Any feedback?
Information on EC 4.2.2.5 - chondroitin AC lyase and Organism(s) Pedobacter heparinus and UniProt Accession Q59288
for references in articles please use BRENDA:EC4.2.2.5Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
4.2.2.5 chondroitin AC lyaseIUBMB Comments
Acts on chondroitin 4-sulfate and chondroitin 6-sulfate, but less well on hyaluronate. In general, chondroitin sulfate (CS) and dermatan sulfate (DS) chains comprise a linkage region, a chain cap and a repeat region. The repeat region of CS is a repeating disaccharide of glucuronic acid (GlcA) and N-acetylgalactosamine (GalNAc) [-4)GlcA(beta1-3)GalNAc(beta1-]n, which may be O-sulfated on the C-4 and/or C-6 of GalNAc and C-2 of GlcA. GlcA residues of CS may be epimerized to iduronic acid (IdoA) forming the repeating disaccharide [-4)IdoA(alpha1-3)GalNAc(beta1-]n of DS. Both the concentrations and locations of sulfate-ester substituents vary with glucosaminoglycan source .
Specify your search results
Word Map
- 4.2.2.5
- glycosaminoglycans
- proteoglycans
- dermatan
- heparan
-
hyaluronic
- hyaluronidase
-
glucuronic
- heparinum
- flavobacterium
- heparitinase
- 6-sulfate
- lyases
-
iduronic
-
4-sulphate
-
glca
-
cetylpyridinium
- hexasaccharide
-
monosulfated
-
cuprolinic
-
3hglucosamine
- galactosaminoglycans
- aurescens
-
undersulfated
-
oversulfated
- keratanase
-
35ssulfate
- analysis
- medicine
- synthesis
-
trisulfated
-
blue-positive
- chondroitin-4-sulfate
- food industry
-
cupromeronic
The taxonomic range for the selected organisms is: Pedobacter heparinus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
Synonyms
chondroitinase ac, chondroitin ac lyase, chondroitinase acii, chnac, chondroitin sulfate lyase, chondroitin lyase ac, c-aci, chondroitin acii lyase, ac i lyase, chondroitin ac i lyase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
A-Chase
-
-
-
-
chondroitin AC eliminase
-
-
-
-
Chondroitin AC lyase
chondroitin sulfate lyase
-
-
-
-
chondroitinase
-
-
-
-
chondroitinase AC
ChSase-AC
-
-
-
-
F-Chase
-
-
-
-
lyase, chondroitin AC
-
-
-
-
Chondroitin AC lyase
-
-
-
-
chondroitinase AC
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Eliminative degradation of polysaccharides containing 1,4-beta-D-hexosaminyl and 1,3-beta-D-glucuronosyl linkages to disaccharides containing 4-deoxy-beta-D-gluc-4-enuronosyl groups
Eliminative degradation of polysaccharides containing 1,4-beta-D-hexosaminyl and 1,3-beta-D-glucuronosyl linkages to disaccharides containing 4-deoxy-beta-D-gluc-4-enuronosyl groups
Eliminative degradation of polysaccharides containing 1,4-beta-D-hexosaminyl and 1,3-beta-D-glucuronosyl linkages to disaccharides containing 4-deoxy-beta-D-gluc-4-enuronosyl groups
acts on chondroitin 4-sulfate and chondroitin 6-sulfate, but less well on hyaluronate
Eliminative degradation of polysaccharides containing 1,4-beta-D-hexosaminyl and 1,3-beta-D-glucuronosyl linkages to disaccharides containing 4-deoxy-beta-D-gluc-4-enuronosyl groups
acts on chondroitin 4-sulfate and chondroitin 6-sulfate, but less well on hyaluronate, mechanism, active site structure, His225, Tyr234, Arg288, and Glu371 form a catalytic tetrad
