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Enzyme Nomenclature
Information on EC 4.2.2.5 - chondroitin AC lyase
for references in articles please use BRENDA:EC4.2.2.5
Word Map on EC 4.2.2.5
- 4.2.2.5
-
proteoglycans
- glycosaminoglycans
- dermatan
-
heparan
- disaccharide
- hyaluronidase
- cartilage
-
hyaluronic
- oligosaccharide
- heparitinase
-
axon
-
articular
-
nitrous
- flavobacterium
-
glucuronic
- 6-sulfate
-
aggrecan
- heparinum
-
35ssulfate
-
3hglucosamine
- keratanase
-
hexasaccharide
-
alcian
-
iduronic
-
decorin
-
cspgs
-
lyases
-
4-sulphate
- chabc
-
tetrasaccharide
-
sulfate-containing
- aurescens
-
cuprolinic
- phosphacan
-
trisulfated
- chondroitin-4-sulfate
-
galactosaminoglycans
- food industry
-
unsulfated
-
monosulfated
-
neurocan
-
oversulfated
-
undersulfated
-
cetylpyridinium
- medicine
- analysis
-
glca
-
blue-positive
-
hexuronic
-
perineuronal
-
beta-d-xyloside
- chlorate
-
stub
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
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EC NUMBER 
COMMENTARY 
4.2.2.5
-
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RECOMMENDED NAME
GeneOntology No.
chondroitin AC lyase
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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
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
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, 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, 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, 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
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
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
-
-
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
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
elimination
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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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].
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CAS REGISTRY NUMBER
COMMENTARY
9047-57-8
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
multiple forms: chondroitinase I, chondroitinase II and chondroitinase III
-
-
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
-
chondroitin AC I lyase, an enzyme belonging to the class of lyases, which due to its endolytic activity cleaves the glycosidic bonds between GalNAc and D-GlcA for depolymerization of chondroitin sulfate and dermatan sulfate
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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
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
disaccharides
-
i.e. chondroitin 4-sulfate
-
?
chondroitin sulfate C
disaccharides
-
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
-
?
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
?
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
?
-
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
-
-
-
-
?
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
?
-
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 6-sulfate
?
-
exolytic action pattern
the products afforded by chondroitinase ACII contain primarily unsaturated disaccharide
-
?
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 sulfate A
?
-
i.e. chondroitin 4-sulfate, best substrate
-
?
chondroitin sulfate A
?
A9Y5J0
relative activity: 100% (recombinant protein), 100% (native protein)
-
-
?
chondroitin sulfate A
?
-
i.e. chondroitin 4-sulfate, best substrate
-
?
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, low activity
-
?
chondroitin sulfate C
?
A9Y5J0
relative activity: 42% (recombinant protein), 46% (native protein)
-
-
?
chondroitin sulfate C
?
-
i.e. chondroitin 6-sulfate, low activity
-
?
chondroitin sulfate C
?
-
i.e. chondroitin 6-sulfate, wild-type enzyme and mutants R292A, R288A, and Y234F
-
?
dermatan sulfate
?
-
wild-type enzyme and mutants R292A, and Y234F
-
?
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
?
A9Y5J0
relative activity: 54% (recombinant protein), 67% (native protein)
-
-
?
hyaluronic acid
?
-
wild-type enzyme and mutants R292A, R288A, and Y234F
-
?
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
?
-
A9Y5J0
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
?
-
-
chondroitin AC lyase activity is significantly related to the virulence of the strains at 25°C. ChonAC activity is significantly higher in the high virulence group than in the low virulence group at 25°C
-
-
-
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
?
-
-
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
-
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
?
