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Information on EC 3.2.1.103 - keratan-sulfate endo-1,4-beta-galactosidase
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EC Tree
3.2.1.103 keratan-sulfate endo-1,4-beta-galactosidaseIUBMB Comments
Hydrolyses the 1,4-beta-D-galactosyl linkages adjacent to 1,3-N-acetyl-alpha-D-glucosaminyl residues. Also acts on some non-sulfated oligosaccharides, but only acts on blood group substances when the 1,2-linked fucosyl residues have been removed (cf. EC 3.2.1.102 blood-group-substance endo-1,4-beta-galactosidase).
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Word Map
- 3.2.1.103
- proteoglycans
- chondroitinase
- chondroitin
- glycosaminoglycans
- cartilage
- hyaluronidase
- dermatan
- heparitinase
-
interglobular
-
endo-beta-d-galactosidase
-
35ssulphate
-
sulphate-rich
-
fuchsin
-
cupromeronic
-
kspgs
- analysis
- medicine
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
Synonyms
keratanase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
endo-beta-galactosidase
galactosidase, keratosulfate endo- beta-
-
-
-
-
keratan sulfate endogalactosidase
-
-
-
-
keratanase
endo-beta-galactosidase
-
-
-
-
keratanase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(Galbeta(1-4)GlcNAcbeta(1-3))n + H2O = (Galbeta(1-4)GlcNAcbeta(1-3))n-m + (Galbeta(1-4)GlcNAcbeta(1-3))m
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
keratan-sulfate 4-beta-D-galactanohydrolase
Hydrolyses the 1,4-beta-D-galactosyl linkages adjacent to 1,3-N-acetyl-alpha-D-glucosaminyl residues. Also acts on some non-sulfated oligosaccharides, but only acts on blood group substances when the 1,2-linked fucosyl residues have been removed (cf. EC 3.2.1.102 blood-group-substance endo-1,4-beta-galactosidase).
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CAS REGISTRY NUMBER
COMMENTARY
55072-01-0
-
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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
Fucalpha1-2Galbeta1-3GlcNAcbeta1-3Galbeta1-4Glc + H2O
?
-
-
-
-
?
Fucalpha1-2Galbeta1-3GlcNAcbeta1-3Galbeta1-4Glc-Cer + H2O
Fucalpha1-2Galbeta1-3GlcNAcbeta1-3Gal + Glc-Cer
Gal(beta1-4)GlcNAc(beta1-3)Gal(beta1-4)sorbitol + H2O
Gal(beta1-4)GlcNAc(beta1-3)Gal + sorbitol
-
-
-
?
Galbeta1-3GlcNAc(6-2alphaNeuAc)beta1-3Galbeta1-4Glc + H2O
?
-
-
-
-
?
Galbeta1-3[Fucalpha1-4]GlcNAcbeta1-3Galbeta1-4Glc-Cer + H2O
Galbeta1-3[Fucalpha1-4]GlcNAcbeta1-3Gal + Glc-Cer
Galbeta1-4GlcNAcbeta1-3Galbeta1-3Galbeta1-4Glc-Cer + H2O
Galbeta1-4GlcNAcbeta1-3Galbeta1-3Gal + Glc-Cer
glycosphingolipids + H2O
?
-
lacto-N-glycosylceramide series having the common structure R-GlcAcbeta1-3Galbeta1-4Glc(or GlcNAc) are hydrolyzed at Galbeta1-4Glc (or GlcNAC) linkages. beta-Galactosyl linkages in globo series or ganglio series of glycolipids are not hydrolyzed
-
-
?
lacto-N-tetraitol + H2O
sorbitol + Galbeta(1-3)GlcNAcbeta(1-3)Gal
-
-
-
?
mucin + H2O
GlcNAcbeta(1-3)Gal + GlcNAc-6Sbeta(1-3)Gal + resistant polymer
-
desialyzed pig colonic mucin
-
?