Eliminative degradation of polysaccharides containing 1,4-beta-D-hexosaminyl and 1,3-beta-D-glucuronosyl linkages to disaccharides containing 4-deoxy-beta-D-gluc-4-enuronosyl groups
random attack
-
Eliminative degradation of polysaccharides containing 1,4-beta-D-hexosaminyl and 1,3-beta-D-glucuronosyl linkages to disaccharides containing 4-deoxy-beta-D-gluc-4-enuronosyl groups
acts on chondroitin 4-sulfate and chondroitin 6-sulfate, but less well on hyaluronate
-
Eliminative degradation of polysaccharides containing 1,4-beta-D-hexosaminyl and 1,3-beta-D-glucuronosyl linkages to disaccharides containing 4-deoxy-beta-D-gluc-4-enuronosyl groups
acts on chondroitin 4-sulfate and chondroitin 6-sulfate, but less well on hyaluronate, random endolytic elimination mechanism
-
Eliminative degradation of polysaccharides containing 1,4-beta-D-hexosaminyl and 1,3-beta-D-glucuronosyl linkages to disaccharides containing 4-deoxy-beta-D-gluc-4-enuronosyl groups
acts on chondroitin 4-sulfate and chondroitin 6-sulfate, but less well on hyaluronate, reaction mechanism
-
Eliminative degradation of polysaccharides containing 1,4-beta-D-hexosaminyl and 1,3-beta-D-glucuronosyl linkages to disaccharides containing 4-deoxy-beta-D-gluc-4-enuronosyl groups
acts on chondroitin 4-sulfate and chondroitin 6-sulfate, but less well on hyaluronate, stepwise reaction mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
elimination
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
chondroitin AC lyase
Acts on chondroitin 4-sulfate and chondroitin 6-sulfate, but less well on hyaluronate. In general, chondroitin sulfate (CS) and dermatan sulfate (DS) chains comprise a linkage region, a chain cap and a repeat region. The repeat region of CS is a repeating disaccharide of glucuronic acid (GlcA) and N-acetylgalactosamine (GalNAc) [-4)GlcA(beta1-3)GalNAc(beta1-]n, which may be O-sulfated on the C-4 and/or C-6 of GalNAc and C-2 of GlcA. GlcA residues of CS may be epimerized to iduronic acid (IdoA) forming the repeating disaccharide [-4)IdoA(alpha1-3)GalNAc(beta1-]n of DS. Both the concentrations and locations of sulfate-ester substituents vary with glucosaminoglycan source [4].
CAS REGISTRY NUMBER
COMMENTARY
9047-57-8
-
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
dermatan sulfate
?
wild-type enzyme and mutants R292A, and Y234F
-
?
heparan sulfate
?
wild-type enzyme and mutants R292A, R288A, and Y234F
-
?
hyaluronic acid
?
wild-type enzyme and mutants R292A, R288A, and Y234F
-
?
benzyl 4-O-(2'-nitrophenyl)-beta-D-glucopyranosiduronic acid
?
-
synthetic chromogenic substrate
-
?
benzyl 4-O-(3',4'-dinitrophenyl)-beta-D-glucopyranosiduronic acid
?
-
synthetic chromogenic substrate
-
?
benzyl 4-O-(4'-chloro-2'-nitrophenyl)-beta-D-glucopyranosiduronic acid
?
-
synthetic chromogenic substrate
-
?
benzyl S-(2-acetamido-2-deoxy-beta-D-galactopyranosyl)-(1-4)-4-deoxy-4-thio-beta-D-glucopyranosiduronic acid
?
-
very slow cleavage, 9% product after 24 h
-
-
?
chondroitin 4-sulfate
2-acetamido-2-deoxy-3-O-(beta-D-gluco-4-enepyranosyluronic acid)-4-O-sulfo-D-galactose
chondroitin sulfate A
unsaturated chondroitin A sulfate disaccharide
-
i.e. chondroitin 4-sulfate
-
?
chondroitin sulfate C
unsaturated chondroitin sulfate C disaccharide
-
i.e. chondroitin 6-sulfate
product analysis
?
chondroitin sulfate/dermatan sulfate chain
?
