Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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

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
stepwise 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
-
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
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, lytic mechanism with Tyr242 acting as a general base that abstracts the proton from the C5 position of glucuronic acid while Asn183 and His233 neutralize the charge on the glucuronate acidic group, substrate binding site
-
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
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
-
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
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
4-O-(2',4'-dinitrophenyl)-beta-D-glucopyranosiruronic acid
?
-
-
-
-
?
benzyl 4-deoxy-4-fluoro-beta-D-glucopyranosiduronic acid
?
benzyl 4-O-(2',4'-dinitrophenyl)-beta-D-glucopyranosiduronic acid
?
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 4-sulfate
chondroitin 4-sulfate disaccharide
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
-
-
?
GlcNAc-D-glucuronic acid-GlcNAc-D-glucuronic acid
DELTA-4,5-uronic acid-GlcNAc + N-acetyl-D-glucosamine + DELTA-4,5-glucuronic acid
-
-
-
?
heparan sulfate
?
wild-type enzyme and mutants R292A, R288A, and Y234F
-
?
hyaluronan methyl ester
?
-
-
-
-
?
hyaluronate
hyaluronate oligosaccharides
-
-
-
-
?
methyl 4-deoxy-4-fluoro-beta-D-glucopyranosiduronic acid
?
-
synthetic chromogenic substrate
-
?
phenyl 4-deoxy-4-fluoro-beta-D-glucopyranosiduronic acid
?
phenyl 4-methylumbelliferyl-beta-D-glucopyranosiduronic acid
?
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
?
additional information
?
-
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

?
-
-
-
-
?
chondroitin
?
-
degradation is faster than with chondroitin 4-sulfate or chondroitin 6-sulfate
-
-
?
chondroitin
?
-
best 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
-
-
-
?
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

?
61% of the activity with hyaluronic acid
-
-
?
chondroitin 4-sulfate
?
-
ACII lyase is an exolytic enzyme able to cut the polysaccharide chains starting from the nonreducing end
-
-
?
chondroitin 4-sulfate
?
-
exolytic action pattern
the products afforded by chondroitinase ACII contain primarily unsaturated disaccharide
-
?
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 4-sulfate
?
-
-
-
?
chondroitin 4-sulfate
?
-
-
-
?
chondroitin 4-sulfate

chondroitin 4-sulfate disaccharide
-
-
-
?
chondroitin 4-sulfate
chondroitin 4-sulfate disaccharide
-
-
-
?
chondroitin 6-sulfate

?
86% of the activity with hyaluronic acid
-
-
?
chondroitin 6-sulfate
?
-
-
-
-
?
chondroitin 6-sulfate
?
-
-
-
-
?
chondroitin 6-sulfate
?
-
exolytic action pattern
the products afforded by chondroitinase ACII contain primarily unsaturated disaccharide
-
?
chondroitin 6-sulfate
?
-
-
-
-
?
chondroitin 6-sulfate
?
-
i.e. chondroitin sulfate C
-
-
?
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
-
?
chondroitin 6-sulfate
?
-
-
-
?
chondroitin 6-sulfate
?
-
-
-
?
chondroitin sulfate A

?
-
i.e. chondroitin 4-sulfate, best substrate
-
?
chondroitin sulfate A
?
relative activity: 100% (recombinant protein), 100% (native protein)
-
-
?
chondroitin sulfate A
?
-
i.e. chondroitin 4-sulfate, best substrate
-
?
chondroitin sulfate A
?
-
-
-
-
?
chondroitin sulfate A
?
-
i.e. chondroitin 4-sulfate
-
?
chondroitin sulfate A
?
-
-
-
-
?
chondroitin sulfate A
?
-
i.e. chondroitin 4-sulfate
-
?
chondroitin sulfate A
?
-
i.e. chondroitin 4-sulfate
-
?
chondroitin sulfate A
?
-
i.e. chondroitin 4-sulfate
-
?
chondroitin sulfate A
?
i.e. chondroitin 4-sulfate
-
?
chondroitin sulfate A
?
i.e. chondroitin 4-sulfate, best substrate, wild-type enzyme and mutants R292A, R288A, H225A and Y234F
-
?
chondroitin sulfate A
?
-
-
-
-
?
chondroitin sulfate B

