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Information on EC 3.2.1.102 - blood-group-substance endo-1,4-beta-galactosidase and Organism(s) Clostridium perfringens and UniProt Accession Q6RUF5
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3.2.1.102 blood-group-substance endo-1,4-beta-galactosidaseIUBMB Comments
Hydrolyses the 1,4-beta-D-galactosyl linkages adjacent to a 1,3-alpha-D-galactosyl or N-acetylgalactosaminyl residues and a 1,2-alpha-D-fucosyl residue.
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Word Map
- 3.2.1.102
- epitope
-
xenotransplantation
- clostridium
-
alphagal
- perfringens
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galalpha1-3gal
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xenoantigenic
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hyperacute
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galalpha1-3galbeta1-4glcnac
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alpha-galactosyl
- saporin
- medicine
- analysis
The taxonomic range for the selected organisms is: Clostridium perfringens
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
endogalc, endo-beta-galactosidase c, abase, endo-beta-galactosidase dii, e-abase, sp3gh98, sp4gh98, gh98cbm51, inverting endo-beta-galactosidase, blood group glycotope-cleaving endo-beta-galactosidase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
endo-beta-galactosidase
galactosidase, endo-beta-
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additional information
endo-beta-galactosidase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
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SYSTEMATIC NAME
IUBMB Comments
blood-group-substance 4-beta-D-galactanohydrolase
Hydrolyses the 1,4-beta-D-galactosyl linkages adjacent to a 1,3-alpha-D-galactosyl or N-acetylgalactosaminyl residues and a 1,2-alpha-D-fucosyl residue.
CAS REGISTRY NUMBER
COMMENTARY
52720-51-1
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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
blood group A glycoconjugate + H2O
?
substrate from human erythrocytes and from porcine gastric mucin, liberation of the A trisaccharide GalNAcalpha(1-3)fucosealpha(1-2)galactose, product identification by NMR
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?
blood group B glycoconjugate + H2O
?
substrate from human erythrocytes and human ovarian cyst, liberation of the B trisaccharide Galalpha(1-3)fucosealpha(1-2)galactose, product identification by NMR
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?
2,4-dinitrophenyl 2-acetamido-2-deoxy-D-galactopyranosyl-(1,3)-[alpha-L-fucopyranosyl-(1,2)]-beta-D-galactopyranoside + H2O
?
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?
Galalpha(1-3)[Fucalpha(1-2)]Galbeta(1-4)GlcNAcbeta-CH2-CH2-N3 + H2O
?
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analog of blood group B antigen
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-
?
Galalpha(1-3)[Fucalpha(1-2)]Galbeta(1-4)GlcNAcbeta-R + H2O
Galalpha(1-3)[Fucalpha(1-2)]Gal + GlcNAcbeta-R
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analog of blood group B antigen, digested more effciently than the blood group A analog
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?
Galalpha1-3Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glc + H2O
Galalpha1-3Galbeta + GlcNAcbeta1-3Galbeta1-4Glc
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-
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?
GalNAcalpha(1-3)[Fucalpha(1-2)]Galbeta(1-4)GlcNAcbeta-CH2-CH2-N3 + H2O
?
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analog of blood group A antigen
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-
?
GalNAcalpha(1-3)[Fucalpha(1-2)]Galbeta(1-4)GlcNAcbeta-R + H2O
GalNAcalpha(1-3)[Fucalpha(1-2)]Gal + GlcNAcbeta-R
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analog of blood group A antigen
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additional information
?