-
chondroitin AC I lyase cleaves the linkage between GalNAc and D-GlcA, with the formation of a 4,5 double bond at HexA and a water molecule elimination
-
-
?
chondroitin/dermatan sulfate chain
?
-
chon-AC-lyase cleaves the linkage between GalNAc and D-GlcA
-
-
?
hyaluronate
?
-
degradation is faster than with chondroitin 4-sulfate or chondroitin 6-sulfate
-
-
?
methyl 4-deoxy-4-fluoro-beta-D-glucopyranosiduronic acid
?
-
synthetic chromogenic substrate
-
?
phenyl 4-O-(2',4'-dinitrophenyl)-beta-D-glucopyranosiduronic acid
?
-
-
-
-
?
proteoglycan
protein-keratan sulfate
-
-
the protein-keratan sulfate core isolated after limit digestion of proteoglycan contains about 44% protein, 38% keratan sulfate, and 18% of the enzymatically modified oligosaccharide attachment region between the chondroitin sulfate chains and protein core: gluco-4-enepyranosyluronic acid-(galactosyl)2-xylose
?
chondroitin sulfate A
?
i.e. chondroitin 4-sulfate, best substrate, wild-type enzyme and mutants R292A, R288A, H225A and Y234F
-
?
chondroitin sulfate C
?
i.e. chondroitin 6-sulfate, wild-type enzyme and mutants R292A, R288A, and Y234F
-
?
benzyl 4-deoxy-4-fluoro-beta-D-glucopyranosiduronic acid
?
-
synthetic chromogenic substrate
-
?
benzyl 4-deoxy-4-fluoro-beta-D-glucopyranosiduronic acid
?
-
synthetic chromogenic substrate
-
?
benzyl 4-O-(2',4'-dinitrophenyl)-beta-D-glucopyranosiduronic acid
?
-
synthetic chromogenic substrate
-
?
benzyl 4-O-(2',4'-dinitrophenyl)-beta-D-glucopyranosiduronic acid
?
-
synthetic chromogenic substrate
-
?
chondroitin
?
-
degradation is faster than with chondroitin 4-sulfate or chondroitin 6-sulfate
-
-
?
chondroitin 4-sulfate
2-acetamido-2-deoxy-3-O-(beta-D-gluco-4-enepyranosyluronic acid)-4-O-sulfo-D-galactose
-
-
-
?
chondroitin 4-sulfate
2-acetamido-2-deoxy-3-O-(beta-D-gluco-4-enepyranosyluronic acid)-4-O-sulfo-D-galactose
-
-
-
-
?
chondroitin 4-sulfate
2-acetamido-2-deoxy-3-O-(beta-D-gluco-4-enepyranosyluronic acid)-4-O-sulfo-D-galactose
-
i.e. chondroitin sulfate A
-
-
?
chondroitin 4-sulfate
?
-
chondroitin AC lyase is specific for chondroitin 4-sulfate and has endolytic activity
-
-
?
chondroitin 4-sulfate
?
-
random endolytic action pattern
the products of chondroitinase AC contain unsaturated oligosaccharides of sizes ranging from disaccharide to decasaccharide
-
?
chondroitin 6-sulfate
?
-
the degradation of chondroitin by an anionic E1cb elimination mechanism involves proton abstraction from C5 of glucuronic acid, Tyr234 is the key base catalysts
-
-
?
chondroitin 6-sulfate
?
-
random endolytic action pattern
the products of chondroitinase AC contain unsaturated oligosaccharides of sizes ranging from disaccharide to decasaccharide
-
?
phenyl 4-deoxy-4-fluoro-beta-D-glucopyranosiduronic acid
?
-
synthetic chromogenic substrate
-
?
phenyl 4-deoxy-4-fluoro-beta-D-glucopyranosiduronic acid
?
-
synthetic chromogenic substrate
-
?
phenyl 4-methylumbelliferyl-beta-D-glucopyranosiduronic acid
?