?
-
-
-
-
?
chondroitin sulfate B
?
-
-
-
-
?
chondroitin sulfate C

?
-
i.e. chondroitin 6-sulfate, low activity
-
?
chondroitin sulfate C
?
relative activity: 42% (recombinant protein), 46% (native protein)
-
-
?
chondroitin sulfate C
?
-
i.e. chondroitin 6-sulfate, low activity
-
?
chondroitin sulfate C
?
-
-
-
-
?
chondroitin sulfate C
?
-
i.e. chondroitin 6-sulfate
-
?
chondroitin sulfate C
?
-
i.e. chondroitin 6-sulfate
-
?
chondroitin sulfate C
?
-
-
-
-
?
chondroitin sulfate C
?
-
i.e. chondroitin 6-sulfate
-
?
chondroitin sulfate C
?
-
i.e. chondroitin 6-sulfate
-
?
chondroitin sulfate C
?
-
i.e. chondroitin 6-sulfate
-
?
chondroitin sulfate C
?
-
i.e. chondroitin 6-sulfate
-
?
chondroitin sulfate C
?
i.e. chondroitin 6-sulfate
-
?
chondroitin sulfate C
?
i.e. chondroitin 6-sulfate, wild-type enzyme and mutants R292A, R288A, and Y234F
-
?
chondroitin sulfate C
?
-
-
-
-
?
chondroitin sulfate D

?
-
-
-
-
?
chondroitin sulfate D
?
-
-
-
-
?
chondroitin sulfate E

?
-
-
-
-
?
chondroitin sulfate E
?
-
-
-
-
?
dermatan sulfate

?
-
-
-
-
?
dermatan sulfate
?
-
-
-
-
?
dermatan sulfate
?
wild-type enzyme and mutants R292A, and Y234F
-
?
hyaluronan

?
-
-
-
?
hyaluronate

?
-
-
-
-
?
hyaluronate
?
-
degradation is faster than with chondroitin 4-sulfate or chondroitin 6-sulfate
-
-
?
hyaluronate
?
-
degradation is faster than with chondroitin 4-sulfate or chondroitin 6-sulfate
-
-
?
hyaluronic acid

?
-
-
-
?
hyaluronic acid
?
-
low activity
-
?
hyaluronic acid
?
relative activity: 54% (recombinant protein), 67% (native protein)
-
-
?
hyaluronic acid
?
-
low activity
-
?
hyaluronic acid
?
-
-
-
?
hyaluronic acid
?
wild-type enzyme and mutants R292A, R288A, and Y234F
-
?
hyaluronic acid
?
-
-
-
?
hyaluronic acid
?
-
-
-
?
hyaluronic acid
?
-
-
-
-
?
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