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endo-beta-galactosidase C cleaves Galbeta1-4GlcNAc linkage and is capable of digesting alphaGal epitopes comprising two galactosyl residues at the distal end of the glycan
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NATURAL SUBSTRATE
NATURAL 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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.064 - 0.61
2,4-dinitrophenyl 2-acetamido-2-deoxy-D-galactopyranosyl-(1,3)-[alpha-L-fucopyranosyl-(1,2)]-beta-D-galactopyranoside
0.064
2,4-dinitrophenyl 2-acetamido-2-deoxy-D-galactopyranosyl-(1,3)-[alpha-L-fucopyranosyl-(1,2)]-beta-D-galactopyranoside
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wild type enzyme, at pH 6.0 and 37°C
0.31
2,4-dinitrophenyl 2-acetamido-2-deoxy-D-galactopyranosyl-(1,3)-[alpha-L-fucopyranosyl-(1,2)]-beta-D-galactopyranoside
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mutant enzyme E354A, at pH 6.0 and 37°C
0.59
2,4-dinitrophenyl 2-acetamido-2-deoxy-D-galactopyranosyl-(1,3)-[alpha-L-fucopyranosyl-(1,2)]-beta-D-galactopyranoside
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mutant enzyme E467A, at pH 6.0 and 37°C
0.61
2,4-dinitrophenyl 2-acetamido-2-deoxy-D-galactopyranosyl-(1,3)-[alpha-L-fucopyranosyl-(1,2)]-beta-D-galactopyranoside
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mutant enzyme D429A, at pH 6.0 and 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.17 - 1.75
2,4-dinitrophenyl 2-acetamido-2-deoxy-D-galactopyranosyl-(1,3)-[alpha-L-fucopyranosyl-(1,2)]-beta-D-galactopyranoside
0.17
2,4-dinitrophenyl 2-acetamido-2-deoxy-D-galactopyranosyl-(1,3)-[alpha-L-fucopyranosyl-(1,2)]-beta-D-galactopyranoside
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mutant enzyme E354A, at pH 6.0 and 37°C
1.35
2,4-dinitrophenyl 2-acetamido-2-deoxy-D-galactopyranosyl-(1,3)-[alpha-L-fucopyranosyl-(1,2)]-beta-D-galactopyranoside
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mutant enzyme D429A, at pH 6.0 and 37°C
1.55
2,4-dinitrophenyl 2-acetamido-2-deoxy-D-galactopyranosyl-(1,3)-[alpha-L-fucopyranosyl-(1,2)]-beta-D-galactopyranoside
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mutant enzyme E467A, at pH 6.0 and 37°C
1.75
2,4-dinitrophenyl 2-acetamido-2-deoxy-D-galactopyranosyl-(1,3)-[alpha-L-fucopyranosyl-(1,2)]-beta-D-galactopyranoside
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wild type enzyme, at pH 6.0 and 37°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5.33 - 26.67
2,4-dinitrophenyl 2-acetamido-2-deoxy-D-galactopyranosyl-(1,3)-[alpha-L-fucopyranosyl-(1,2)]-beta-D-galactopyranoside
5.33
2,4-dinitrophenyl 2-acetamido-2-deoxy-D-galactopyranosyl-(1,3)-[alpha-L-fucopyranosyl-(1,2)]-beta-D-galactopyranoside
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mutant enzyme E354A, at pH 6.0 and 37°C
21.67
2,4-dinitrophenyl 2-acetamido-2-deoxy-D-galactopyranosyl-(1,3)-[alpha-L-fucopyranosyl-(1,2)]-beta-D-galactopyranoside
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mutant enzyme D429A, at pH 6.0 and 37°C
26.67
2,4-dinitrophenyl 2-acetamido-2-deoxy-D-galactopyranosyl-(1,3)-[alpha-L-fucopyranosyl-(1,2)]-beta-D-galactopyranoside
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mutant enzyme E467A, at pH 6.0 and 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
2-3fold preference for blood group A antigen
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
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endo-beta-galactosidase C overexpression results in accelerated proliferation of mouse NIH3T3 fibroblasts
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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the enzyme contains a central catalytic TIM barrel domain, the GH98 catalytic domain, and two other domains, domain organization, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D429A
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the mutants shows reduced activity compared to the wild type enzyme
E354A
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the activity of the E354A mutant with nonactivated natural substrates is 1100fold lower than that of the wild type enzyme, while its activity is only 10fold lower when assayed with 2,4-dinitrophenyl-beta-A-trisaccharide