NeuAcalpha2-3Galbeta1-3GlcNAc(6-2alphaNeuAc)beta1-3Galbeta1-4Glc + H2O
?
-
-
-
-
?
NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glc-Cer + H2O
NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-3Gal + Glc-Cer
NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-4Galbeta1-3GlcNAcbeta1-3Galbeta1-4Glc-Cer + H2O
NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-4Galbeta1-3GlcNAcbeta1-3Gal + Glc-Cer
NeuAcalpha2-6Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glc + H2O
?
-
-
-
-
?
polyglycosylceramides + H2O
?
-
in absence of sodium taurodeoxycholate conversion into at least three shorter-chain glycosphingolipids, in presence of sodium taurodeoxycholate conversion into glucosylceramide
in absence of sodium taurodeoxycholate conversion into at least three shorter-chain glycosphingolipids, in presence of sodium taurodeoxycholate conversion into glucosylceramide
?
sulfated glycosaminoglycan + H2O
N-acetyl-D-glucosamine-6-sulfate + ?
-
pH 6.8
-
-
?
Fucalpha1-2Galbeta1-3GlcNAcbeta1-3Galbeta1-4Glc-Cer + H2O
Fucalpha1-2Galbeta1-3GlcNAcbeta1-3Gal + Glc-Cer
-
-
-
?
Fucalpha1-2Galbeta1-3GlcNAcbeta1-3Galbeta1-4Glc-Cer + H2O
Fucalpha1-2Galbeta1-3GlcNAcbeta1-3Gal + Glc-Cer
-
-
-
?
Galalpha1-3Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glc-Cer + H2O
?
-
-
-
-
?
Galalpha1-3Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glc-Cer + H2O
?
-
no activity
-
-
?
Galalpha1-3Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glc-Cer + H2O
?
-
-
-
-
?
Galbeta1-3[Fucalpha1-4]GlcNAcbeta1-3Galbeta1-4Glc + H2O
?
-
-
-
-
?
Galbeta1-3[Fucalpha1-4]GlcNAcbeta1-3Galbeta1-4Glc-Cer + H2O
Galbeta1-3[Fucalpha1-4]GlcNAcbeta1-3Gal + Glc-Cer
-
-
-
?
Galbeta1-3[Fucalpha1-4]GlcNAcbeta1-3Galbeta1-4Glc-Cer + H2O
Galbeta1-3[Fucalpha1-4]GlcNAcbeta1-3Gal + Glc-Cer
-
-
-
?
Galbeta1-4GlcNAcbeta1-3Galbeta1-3Galbeta1-4Glc-Cer + H2O
Galbeta1-4GlcNAcbeta1-3Galbeta1-3Gal + Glc-Cer
-
-
-
?
Galbeta1-4GlcNAcbeta1-3Galbeta1-3Galbeta1-4Glc-Cer + H2O
Galbeta1-4GlcNAcbeta1-3Galbeta1-3Gal + Glc-Cer
-
-
-
?
Galbeta1-4GlcNAcbeta1-3Galbeta1-3Galbeta1-4Glc-Cer + H2O
Galbeta1-4GlcNAcbeta1-3Galbeta1-3Gal + Glc-Cer
-
-
-
-
?
keratan sulfate + H2O
keratan oligosaccharides
-
from bovine cornea
-
-
?
keratan sulfate + H2O
keratan oligosaccharides
-
from bovine cornea
more than 75% of the oligosaccharides are sulfated unbranched poly(N-acetyllactosamine) sequences, (-3/4GlcNAcbeta1-3Galbeta1-)n. SO3-beta1-3Gal accounts for almost 35% of the oligosaccharide material while 40% consists of four oligosaccharides, unbranched tetrasaccharides, hexasaccharides, octasaccharides and decasaccharides of poly(N-acetyllactosamine)type, having 3, 5, 7 and 9 sulfate residues respectively. A sulfate residue is attached to the C6 position of each N-acetylglucosamine and each internal galactose residue of the four oligosaccharides
?