?
-
-
no activity with dermatan sufate, heparin and heparan sulfate, the latter of porcine or bovine source
-
?
additional information
?
-
no activity with dermatan sulfate or heparin as substrate
-
-
?
additional information
?
-
-
no activity with dermatan sufate, heparin and heparan sulfate, the latter of porcine or bovine source
-
?
additional information
?
-
-
constitutive enzyme
-
-
?
additional information
?
-
-
chondroitin AC lyase activity is significantly related to the virulence of the strains at 25ưC. ChonAC activity is significantly higher in the high virulence group than in the low virulence group at 25ưC
-
-
?
additional information
?
-
-
chondroitin/dermatan sulfate chain of decorin, with a high complexity due to the large variety of glycoforms, from human skin fibroblasts is released by reductive beta-elimination reaction and digested with chondroitin AC I lyase. Mass spectrometric substrate and product analysis, e.g. tetrasulfated octasaccharide, decasaccharides, a trisulfated, a hexasulfated [4,5-D-GlcAGalNAc(IdoAGalNAc)4], and [4,5-D-GlcAGalNAc(IdoAGalNAc)3], and disaccharides, overview
-
-
?
additional information
?
-
-
the enzyme als acts as an exoglycosidase towards hyaluronate
-
-
?
additional information
?
-
-
no activity with dermatan sulfate
-
-
?
additional information
?
-
-
substrate specificity, no activity with dermatan sulfate
-
?
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
?
-
-
constitutive enzyme
-
-
?
additional information
?
-
-
digestion of amyloid fibrils with chondroitinase AC hydrolyzes keratan sulfate and heparan sulfate
-
-
?
additional information
?
-
-
does not split endogalactosaminidic bonds neighbouring to reduced disaccharide units
-
-
?
additional information
?
-
-
no activity with chondroitin sulfate B, heparin or heparan sulfate
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
brenda
Klingbeil, U.; Klein, U.; von Figura, K.
Action of chondroitinases ABC and AC on chondroitin 4-sulfate-oligosaccharides with terminal N-acetylgalactosaminitol residues
Hoppe-Seyler's Z. Physiol. Chem.
359
765-767
1978
Proteus vulgaris
brenda
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
brenda
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
brenda
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
brenda
Hiyama, K.; Okada, S.
Multiple forms of chondroitinase AC from Arthrobacter aurescens
Agric. Biol. Chem.
41
1279-1286
1977
Paenarthrobacter aurescens
-
brenda
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
brenda
Ulrich, H.P.; Klein, U.; von Figura, K.
Degradation of even-numbered reduced and non-reduced hyaluronate oligosaccharides with D-glucuronic acid or N-acetyl-D-glucosamine as non-reducing terminal by chondroitin ABC and AC lyases
Hoppe-Seyler's Z. Physiol. Chem.
360
1457-1463
1979
Paenarthrobacter aurescens
brenda
Hiyama, K.; Okada, S.
Amino acid composition and physiochemical characterization of chondroitinase from Arthrobacter aurescens
J. Biochem.
78
1183-1190
1975
Paenarthrobacter aurescens
brenda
Kitamikado, M.; Lee, Y.Z.
Chondroitinase-producing bacteria in natural habitats
Appl. Microbiol.
29
414-421
1975
Aeromonas sp.
brenda
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
brenda
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
brenda
Griffin, B.R.
Characteristics of a chondroitin AC lyase produced by Cytophaga columnaris
Trans. Am. Fish. Soc.
120
391-395
1991
Flavobacterium columnare
-
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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)
brenda
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
brenda
Hong, S.W.; Kim, B.T.; Shin, H.Y.; Kim, W.S.; Lee, K.S.; Kim, Y.S.; Kim, D.H.
Purification and characterization of novel chondroitin ABC and AC lyases from Bacteroides stercoris HJ-15, a human intestinal anaerobic bacterium
Eur. J. Biochem.
269
2934-2940
2002
Bacteroides stercoris, Bacteroides stercoris HJ-15
brenda
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
brenda
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