-
synthetic chromogenic substrate
-
?
phenyl 4-methylumbelliferyl-beta-D-glucopyranosiduronic acid
?
-
synthetic chromogenic substrate
-
?
additional information
?
-
Arg292 is involved in recognition of the N-acetyl and sulfate moieties of galactosamine, but does not participate directly in catalysis
-
?
additional information
?
-
-
developement of an assay using synthetic substrates, which can be monitored by 3 different techniques, UV-Vis spectroscopy, fluorescence spectroccopy, and fluoride ion-selective electrode usage, overview, products of chondroitin sulfate cleavages are disaccharides or oligosaccharides with DELTA4,5-unsaturated uronic acid resdiues at the nonreducing end, methyl 4-deoxy-4-fluoro-beta-D-glucopyranosiduronic acid is a poor substrate
-
?
additional information
?
-
-
elimination mechanism, but no syn-elimination, resulting in disaccharides or oligosaccharides with DELTA4,5-unsaturated uronic acid residues at the nonreducing end
-
?
additional information
?
-
-
the active site forms a tunnel, structurally involved residue Arg292 is responsible for substrate recognition of N-acetyl or O-sulfo moieties in galactosamine residues, it does not participate in catalysis
-
?
additional information
?
-
-
digestion of amyloid fibrils with chondroitinase AC hydrolyzes keratan sulfate and heparan sulfate
-
-
?
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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
benzyl 4-deoxy-5-fluoro-beta-D-galactopyranosiduronic acid
-
competitive inhibition
benzyl S-(2-acetamido-2-deoxy-beta-D-galactopyranosyl)-(1-4)-4-deoxy-4-thio-beta-D-glucopyranosiduronic acid
-
competitive versus phenyl 4-O -(2',4'-dinitrophenyl)-beta-D-glucopyranosiduronic acid
phenyl 4-deoxy-4,4-difluoro-beta-D-xylo-hexopyranosiduronic acid
-
competitive inhibition
additional information
-
degree of inhibition by fatty acids depends on the chain length and the number of unsaturated bonds as well as the stereochemistry, overview
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
6.9
4-O-(2',4'-dinitrophenyl)-beta-D-glucopyranosiruronic acid
-
pH 6.8, 30°C, wild-type enzyme
16.9
benzyl 4-O-(2'-nitrophenyl)-beta-D-glucopyranosiduronic acid
-
pH 6.8
9
benzyl 4-O-(3',4'-dinitrophenyl)-beta-D-glucopyranosiduronic acid
-
pH 6.8
12.2
benzyl 4-O-(4'-chloro-2'-nitrophenyl)-beta-D-glucopyranosiduronic acid
-
pH 6.8
28
benzyl 4-deoxy-4-fluoro-beta-D-glucopyranosiduronic acid
-
pH 6.8, 30°C
7
benzyl 4-O-(2',4'-dinitrophenyl)-beta-D-glucopyranosiduronic acid
-
pH 6.8
7
benzyl 4-O-(2',4'-dinitrophenyl)-beta-D-glucopyranosiduronic acid
-
pH 6.8, 30°C
114
phenyl 4-deoxy-4-fluoro-beta-D-glucopyranosiduronic acid
-
pH 6.8, 30°C
0.9
phenyl 4-methylumbelliferyl-beta-D-glucopyranosiduronic acid
-
pH 8.0, 30°C
additional information
additional information
-
effect of temperature in the Km-value
-
additional information
additional information
-
kinetics, measurement of deuterium isotope effects
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.041
4-O-(2',4'-dinitrophenyl)-beta-D-glucopyranosiruronic acid
-
pH 6.8, 30°C, wild-type enzyme
0.019
benzyl 4-O-(2',4'-dinitrophenyl)-beta-D-glucopyranosiduronic acid
-
pH 6.8
0.027
benzyl 4-O-(2'-nitrophenyl)-beta-D-glucopyranosiduronic acid
-
pH 6.8
0.019
benzyl 4-O-(3',4'-dinitrophenyl)-beta-D-glucopyranosiduronic acid
-
pH 6.8
0.035
benzyl 4-O-(4'-chloro-2'-nitrophenyl)-beta-D-glucopyranosiduronic acid
-
pH 6.8
0.005
benzyl S-(2-acetamido-2-deoxy-beta-D-galactopyranosyl)-(1-4)-4-deoxy-4-thio-beta-D-glucopyranosiduronic acid
-
-
additional information
additional information
-
effect of temperature in the turnover number
-
234
chondroitin 4-sulfate
-
recombinant enzyme, pH 8.0, 35°C, dependent on expression system
423 - 480
chondroitin 6-sulfate
-
recombinant enzyme, pH 8.0, 35°C, dependent on expression system
0.0015
phenyl 4-methylumbelliferyl-beta-D-glucopyranosiduronic acid
-
pH 8.0
0.0016
phenyl 4-methylumbelliferyl-beta-D-glucopyranosiduronic acid
-
pH 8.0
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
45
benzyl S-(2-acetamido-2-deoxy-beta-D-galactopyranosyl)-(1-4)-4-deoxy-4-thio-beta-D-glucopyranosiduronic acid
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.18
