside
O33835
mutant enzyme D327G, in 200 mM sodium citrate buffer (pH 5.0), at 37°C
0.133
2-nitrophenyl alpha-D-galactoside
O33835
mutant enzyme D327G, in 200 mM sodium citrate buffer (pH 5.0), at 37°C
0.143
2-nitrophenyl alpha-D-galactoside
O33835
wild type enzyme, in 200 mM sodium citrate buffer (pH 5.0), at 37°C
0.086
3,4-dimethylphenyl alpha-D-galactoside
O33835
wild type enzyme, in 200 mM sodium citrate buffer (pH 5.0), at 37°C
0.089
3,4-dimethylphenyl alpha-D-galactoside
O33835
mutant enzyme D327G, in 200 mM sodium citrate buffer (pH 5.0), at 37°C
0.096
3-nitrophenyl alpha-D-galactoside
O33835
wild type enzyme, in 200 mM sodium citrate buffer (pH 5.0), at 37°C
0.14
3-nitrophenyl alpha-D-galactoside
O33835
mutant enzyme D327G, in 200 mM sodium citrate buffer (pH 5.0), at 37°C
0.104
4-bromophenyl alpha-D-galactoside
O33835
mutant enzyme D327G, in 200 mM sodium citrate buffer (pH 5.0), at 37°C
0.111
4-bromophenyl alpha-D-galactoside
O33835
wild type enzyme, in 200 mM sodium citrate buffer (pH 5.0), at 37°C
0.08
4-nitrophenyl alpha-D-galactoside
O33835
wild type enzyme, in 200 mM sodium citrate buffer (pH 5.0), at 37°C
0.083
4-nitrophenyl alpha-D-galactoside
O33835
mutant enzyme D327G, in 200 mM sodium citrate buffer (pH 5.0), at 37°C
0.048
4-O-methylphenyl alpha-D-galactoside
O33835
wild type enzyme, in 200 mM sodium citrate buffer (pH 5.0), at 37°C
0.088
4-O-methylphenyl alpha-D-galactoside
O33835
mutant enzyme D327G, in 200 mM sodium citrate buffer (pH 5.0), at 37°C
0.039
beta-naphthyl alpha-D-galactoside
O33835
wild type enzyme, in 200 mM sodium citrate buffer (pH 5.0), at 37°C
0.225
beta-naphthyl alpha-D-galactoside
O33835
mutant enzyme D327G, in 200 mM sodium citrate buffer (pH 5.0), at 37°C
0.176
phenyl alpha-D-galactoside
O33835
wild type enzyme, in 200 mM sodium citrate buffer (pH 5.0), at 37°C
0.324
phenyl alpha-D-galactoside
O33835
mutant enzyme D327G, in 200 mM sodium citrate buffer (pH 5.0), at 37°C
0.04
4-nitrophenyl alpha-D-galactopyranoside
pH 5.0, 65°C, wild-type enzyme
0.1
4-nitrophenyl alpha-D-galactopyranoside
37°C, pH 5.0, mutant enzyme 328A
0.1
4-nitrophenyl alpha-D-galactopyranoside
37°C, pH 5.0, mutant enzyme F194K
0.1
4-nitrophenyl alpha-D-galactopyranoside
pH 5.0, 65°C, mutant enzyme D327G
0.11
4-nitrophenyl alpha-D-galactopyranoside
37°C, pH 5.0, wild-type enzyme
0.11
4-nitrophenyl alpha-D-galactopyranoside
37°C, pH 5.0, mutant enzyme G385L
0.11
4-nitrophenyl alpha-D-galactopyranoside
37°C, pH 5.0, mutant enzyme P402S
0.12
4-nitrophenyl alpha-D-galactopyranoside
pH 5.0, 65°C, mutant enzyme D327G, assay performed in 500 mM NaN3
0.32
4-nitrophenyl alpha-D-galactopyranoside
37°C, pH 5.0, mutant enzyme L195C
0.43
4-nitrophenyl alpha-D-galactopyranoside
37°C, pH 5.0, mutant enzyme P402D
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.085
2,4-dinitrophenyl alpha-D-galactoside
O33835
mutant enzyme D327G, in 200 mM sodium citrate buffer (pH 5.0), at 37°C
0.41
2,4-dinitrophenyl alpha-D-galactoside
O33835
wild type enzyme, in 200 mM sodium citrate buffer (pH 5.0), at 37°C
12.23
2,4-dinitrophenyl alpha-D-galactoside