-
-
chondroitin AC lyase activity is significantly related to the virulence of the strains at 25°C. ChonAC activity is significantly higher in the high virulence group than in the low virulence group at 25°C
-
-
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ba2+
Ca2+
Mg2+
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INHIBITORS
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
-
not affected by Mg2+, Mn2+, Ca2+, Co2+, and EDTA
-
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
-
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
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
not affected by Mg2+, Mn2+, Ca2+, Co2+, and EDTA
-
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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, 30°C
7
benzyl 4-O-(2',4'-dinitrophenyl)-beta-D-glucopyranosiduronic acid
-
pH 6.8
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
-
effect of temperature in the Km-value
-
additional information
additional information
-
Km for chondroitin 4-sulfate: 0.2 g/L; Km for chondroitin 6-sulfate: 0.408 g/L, Km for hyaluronate: 0.412 g/L
-
additional information
additional information
-
kinetics, measurement of deuterium isotope effects
-
additional information
additional information
-
Km-value for chondroitin sulfate A is 0.4 mg/ml, Km-value for chondroitin sulfate C is 0.5 mg/ml, at pH 7 and 30°C
-
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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
-
-
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
additional information
additional information
-
effect of temperature in the turnover number
-
additional information
additional information
-
effect of temperature in the turnover number
-
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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
-
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
62.5
-
purified transconjugated wild-type, substrate chondroitin 6-sulfate
123.9
-
purified transconjugated wild-type, substrate chondroitin 4-sulfate
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 8
-
pH 5: about 25% of maximal activity, pH 8: about 35% of maximal activity
5 - 9.5
-
pH 5.0: about 30% of maximal activity, pH 9.5: about 40% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
40
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 55
-
25°C: about 85% of maximal activity, 55°C: about 45% of maximal activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Pedobacter heparinus (strain ATCC 13125 / DSM 2366 / CIP 104194 / JCM 7457 / NBRC 12017 / NCIMB 9290 / NRRL B-14731 / HIM 762-3)
Pedobacter heparinus (strain ATCC 13125 / DSM 2366 / CIP 104194 / JCM 7457 / NBRC 12017 / NCIMB 9290 / NRRL B-14731 / HIM 762-3)
Pedobacter heparinus (strain ATCC 13125 / DSM 2366 / CIP 104194 / JCM 7457 / NBRC 12017 / NCIMB 9290 / NRRL B-14731 / HIM 762-3)
Pedobacter heparinus (strain ATCC 13125 / DSM 2366 / CIP 104194 / JCM 7457 / NBRC 12017 / NCIMB 9290 / NRRL B-14731 / HIM 762-3)
Pedobacter heparinus (strain ATCC 13125 / DSM 2366 / CIP 104194 / JCM 7457 / NBRC 12017 / NCIMB 9290 / NRRL B-14731 / HIM 762-3)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
76000
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
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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
side-chain modification
side-chain modification
-
carbohydrate content of chondroitinase I is 4.1%, carbohydrate content of chondroitinase II is 2.7%, carbohydrate content of chondroitinase III is 3.1%
side-chain modification
-
glycoprotein containing mannose, glucose, glucosamine and glucuronic acid in the ratio 3:5:4:2, carbohydrate content 4.1%
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme alone and in complex with substrates chondroitin 4-sulfate tetrasaccharide, and hyaluronan tetrasaccharide, hanging drop vapour diffusion method, 0.002 ml protein solution: 10 mg/ml protein, + 0.002 ml reservoir solution: 23% w/v PEG 8000, 0.1 M sodium phosphate, pH 6.4, 0.4 M ammonium acetate, 10% v/v glycerol, suspended over 1 ml reservoir solution, a few days, larger crystals by macroseeding, X-ray diffraction structure determination and analysis of the enzyme-substrate complexes at 1.25-1.9 A high resolution
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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
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
wild-type enzyme, and recombinant mutant enzymes from Flavobacterium heparinum mutant strains
-
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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 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
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gene cslA, DNA sequence determination and analysis, chromosomal localization, expression in Escherichia coli
-
mutant R292A, expression in Escherichia coli and conjugation to Flavobacterium heparinum to create a mutant strain
-
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
R288A
-
site-directed mutagenesis, active site residue, nearly inactive mutant
R292A
Y234F
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
R292A
-
site-directed mutagenesis, substrate recognition residue, mutant with residual activity
R292A
-
site-directed mutagenesis, substrate recognition residue, reduced activity, action pattern is neither purely random endolytic nor purely random exolytic
Y234F
-
site-directed mutagenesis, active site residue, nearly inactive mutant
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
useful tool for the identification and structural characterization of chondriotin and dermatan sulfates
food industry
-
in Flavobacterium columnare strains C, E, G and H isolated from disease outbreaks, chondroitinase activity is significantly higher in the virulent, rhizoid variants than in the rough variants of the same strain. Temperature significantly increases the adhesion of rhizoid variants up to 20°C. Both rhizoid colony morphology and high chondroitinase activity seem to be needed for virulence and temperature may promote the adhesion of the virulent variants to surfaces at fish farms
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
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LINKS TO OTHER DATABASES (specific for EC-Number 4.2.2.5)
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