keratan sulfate + H2O
keratan oligosaccharides
-
from bovine cornea
GlcNAcbeta1-3Gal + sulfated disaccharides, trisaccharides, tetrasaccharides, hexasaccharides, octasaccharides and decasaccharides based on the sequence (-3/4GlcNAcbeta1-3Galbeta1-), having 1, 3, 5, 7 and 9 sulfate groups
?
keratan sulfate + H2O
keratan oligosaccharides
-
-
6-O-sulfo-GlcNAcbeta1-3Gal is the major product
?
keratan sulfate + H2O
keratan oligosaccharides
-
-
2-acetamido-2-deoxy-6-O-sulfo-beta-D-Gal-(1-3)-D-Gal + 2-acetamido-2-deoxy-6-O-sulfo-beta-D-Glc-(1-3)-6-O-sulfoD-Gal-(1-4)-2-acetamido-2-deoxy-6-O-sulfo-beta-D-Glc-(1-3)-D-Gal
?
keratan sulfate + H2O
keratan oligosaccharides
-
from teleost skin
6-O-sulfo-GlcNAcbeta1-3Gal is one of the major products, GlcNAcbeta1-3Gal
?
keratan sulfate + H2O
keratan oligosaccharides
-
from teleost skin
no production of GlcNAcbeta1-3Gal, 6-O-sulfo-GlcNAcbeta1-3Gal is one of the major products
?
keratan sulfate + H2O
keratan oligosaccharides
-
keratan sulfate chains from bovine articular cartilage. Presence of fucose on N-acetylglucosamine residues in keratan sulfates protects both of the adjacent unsulfated galactose residues from keratanase cleavage
GlcNAc(6S)beta1-3Galbeta1-4(Fucalpha1-3)GlcNAc(6S)beta1-3Galbeta1-4GlcNAc(6S)beta1-3Gal-ol + GlcNAc(6S)beta1-3Galbeta1-4(Fucalpha-3)GlcNAc(6S)beta1-3Galbeta1-4GlcNAc(6S)beta1-6(Galbeta1-33)GalNAc-ol
?
keratan sulfate + H2O
keratan oligosaccharides
-
from nasal carilage
-
-
?
keratan sulfate + H2O
keratan oligosaccharides
-
from teleost skin
6-O-sulfo-GlcNAcbeta1-3Gal is one of the major products, GlcNAcbeta1-3Gal
?
lacto-N-tetraose + H2O
glucose + Galbeta(1-3)GlcNAcbeta(1-3)Gal
-
-
-
?
lacto-N-tetraose + H2O
glucose + Galbeta(1-3)GlcNAcbeta(1-3)Gal
-
-
-
-
?
neolacto-type glycosphingolipid + H2O
glucosylceramide + ?
-
hydrolysis of the internal beta1,4-galactosyl linkage of various neolacto-type glycosphingolipids to produce glucosylceramides
-
?
neolacto-type glycosphingolipid + H2O
glucosylceramide + ?
-
hydrolysis of the internal beta1,4-galactosyl linkage of various neolacto-type glycosphingolipids to produce glucosylceramides
-
?
NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glc-Cer + H2O
NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-3Gal + Glc-Cer
-
-
-
?
NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glc-Cer + H2O
NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-3Gal + Glc-Cer
-
-
-
?
NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glc-Cer + H2O
NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-3Gal + Glc-Cer
-
-
-
-
?
NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glc-Cer + H2O
NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-3Gal + Glc-Cer
-
-
-
?
NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-4Galbeta1-3GlcNAcbeta1-3Galbeta1-4Glc-Cer + H2O
NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-4Galbeta1-3GlcNAcbeta1-3Gal + Glc-Cer
-
-
-
?
NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-4Galbeta1-3GlcNAcbeta1-3Galbeta1-4Glc-Cer + H2O
NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-4Galbeta1-3GlcNAcbeta1-3Gal + Glc-Cer
-
no activity
-
-
?
NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-4Galbeta1-3GlcNAcbeta1-3Galbeta1-4Glc-Cer + H2O
NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-4Galbeta1-3GlcNAcbeta1-3Gal + Glc-Cer
-
-
-
?
additional information
?
-
-
hydrolyzes the type 2 sequence Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glc at about twice the rate of the type 1 isomer, Galbeta1-3GlcNAcbeta1-3Galbeta1-4Glc
-
-
?
additional information
?
-
-
no activity with Galbeta1-4GlcNAcbeta1-6Galbeta1-4GlcNAcbeta1-6(Galbeta1-3)GalNAc-ol
-
-
?
additional information
?
-
-
AB active blood group substance can be hydrolyzed only after Smith degradation
-
-
?
additional information
?
-
-
induced with high efficiency in culture medium containing Smith-degraded gastric mucin
-
-
?
additional information
?
-
-
sialosyl substitution at the terminal galactosyl residue of lacto-N-neotetraosyl structure of paragloboside greatly enhances the hydrolyzability of the internal Galbeta1-4Glc linkage, thus producing a high yield of sialotetrasaccharide (AcNeualpha2-3Galbeta1-4GlcNAcbeta-3Gal). The Galbeta1-4GlcNAc linkage located in the middle of the repeating Galbeta1-4GlcNAc(or Glc) unit seen in H2-glycolipid or Ab-glycolipid, (R-Galbeta1-4GlcNAcbeta1-3Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glc-Cer) is preferentially hydrolyzed relative to the Galbeta1-4Glc linkage directly attached to ceramide. The branched structure as is found in H3-glycolipid greatly reduces the hydrolyzability
-
-
?
additional information
?
-
-
hydrolyzes glycoconjugates containing N-acetyllactosamine repeating units
-
-
?
additional information
?
-
-
the enzyme is produced without induction by keratan sulfate
-
-
?
additional information
?
-
-
the enzyme is produced without induction by keratan sulfate
-
-
?
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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
additional information
?
-
-
induced with high efficiency in culture medium containing Smith-degraded gastric mucin
-
-
?
additional information
?
-
-
the enzyme is produced without induction by keratan sulfate
-
-
?
additional information
?
-
-
the enzyme is produced without induction by keratan sulfate
-
-
?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Galbeta1-4GlcNAcbeta1-3Gal
-
when assayed with lacto-N-neotetraosylceramide
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Arthritis
Immunity to the G1 globular domain of the cartilage proteoglycan aggrecan can induce inflammatory erosive polyarthritis and spondylitis in BALB/c mice but immunity to G1 is inhibited by covalently bound keratan sulfate in vitro and in vivo.
Carcinoma
Simultaneous expression of keratan sulphate epitope (a sulphated poly-N-acetyllactosamine) and blood group ABH antigens in papillary carcinomas of the human thyroid gland.
Mucopolysaccharidosis IV
Development of Substrate Degradation Enzyme Therapy for Mucopolysaccharidosis IVA Murine Model.
Neoplasms
Simultaneous expression of keratan sulphate epitope (a sulphated poly-N-acetyllactosamine) and blood group ABH antigens in papillary carcinomas of the human thyroid gland.
Rheumatic Diseases
Cellular immunity to the G1 domain of cartilage proteoglycan aggrecan is enhanced in patients with rheumatoid arthritis but only after removal of keratan sulfate.
Spondylitis
Immunity to the G1 globular domain of the cartilage proteoglycan aggrecan can induce inflammatory erosive polyarthritis and spondylitis in BALB/c mice but immunity to G1 is inhibited by covalently bound keratan sulfate in vitro and in vivo.