brenda
Lunin, V.V.; Li, Y.; Linhardt, R.J.; Miyazono, H.; Kyogashima, M.; Kaneko, T.; Bell, A.W.; Cygler, M.
High-resolution crystal structure of Arthrobacter aurescens chondroitin AC lyase: an enzyme-substrate complex defines the catalytic mechanism
J. Mol. Biol.
337
367-386
2004
Paenarthrobacter aurescens
brenda
Xie, H.X.; Nie, P.; Chang, M.X.; Liu, Y.; Yao, W.J.
Gene cloning and functional analysis of glycosaminoglycan-degrading enzyme chondroitin AC lyase from Flavobacterium columnare G4
Arch. Microbiol.
184
49-55
2005
Flavobacterium columnare, Flavobacterium columnare G4
brenda
Ke, T.; Zhangfu, L.; Qing, G.; Yong, T.; Hong, J.; Hongyan, R.; Kun, L.; Shigui, L.
Isolation of Serratia marcescens as a chondroitinase-producing bacterium and purification of a novel chondroitinase AC
Biotechnol. Lett.
27
489-493
2005
Serratia marcescens
brenda
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
brenda
Hirano, K.; Sakai, S.; Ishikawa, T.; Avci, F.Y.; Linhardt, R.J.; Toida, T.
Preparation of the methyl ester of hyaluronan and its enzymatic degradation
Carbohydr. Res.
340
2297-2304
2005
Paenarthrobacter aurescens
brenda
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
brenda
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
brenda
Suomalainen, L.R.; Tiirola, M.; Valtonen, E.T.
Chondroitin AC lyase activity is related to virulence of fish pathogenic Flavobacterium columnare
J. Fish Dis.
29
757-763
2006
Flavobacterium columnare
brenda
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
brenda
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
brenda
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
brenda
Shim, K.W.; Kim, D.H.
Cloning and expression of chondroitinase AC from Bacteroides stercoris HJ-15
Protein Expr. Purif.
58
222-228
2008
Bacteroides stercoris (A9Y5J0)
brenda
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
brenda
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
brenda
Zamfir, A.D.; Flangea, C.; Sisu, E.; Seidler, D.G.; Peter-Katalinic J.
Combining size-exclusion chromatography and fully automated chip-based nanoelectrospray quadrupole time-of-flight tandem mass spectrometry for structural analysis of chondroitin/dermatan sulfate in human decorin
Electrophoresis
32
1639-1646
2011
Homo sapiens
brenda
Kunttu, H.M.; Jokinen, E.I.; Valtonen, E.T.; Sundberg, L.R.
Virulent and nonvirulent Flavobacterium columnare colony morphologies: characterization of chondroitin AC lyase activity and adhesion to polystyrene
J. Appl. Microbiol.
111
1319-1326
2011
Flavobacterium columnare
brenda
Williams, A.; He, W.; Cress, B.F.; Liu, X.; Alexandria, J.; Yoshizawa, H.; Nishimura, K.; Toida, T.; Koffas, M.; Linhardt, R.J.
Cloning and expression of recombinant chondroitinase ACII and its comparison to the Arthrobacter aurescens enzyme
Biotechnol. J.
12
1700239
2017
Paenarthrobacter aurescens, Paenarthrobacter aurescens 161MFSha2.1
brenda
Tao, L.; Song, F.; Xu, N.; Li, D.; Linhardt, R.J.; Zhang, Z.
New insights into the action of bacterial chondroitinase AC I and hyaluronidase on hyaluronic acid
Carbohydr. Polym.
158
85-92
2017
Pedobacter heparinus
brenda
Rani, A.; Dhillon, A.; Sharma, K.; Goyal, A.
Insights into the structural characteristics and substrate binding analysis of chondroitin AC lyase (PsPL8A) from Pedobacter saltans
Int. J. Biol. Macromol.
109
980-991
2018
Pseudopedobacter saltans (F0S764), Pseudopedobacter saltans, Pseudopedobacter saltans DSM 12145 (F0S764)
brenda
Rani, A.; Goyal, A.
A new member of family 8 polysaccharide lyase chondroitin AC lyase (PsPL8A) from Pedobacter saltans displays endo- and exo-lytic catalysis
J. Mol. Catal. B
134
215-224
2016
Pseudopedobacter saltans (F0S764), Pseudopedobacter saltans DSM 12145 (F0S764)
-
brenda
Kale, V.; Fridjonsson, O.; Jonsson, J.O.; Kristinsson, H.G.; Omarsdottir, S.; Hreggvidsson, G.O.
Chondroitin lyase from a marine Arthrobacter sp. MAT3885 for the production of chondroitin sulfate disaccharides
Mar. Biotechnol.
17
479-492
2015
Arthrobacter sp. MAT3885 (I6QML9)
brenda