purified transconjugated wild-type, substrate heparan sulfate
0.2
purified transconjugated wild-type, substrate dermatan sulfate
123.9
purified transconjugated wild-type, substrate chondroitin 4-sulfate
62.5
purified transconjugated wild-type, substrate chondroitin 6-sulfate
94.5
purified transconjugated wild-type, substrate hyaluronic acid
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
-
the enzyme contains a N-terminal signal peptide which is proteolytically cleaved to produce an active enzyme
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
complexes of the wild-type enzyme with dermatan sulfate hexasaccharide, tetrasaccharide, and hyaluronic acid tetrasaccharide, and mutant Y234F enzyme in complex with chondroitin sulfate tetrasaccharide, hanging drop vapour diffusion method, equal volumes, 0.005 ml, of protein and reservoir solution are suspended over 1 ml reservoir solution containing 15% w/v PEG 3350, 0.4 M sodium acetate, 0.1 M HEPES, pH 7.5, at room temperature of about 20°C, 1 day, X-ray diffraction structure determination and analysis at 2.0-2.3 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H225A
site-directed mutagenesis, active site residue, inactive mutant
R288A
site-directed mutagenesis, active site residue, nearly inactive mutant
R292A
site-directed mutagenesis, substrate recognition residue, mutant with residual activity
Y234F
site-directed mutagenesis, active site residue, nearly inactive mutant
R292A
-
site-directed mutagenesis, substrate recognition residue, reduced activity, action pattern is neither purely random endolytic nor purely random exolytic
additional information
additional information
a vector is engineered containing the gene for Flavobacterium heparinum chondroitinase AC for expression in adult bone marrow-derived cells which are then transplanted into an injury site in the CNS. Expression and secretion of active chondroitinase AC is observed in vitro using transfected Chinese hamster ovarian and gliosarcoma cells and in vivo by immunohistochemistry analysis which show degraded chondroitin sulfate coinciding with the location of transfected bone marrow-derived cells. Immunolabelling of the axonal growth-associated protein GAP-43 is observed in vivo and coincides with the location of degraded chondroitin sulfate
additional information
-
a vector is engineered containing the gene for Flavobacterium heparinum chondroitinase AC for expression in adult bone marrow-derived cells which are then transplanted into an injury site in the CNS. Expression and secretion of active chondroitinase AC is observed in vitro using transfected Chinese hamster ovarian and gliosarcoma cells and in vivo by immunohistochemistry analysis which show degraded chondroitin sulfate coinciding with the location of transfected bone marrow-derived cells. Immunolabelling of the axonal growth-associated protein GAP-43 is observed in vivo and coincides with the location of degraded chondroitin sulfate
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
wild-type enzyme, and recombinant mutant enzymes from Flavobacterium heparinum mutant strains
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloning and construction of mutants in Escherichia coli and expression in Flavobacterium heparinum, the Flavobacterium heparinum strains are mutated by conjugation
gene cslA, DNA sequence determination and analysis, chromosomal localization, expression in Escherichia coli
gene cAC, DNA sequence determination and analysis, functional expression without the N-terminal signal peptide in Escherichia coli as His-tagged protein, 2 different expression systems
-
mutant R292A, expression in Escherichia coli and conjugation to Flavobacterium heparinum to create a mutant strain
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
bone marrow-derived mononuclear cells, transfected with our construct and transplanted into CNS, could be a potential tool for studying an alternative chondroitinase AC delivery method
analysis
-
useful tool for the identification and structural characterization of chondriotin and dermatan sulfates
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hascall, V.C.; Riolo, R.L.; Hayward, J.; Reynolds, C.C.