O33835
wild type enzyme, in 200 mM sodium citrate buffer (pH 5.0), at 37°C
0.042
2,5-dinitrophenyl alpha-D-galactoside
O33835
mutant enzyme D327G, in 200 mM sodium citrate buffer (pH 5.0), at 37°C
11.2
2,5-dinitrophenyl alpha-D-galactoside
O33835
wild type enzyme, in 200 mM sodium citrate buffer (pH 5.0), at 37°C
0.035
2-nitrophenyl alpha-D-galactoside
O33835
mutant enzyme D327G, in 200 mM sodium citrate buffer (pH 5.0), at 37°C
0.52
2-nitrophenyl alpha-D-galactoside
O33835
wild type enzyme, in 200 mM sodium citrate buffer (pH 5.0), at 37°C
13.67
2-nitrophenyl alpha-D-galactoside
O33835
wild type enzyme, in 200 mM sodium citrate buffer (pH 5.0), at 37°C
0.01
3,4-dimethylphenyl alpha-D-galactoside
O33835
mutant enzyme D327G, in 200 mM sodium citrate buffer (pH 5.0), at 37°C
0.052 - 2.1
3,4-dimethylphenyl alpha-D-galactoside
O33835
wild type enzyme, in 200 mM sodium citrate buffer (pH 5.0), at 37°C
10.39
3,4-dimethylphenyl alpha-D-galactoside
O33835
wild type enzyme, in 200 mM sodium citrate buffer (pH 5.0), at 37°C
0.042
3-nitrophenyl alpha-D-galactoside
O33835
mutant enzyme D327G, in 200 mM sodium citrate buffer (pH 5.0), at 37°C
10.5
3-nitrophenyl alpha-D-galactoside
O33835
wild type enzyme, in 200 mM sodium citrate buffer (pH 5.0), at 37°C
0.016
4-bromophenyl alpha-D-galactoside
O33835
mutant enzyme D327G, in 200 mM sodium citrate buffer (pH 5.0), at 37°C
12.58
4-bromophenyl alpha-D-galactoside
O33835
wild type enzyme, in 200 mM sodium citrate buffer (pH 5.0), at 37°C
0.03
4-nitrophenyl alpha-D-galactoside
O33835
mutant enzyme D327G, in 200 mM sodium citrate buffer (pH 5.0), at 37°C
8.58
4-nitrophenyl alpha-D-galactoside
O33835
wild type enzyme, in 200 mM sodium citrate buffer (pH 5.0), at 37°C
0.01
4-O-methylphenyl alpha-D-galactoside
O33835
mutant enzyme D327G, in 200 mM sodium citrate buffer (pH 5.0), at 37°C
0.03 - 0.55
4-O-methylphenyl alpha-D-galactoside
O33835
wild type enzyme, in 200 mM sodium citrate buffer (pH 5.0), at 37°C
6.69
4-O-methylphenyl alpha-D-galactoside
O33835
wild type enzyme, in 200 mM sodium citrate buffer (pH 5.0), at 37°C
0.021
beta-naphthyl alpha-D-galactoside
O33835
mutant enzyme D327G, in 200 mM sodium citrate buffer (pH 5.0), at 37°C
6.26
beta-naphthyl alpha-D-galactoside
O33835
wild type enzyme, in 200 mM sodium citrate buffer (pH 5.0), at 37°C
0.027
phenyl alpha-D-galactoside
O33835
mutant enzyme D327G, in 200 mM sodium citrate buffer (pH 5.0), at 37°C
5.71
phenyl alpha-D-galactoside
O33835
wild type enzyme, in 200 mM sodium citrate buffer (pH 5.0), at 37°C
0.06
4-nitrophenyl alpha-D-galactopyranoside
pH 5.0, 65°C, mutant enzyme D327G
1.1
4-nitrophenyl alpha-D-galactopyranoside
37°C, pH 5.0, mutant enzyme 328A
2.07
4-nitrophenyl alpha-D-galactopyranoside
pH 5.0, 65°C, mutant enzyme D327G, assay performed in 500 mM NaN3
8
4-nitrophenyl alpha-D-galactopyranoside
37°C, pH 5.0, wild-type enzyme
8.15
4-nitrophenyl alpha-D-galactopyranoside
37°C, pH 5.0, mutant enzyme G385L
9.8
4-nitrophenyl alpha-D-galactopyranoside
37°C, pH 5.0, mutant enzyme P402S
10.73
4-nitrophenyl alpha-D-galactopyranoside