E467A
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the mutants shows slightly reduced activity compared to the wild type enzyme
additional information
additional information
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mice expressing the enzyme systemically have rough and flaky skin which becomes detectable around 5 days after birth and becomes obscure by 2 weeks after birth. In transgenic mice, proliferating keratinocytes increase approximately 3fold in epidermis compared to wild-type. In transgenic epidermis, the expression domain of cytokeratin 14 increases from 1-2 layers to 4-5 layers and co-expresses with cytokeratin 6 and 10 in the upper layers. Transgenic mice also show delayed development of the barrier function around 8 days postnatal, and acquire the function by 12 days postnatal
additional information
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transgenic expression of enzyme in mouse results in dramaitc reduction in the expression of the alphaGal epitope. Mice show abnormal phenotypes, such as occasional death immediately after birth, growth retardation, and transient skin lesions
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme from strain ATCC 10543, by gel filtration, ion exchange, adsorption, and concanavalin A affinity chromatography, and another step of ion exchange chromatography, 2630fold to homogeneity, recombinant His-tagged enzyme by nickel affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene eabC, DNA and amino acid sequence determination and analysis, functional overexpression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
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the absence of the alphaGal epitope or the exposed N-acetylglucosamine terminal in transgenic mice expressing the enzyme can play a critical role in the proliferation of basal keratinocytes and differentiation of them into the spinous cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ogawa, H.; Muramatsu, H.; Kobayashi, T.; Morozumi, K.; Yokoyama, I.; Kurosawa, N.; Nakao, A.; Muramatsu, T.
Molecular cloning of endo-beta-galactosidase C and its application in removing alpha-galactosyl xenoantigen from blood vessels in the pig kidney
J. Biol. Chem.
275
19368-19374
2000
Clostridium perfringens
Rigden, D.J.
Analysis of glycoside hydrolase family 98: catalytic machinery, mechanism and a novel putative carbohydrate binding module
FEBS Lett.
579
5466-5472
2005
Clostridium perfringens
Anderson, K.M.; Ashida, H.; Maskos, K.; Dell, A.; Li, S.C.; Li, Y.T.
A clostridial endo-beta-galactosidase that cleaves both blood group A and B glycotopes: the first member of a new glycoside hydrolase family, GH98
J. Biol. Chem.
280
7720-7728
2005
Clostridium perfringens (Q6RUF5), Clostridium perfringens, Clostridium perfringens ATCC 10543 (Q6RUF5), Clostridium perfringens ATCC 10543
Misawa, M.; Watanabe, S.; Ihara, S.; Muramatsu, T.; Matsuzaki, T.
Accelerated proliferation and abnormal differentiation of epidermal keratinocytes in endo-beta-galactosidase C transgenic mice
Glycobiology
18
20-27
2008
Clostridium perfringens
Watanabe, S.; Misawa, M.; Matsuzaki, T.; Sakurai, T.; Muramatsu, T.; Yokomine, T.A.; Sato, M.
Production and characterization of transgenic mice systemically expressing endo-beta-galactosidase C
Glycobiology
18
9-19
2008
Clostridium perfringens
Gregg, K.J.; Finn, R.; Abbott, D.W.; Boraston, A.B.
Divergent modes of glycan recognition by a new family of carbohydrate-binding modules
J. Biol. Chem.
283
12604-12613
2008
Clostridium perfringens
Kobayashi, T.; Liu, D.; Ogawa, H.; Miwa, Y.; Nagasaka, T.; Maruyama, S.; Li, Y.T.; Onishi, A.; Iwamoto, M.; Kuzuya, T.; Kadomatsu, K.; Uchida, K.; Nakao, A.
Removal of blood group A/B antigen in organs by ex vivo and in vivo administration of endo-beta-galactosidase (ABase) for ABO-incompatible transplantation
Transpl. Immunol.
20
132-138
2009
Clostridium perfringens
Shaikh, F.A.; Randriantsoa, M.; Withers, S.G.
Mechanistic analysis of the blood group antigen-cleaving endo-beta-galactosidase from Clostridium perfringens
Biochemistry
48
8396-8404
2009
Clostridium perfringens
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