Treatment of bovine nasal cartilage proteoglycan with chondroitinases from Flavobacterium heparinum and Proteus vulgaris
J. Biol. Chem.
247
4521-4528
1972
Pedobacter heparinus
Aguiarand, J.A.K.; Michelacci, Y.M.
Preparation and purification of Flavobacterium heparinum chondroitinases AC and B by hydrophobic interaction chromatography
Braz. J. Med. Biol. Res.
32
545-550
1999
Pedobacter heparinus
Michelacci, Y.M.; Dietrich, C.P.
A comparative study between a chondroitinase B and a chondroitinase AC from Flavobacterium heparinum: Isolation of a chondroitinase AC-susceptible dodecasaccharide from chondroitin sulphate B
Biochem. J.
151
121-129
1975
Pedobacter heparinus
Hiyama, K.; Okada, S.
Action of chondroitinases. I. The mode of action of two chondroitinase-AC preparations of different origin
J. Biochem.
80
1201-1207
1976
Paenarthrobacter aurescens, Pedobacter heparinus
Hiyama, K.; Okada, S.
Action of chondroitinases. III. Ionic strength effects and kinetics in the action of chondroitinase AC
J. Biochem.
82
429-436
1977
Paenarthrobacter aurescens, Pedobacter heparinus
Gu, K.; Linhardt, R.L.; Laliberte, M.; Gu, K.; Zimmermann, J.
Purification, characterization and specificity of chondroitin lyases and glycuronidase from Flavobacterium heparinum
Biochem. J.
312
569-577
1995
Pedobacter heparinus
Fethiere, J.; Eggimann, B.; Cygler, M.
Crystal structure of chondroitin AC lyase, a representative of a family of glycosaminoglycan degrading enzymes
J. Mol. Biol.
288
635-647
1999
Pedobacter heparinus
Fethiere, J.; Shilton, B.H.; Li, Y.; Allaire, M.; Laliberte, M.; Eggimann, B.; Cygler, M.
Crystallization and preliminary analysis of chondroitinase AC from Flavobacterium heparinum
Acta Crystallogr. Sect. D
54
279-280
1998
Pedobacter heparinus
Rye, C.S.; Withers, S.G.
Development of an assay and determination of kinetic parameters for chondroitin AC lyase using defined synthetic substrates
Anal. Biochem.
308
77-82
2002
Pedobacter heparinus
Tkalec, A.L.; Fink, D.; Blain, F.; Zhang-Sun, G.; Laliberte, M.; Bennett, D.C.; Gu, K.; Zimmermann, J.J.F.; Su, H.
Isolation and expression in Escherichia coli of cslA and cslB, genes coding for the chondroitin sulfate-degrading enzymes chondroitinase AC and chondroitinase B, respectively, from Flavobacterium heparinum
Appl. Environ. Microbiol.
66
29-35
2000
Pedobacter heparinus (Q59288), Pedobacter heparinus
Pojasek, K.; Shriver, Z.; Kiley, P.; Venkataraman, G.; Sasisekharan, R.
Recombinant expression, purification, and kinetic characterization of chondroitinase AC and chondroitinase B from Flavobacterium heparinum
Biochem. Biophys. Res. Commun.