37°C, pH 5.0, mutant enzyme P402D
12.2
4-nitrophenyl alpha-D-galactopyranoside
37°C, pH 5.0, mutant enzyme L195C
20.4
4-nitrophenyl alpha-D-galactopyranoside
37°C, pH 5.0, mutant enzyme F194K
65
4-nitrophenyl alpha-D-galactopyranoside
pH 5.0, 65°C, wild-type enzyme
additional information
phenyl alpha-D-galactoside
O33835
wild type enzyme, in 200 mM sodium citrate buffer (pH 5.0), at 37°C
additional information
phenyl alpha-D-galactoside
-
wild type enzyme, in 200 mM sodium citrate buffer (pH 5.0), at 37°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.6
4-nitrophenyl alpha-D-galactopyranoside
pH 5.0, 65°C, mutant enzyme D327G
11.57
4-nitrophenyl alpha-D-galactopyranoside
37°C, pH 5.0, mutant enzyme 328A
17
4-nitrophenyl alpha-D-galactopyranoside
pH 5.0, 65°C, mutant enzyme D327G, assay performed in 500 mM NaN3
24.95
4-nitrophenyl alpha-D-galactopyranoside
37°C, pH 5.0, mutant enzyme P402D
38.76
4-nitrophenyl alpha-D-galactopyranoside
37°C, pH 5.0, mutant enzyme L195C
72.07
4-nitrophenyl alpha-D-galactopyranoside
37°C, pH 5.0, wild-type enzyme
74.09
4-nitrophenyl alpha-D-galactopyranoside
37°C, pH 5.0, mutant enzyme G385L
88.28
4-nitrophenyl alpha-D-galactopyranoside
37°C, pH 5.0, mutant enzyme P402S
198.06
4-nitrophenyl alpha-D-galactopyranoside
37°C, pH 5.0, mutant enzyme F194K
1585
4-nitrophenyl alpha-D-galactopyranoside
pH 5.0, 65°C, wild-type enzyme
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
225
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5 - 7
-
more than 50% of maximal activity at pH 4.5 and pH 7.0, at 75°C
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
62000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 60000, wild type enzyme and its mutants W85Y, F194K, L195C, F328A, P402D, P402S, and G385L, SDS-PAGE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D327G
O33835
mutant has a 200-800fold lower catalytic rate on aryl galactosides relative to the wild type enzyme
D387G
O33835
mutant is 1500fold catalytically slower than the wild type enzyme on p-nitrophenyl alpha-D-galactopyranoside, and exhibits higher activity with increasing pH
D327G
the mutant is an efficient alpha-galactosynthase producing different galactosylated disaccharides from beta-galactosyl-azide donors and 4-nitrophenyl-alpha-and beta-glycosides as acceptors
F328A
transglycosylation is markedly increased compared to wild-type enzyme. kcat/Km value is more than twofold lower than for the wild type enzyme. 16-fold higher yield of products with the (alpha1,2)-bond as compared to products produced by the wild type enzyme
G385L
transglycosylation is markedly increased compared to wild-type enzyme. Mutation G385L results in a twofold decrease in the specific activity of the enzyme during its purification. The kinetic parameters are not determined for the mutant G385L due to its instability
L195C
kcat/Km value is more than twofold lower than for the wild type enzyme
P402D
transglycosylation is markedly increased compared to wild-type enzyme. kcat/Km value is more than twofold lower than for the wild type enzyme. 4-fold higher yield of products with the (alpha1,2)-bond as compared to products produced by the wild type enzyme