Teratocarcinoma
The linear tetrasaccharide, Gal beta 1-4GlcNAc beta 1-6Gal beta 1-4GlcNAc, isolated from radiolabeled teratocarcinoma poly-N-acetyllactosaminoglycan resists the action of E. freundii endo-beta-galactosidase.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 5.8
5.5 - 5.8
-
hydrolysis of keratan sulfate from nasal cartilage or Galalpha1-3Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glc-Cer
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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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). A0A644ZTS8_9ZZZZ
256
0
29595
TrEMBL
other Location (Reliability: 2)
J9FV79_9ZZZZ
1069
0
118335
TrEMBL
Secretory Pathway (Reliability: 2)
A0A644YZZ6_9ZZZZ
262
0
30703
TrEMBL
Secretory Pathway (Reliability: 2)
K1UHZ9_9ZZZZ
223
0
25315
TrEMBL
other Location (Reliability: 1)
A0A644V8P9_9ZZZZ
273
0
31508
TrEMBL
Secretory Pathway (Reliability: 4)
A0A385ZYB8_9ACTN
826
1
83932
TrEMBL
-
K1TDD7_9ZZZZ
272
0
30508
TrEMBL
other Location (Reliability: 2)
K1TCY9_9ZZZZ
210
0
23781
TrEMBL
other Location (Reliability: 1)
A0A1R3T9X1_9BACT
262
0
29416
TrEMBL
-
K1T433_9ZZZZ
197
0
21832
TrEMBL
Secretory Pathway (Reliability: 1)
J9G5K6_9ZZZZ
1037
0
115342
TrEMBL
Mitochondrion (Reliability: 4)
K1U4Z6_9ZZZZ
144
0
16674
TrEMBL
other Location (Reliability: 4)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5 - 5.5
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
37
-
1 h, 50% loss of activity, bovine serum albumin, 0.4 mg/ml, prevents inactivation
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, stable for at least 2-3 months at a protein concentration of 0.044 mg/ml protein, 20% loss of activity in 3 h at a protein concentration of 0.003 mg/ml
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
analysis
-
useful for studying the structure of glycoproteins and oligosaccharides
analysis
-
the enzyme can be used to distinguish between GlcNAcbeta1-6Gal and GlcNAcbeta1-3Gal units within linear backbone sequences of all known types of oligo-(N-acetyllactosamino)glycans
analysis
-
enzyme can be useful in studying the precise structures of keratan sulfates, related glycoproteins and oligosaccharides
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Maaheimo, H.; Penttil, L.; Renkonen, O.
Enzyme-aided construction of medium-sized alditols of complete O-linked saccharides. The constructed hexasaccharide alditol Galbeta1-4GlcNAcbeta1-6Galbeta1-4GlcNAcbeta1-6(Galbeta1-3)GalNAc-ol resists the action of endo-beta-galactosidase from Bacteroides fragilis
FEBS Lett.
349
55-59
1994
Bacteroides fragilis
brenda
Leng, L.; Zhu, A.; Zhang, Z.; Hurst, R.; Goldstein, J.
Cloning, functional expression and purification of endo-beta-galactosidase from Flavobacterium keratolyticus
Gene
222
187-194
1998
Sphingobacterium multivorum
brenda
Fukuda, M.; Matsumara, G.
endo-beta-Galactosidase of Escherichia freundii. Hydrolysis of pig colonic mucin and milk oligosaccharides by endoglycosidic action
Biochem. Biophys. Res. Commun.
64
465-471
1975
Citrobacter freundii
brenda
Fukuda, M.; Watanabe, K.; Hakomori, S.I.
Release of oligosaccharides from various glycosphingolipids by endo-beta-galactosidase
J. Biol. Chem.
253
6814-6819
1978
Escherichia coli
brenda
Fukuda, M.
Purification and characterization of endo-beta-galactosidase from Escherichia freundii induced by hog gastric mucin
J. Biol. Chem.
256
3900-3905
1981
Citrobacter freundii
brenda
Nakagawa, H.; Yamada, T.; Chien, J.L.; Gardas, A.; Kitamikado, M.; Li, S.C.; Li, Y.T.