286
343-351
2001
Pedobacter heparinus
Huang, W.; Boju, L.; Tkalec, L.; Su, H.; Yang, H.O.; Gunay, N.S.; Linhardt, R.J.; Kim, Y.S.; Matte, A.; Cygler, M.
Active site of chondroitin AC lyase revealed by the structure of enzyme-oligosaccharide complexes and mutagenesis
Biochemistry
40
2359-2372
2001
Pedobacter heparinus (Q59288)
Capila, I.; Wu, Y.; Rethwisch, D.W.; Matte, A.; Cygler, M.; Linhardt, R.J.
Role of arginine 292 in the catalytic activity of chondroitin AC lyase from Flavobacterium heparinum
Biochim. Biophys. Acta
1597
260-270
2002
Pedobacter heparinus
Rye, C.S.; Withers, S.G.
Elucidation of the mechanism of polysaccharide cleavage by chondroitin AC lyase from Flavobacterium heparinum
J. Am. Chem. Soc.
124
9756-9767
2002
Pedobacter heparinus
Suzuki, K.; Terasaki, Y.; Uyeda, M.
Inhibition of hyaluronidases and chondroitinases by fatty acids
J. Enzyme Inhib. Med. Chem.
17
183-186
2002
Paenarthrobacter aurescens, Pedobacter heparinus
Rye, C.S.; Withers, S.G.
The synthesis of a novel thio-linked disaccharide of chondroitin as a potential inhibitor of polysaccharide lyases
Carbohydr. Res.
339
699-703
2004
Pedobacter heparinus
Rye, C.S.; Matte, A.; Cygler, M.; Withers, S.G.
An atypical approach identifies TYR234 as the key base catalyst in chondroitin AC lyase
ChemBioChem
7
631-637
2006
Pedobacter heparinus
Makovitzky, J.; Richter, S.; Appel, T.R.
Topooptical investigations and enzymatic digestions on tissue-isolated amyloid fibrils
Acta Histochem.
108
193-196
2006
Pedobacter heparinus
Zhang, Z.; Park, Y.; Kemp, M.M.; Zhao, W.; Im, A.R.; Shaya, D.; Cygler, M.; Kim, Y.S.; Linhardt, R.J.
Liquid chromatography-mass spectrometry to study chondroitin lyase action pattern
Anal. Biochem.
385
57-64
2009
Paenarthrobacter aurescens, Pedobacter heparinus
Volpi, N.; Maccari, F.
Structural characterization and antithrombin activity of dermatan sulfate purified from marine clam Scapharca inaequivalvis
Glycobiology
19
356-367
2008
Paenarthrobacter aurescens, Pedobacter heparinus
Coulson-Thomas, Y.M.; Coulson-Thomas, V.J.; Filippo, T.R.; Mortara, R.A.; da Silveira, R.B.; Nader, H.B.; Porcionatto, M.A.
Adult bone marrow-derived mononuclear cells expressing chondroitinase AC transplanted into CNS injury sites promote local brain chondroitin sulphate degradation
J. Neurosci. Methods
171
19-29
2008
Pedobacter heparinus (Q59288), Pedobacter heparinus
Flangea, C.; Schiopu, C.; Sisu, E.; Serb, A.; Przybylski, M.; Seidler, D.G.; Zamfir, A.D.
Determination of sulfation pattern in brain glycosaminoglycans by chip-based electrospray ionization ion trap mass spectrometry
Anal. Bioanal. Chem.
395
2489-2498
2009
Pedobacter heparinus
Zamfir, A.D.; Flangea, C.; Sisu, E.; Serb, A.F.; Dinca, N.; Bruckner, P.; Seidler, D.G.
Analysis of novel over- and under-sulfated glycosaminoglycan sequences by enzyme cleavage and multiple stage MS
Proteomics
9
3435-3444
2009
Pedobacter heparinus
EXTERNAL LINKS (specific for EC-Number 4.2.2.5)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