P402S
no significant changes in the kinetic parameters of hydrolysis
W85Y
no significant changes in the kinetic parameters of hydrolysis
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 8
-
75°C, 50 mM citrate-phosphate buffer, less than 40% loss of activity after 5 h
656702
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
75
-
pH 7, 20 mM Tris-HCl buffer, 1 mg/ml protein concentration, 50% loss of activity after 7 days
80
-
pH 7, 20 mM Tris-HCl buffer, 1 mg/ml protein concentration, 50% loss of activity after 48 h
85
-
pH 7, 20 mM Tris-HCl buffer, 1 mg/ml protein concentration, 50% loss of activity after 6 h
90
-
pH 7, 20 mM Tris-HCl buffer, 1 mg/ml protein concentration, 50% loss of activity after 70 min
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
the mutant is an efficient alpha-galactosynthase producing different galactosylated disaccharides from beta-galactosyl-azide donors and 4-nitrophenyl-alpha-and beta-glycosides as acceptors
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Liebl, W.; Wagner, B.; Schellhase, J.
Properties of an alpha-Galactosidas, and structure of its gene galA, within an alpha- and beta-galactoside utilization gene cluster of the hyperthermophilic bacterium Thermotoga maritima
Syst. Appl. Microbiol.
21
1-11
1998
Thermotoga maritima
Miller, E.S.; Parker, K.N.; Liebl, W.; Lam, D.; Callem, W.; Snead, M.A.; mathur, E.J.; Short, J.M.; Kelly, R.M.
alpha-D-Galactosidases from Thermotoga species
Methods Enzymol.
330
246-260
2001
Thermotoga maritima, Thermotoga neapolitana, Thermotoga maritima DSM 3109, Thermotoga neapolitana DSM Z5068
Comfort, D.A.; Bobrov, K.S.; Ivanen, D.R.; Shabalin, K.A.; Harris, J.M.; Kulminskaya, A.A.; Brumer, H.; Kelly, R.M.
Biochemical analysis of Thermotoga maritima GH36 alpha-galactosidase (TmGalA) confirms the mechanistic commonality of clan GH-D glycoside hydrolases
Biochemistry
46
3319-3330
2007
Thermotoga maritima (O33835), Thermotoga maritima, Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589 (O33835)
Young, D.D.; Nichols. J.; Kelly, R.M.; Deiters, A.
Microwave activation of enzymatic catalysis
J. Am. Chem. Soc.
130
10048-10049
2008
Thermotoga maritima (O33835)
Bobrov, K.; Borisova, A.; Eneyskaya, E.; Ivanen, D.; Shabalin, K.; Kulminskaya, A.; Rychkov, G.
Improvement of the efficiency of transglycosylation catalyzed by alpha-galactosidase from Thermotoga maritima by protein engineering
Biochemistry
78
1112-1123
2013
Thermotoga maritima (G4FEF4), Thermotoga maritima, Thermotoga maritima DSM 3109 (G4FEF4)
Cobucci-Ponzano, B.; Zorzetti, C.; Strazzulli, A.; Carillo, S.; Bedini, E.; Corsaro, M.; Comfort, D.; Kelly, R.; Rossi, M.; Moracci, M.
A novel alpha-D-galactosynthase from Thermotoga maritima converts beta-D-galactopyranosyl azide to alpha-galacto-oligosaccharides
Glycobiology
21
448-456
2011
Thermotoga maritima (G4FEF4), Thermotoga maritima DSM 3109 (G4FEF4)
EXTERNAL LINKS (specific for EC-Number 3.2.1.22)
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