Isolation and characterization of an endo-beta-galactosidase from a new strain of Escherichia freundii
J. Biol. Chem.
255
5955-5959
1980
Citrobacter freundii
brenda
Kitamikado, M.; Ito, M.; Li, Y.T.
Isolation and characterization of a keratan sulfate-degrading endo-beta-galactosidase from Flavobacterium keratolyticus
J. Biol. Chem.
256
3906-3909
1981
Sphingobacterium multivorum
brenda
Kitamikado, M.; Ito, M.; Li, Y.T.
endo-beta-Galactosidase from Flavobacterium keratolyticus
Methods Enzymol.
83
619-625
1982
Sphingobacterium multivorum
brenda
Li, Y.T.; Nakagawa, H.; Kitamikado, M.; Li, S.C.
endo-beta-Galactosidase from Escherichia freundii
Methods Enzymol.
83
610-619
1982
Citrobacter freundii
brenda
Scudder, P.; Uemura, K.i.; Dolby, J.; Fukuda, M.N.; Feizi, T.
Isolation and characterization of an endo-beta-galactosidase from Bacteroides fragilis
Biochem. J.
213
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1983
Bacteroides fragilis
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brenda
Hounsell, E.F.; Feeney, J.; Scudder, P.; Tang, P.W.; Feizi, T.
1H-NMR studies at 500 MHz of a neutral disaccharide and sulphated di-, tetra-, hexa- and larger oligosaccharides obtained by endo-beta-galactosidase treatment of keratan sulphate
Eur. J. Biochem.
157
375-384
1986
Bacteroides fragilis
brenda
Scudder, P.; Tang, P.W.; Hounsell, E.F.; Lawson, A.M.; Mehemet, H.; Feizi, T.
Isolation and characterization of sulphated oligosaccharides released from bovine corneal keratan sulphate by the action of endo-beta-galactosidase
Eur. J. Biochem.
157
365-373
1986
Bacteroides fragilis
brenda
Ito, M.; Hirabayashi, Y.; Yamagata, T.
Substrate specificity of endo-beta-galactosidases from Flavobacterium keratolyticus and Escherichia freundii is different from that of Pseudomonas sp.
J. Biochem.
100
773-780
1986
Citrobacter freundii, Pseudomonas sp., Sphingobacterium multivorum
brenda
Fukuda, M.N.; Matsumura, G.
endo-beta-Galactosidase of Escherichia freundii. Purification and endoglycosidic action on keratan sulfates, oligosaccharides, and blood group active glycoprotein
J. Biol. Chem.
251
6218-6225
1976
Citrobacter freundii
brenda
Tai, G.H.; Huckerby, T.N.; Nieduszynski, A.
N.m.r. spectroscopic studies of fucose-containing oligosaccharides derived from keratanase digestion of articular cartilage keratan sulphates. Influence of fucose residues on keratanase cleavage
Biochem. J.
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1993
Pseudomonas sp.
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brenda
Akhtar, S.; Kerr, B.C.; Hayes, A.J.; Hughes, C.E.; Meek, K.M.; Caterson, B.
Immunochemical localization of keratan sulfate proteoglycans in cornea, sclera, and limbus using a keratanase-generated neoepitope monoclonal antibody
Invest. Ophthalmol. Vis. Sci.
49
2424-2431
2008
Homo sapiens
brenda
Fosang, A.J.; Last, K.; Poon, C.J.; Plaas, A.H.
Keratan sulphate in the interglobular domain has a microstructure that is distinct from keratan sulphate elsewhere on pig aggrecan
Matrix Biol.
28
53-61
2009
Citrobacter freundii
brenda
Kershaw-Young, C.M.; Stuart, C.; Evans, G.; Maxwell, W.M.
The effect of glycosaminoglycan enzymes and proteases on the viscosity of alpaca seminal plasma and sperm function
Anim. Reprod. Sci.
138
261-267
2013
Pseudomonas sp.
brenda
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