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Information on EC 4.2.2.21 - chondroitin-sulfate-ABC exolyase
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EC Tree
4.2.2.21 chondroitin-sulfate-ABC exolyaseIUBMB Comments
This enzyme degrades a variety of glycosaminoglycans of the chondroitin-sulfate- and dermatan-sulfate type. Chondroitin sulfate, chondroitin-sulfate proteoglycan and dermatan sulfate are the best substrates but the enzyme can also act on hyaluronan at a much lower rate. Keratan sulfate, heparan sulfate and heparin are not substrates. The related enzyme EC 4.2.2.20, chondroitin-sulfate-ABC endolyase, has the same substrate specificity but produces a mixture of oligosaccharides of different sizes that are ultimately degraded to tetra- and disaccharides . Both enzymes act by the removal of a relatively acidic C-5 proton of the uronic acid followed by the elimination of a 4-linked hexosamine, resulting in the formation of an unsaturated C4---C5 bond on the hexuronic acid moiety of the products [4,6].
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Word Map
- 4.2.2.21
- glycosaminoglycans
-
articular
- dermatan
-
tensile
-
4-sulfated
- chabc
-
neocartilage
-
fibrocartilage
-
perineuronal
-
chondroitinase-ac
-
oversulfated
-
l-iduronic
- neurocan
- analysis
- medicine
- galactosaminoglycans
- chondroitin-4-sulfate
- synthesis
- biotechnology
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
chondroitinase-abc, cabcii, hclase, bactnabc, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
chondroitinase ABC
chondroitinase-ABC
EC 4.2.2.4
-
-
formerly, part transferred
-
EC 4.2.99.6
-
-
formerly, part transferred
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
[GlcAbeta(1-3)GalNAc(4S)beta(1-4)]3 = [GlcAbeta(1-3)GalNAc(4S)beta(1-4)]2 + 2-(acetylamino)-2-deoxy-3-O-alpha-L-threo-hex-4-enopyranuronosyl-4-O-sulfo-beta-D-galactopyranose
[GlcAbeta(1-3)GalNAc(4S)beta(1-4)]3 = [GlcAbeta(1-3)GalNAc(4S)beta(1-4)]2 + 2-(acetylamino)-2-deoxy-3-O-alpha-L-threo-hex-4-enopyranuronosyl-4-O-sulfo-beta-D-galactopyranose
related enzyme EC 4.2.2.20
-
[GlcAbeta(1-3)GalNAc(4S)beta(1-4)]3 = [GlcAbeta(1-3)GalNAc(4S)beta(1-4)]2 + 2-(acetylamino)-2-deoxy-3-O-alpha-L-threo-hex-4-enopyranuronosyl-4-O-sulfo-beta-D-galactopyranose
only disaccharide products and no tetrasaccharide for each of the substrates tested are found during the course of digestion, consistent with an exolytic mode of action for the enzyme
[GlcAbeta(1-3)GalNAc(4S)beta(1-4)]3 = [GlcAbeta(1-3)GalNAc(4S)beta(1-4)]2 + 2-(acetylamino)-2-deoxy-3-O-alpha-L-threo-hex-4-enopyranuronosyl-4-O-sulfo-beta-D-galactopyranose
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
chondroitin-sulfate-ABC exolyase
This enzyme degrades a variety of glycosaminoglycans of the chondroitin-sulfate- and dermatan-sulfate type. Chondroitin sulfate, chondroitin-sulfate proteoglycan and dermatan sulfate are the best substrates but the enzyme can also act on hyaluronan at a much lower rate. Keratan sulfate, heparan sulfate and heparin are not substrates. The related enzyme EC 4.2.2.20, chondroitin-sulfate-ABC endolyase, has the same substrate specificity but produces a mixture of oligosaccharides of different sizes that are ultimately degraded to tetra- and disaccharides [4]. Both enzymes act by the removal of a relatively acidic C-5 proton of the uronic acid followed by the elimination of a 4-linked hexosamine, resulting in the formation of an unsaturated C4---C5 bond on the hexuronic acid moiety of the products [4,6].
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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
2-aminobenzamide-labeled chondroitin sulfate-C hexasaccharide
unsaturated 2-aminobenzamide-labeled chondroitin sulfate-C disaccharide + ?
-
-
-
?
2-aminobenzamide-labeled chondroitin sulfate-C tetrasaccharide
unsaturated 2-aminobenzamide-labeled chondroitin sulfate-C disaccharide + disaccharide
-
-
-
?
bovine nasal cartilage proteoglycan
2-acetamido-2-deoxy-3-O-(3-D-gluco-4-enepyranosyluronic acid)-4-O-sulfo-D-galactose + bovine nasal cartilage proteoglycan core
chondroitin sulfate
unsaturated sulfated chondroitin disaccharide
-
-
-
-
?
chondroitin sulfate A
unsaturated chondroitin sulfate A disaccharides
-
-
-
?
chondroitin sulfate A
unsaturated sulfated chondroitin A disaccharide
-
-
-
-
?
chondroitin sulfate C
unsaturated chondroitin sulfate C disaccharide
-
-
-
-
?
chondroitin sulfate C
unsaturated chondroitin sulfate C disaccharides
-
-
-
?
chondroitin sulfate D
unsaturated chondroitin sulfate D disaccharide
-
-
contains 2-acetamido-2-deoxy-3-O-(P-n-gluco-4-enepyranosyluronic acid)-6-O-sulfo-D-galactose
-
?
chondroitin sulfate D
unsaturated chondroitin sulfate D disaccharides
-
-
-
?
chondroitin sulfate E
unsaturated chondroitin sulfate E disaccharide
-
-
-
-
?
chondroitin sulfate E
unsaturated chondroitin sulfate E disaccharides
-
-
-
?
chondroitin-4-sulfate
2-acetamido-2-deoxy-3-O-(3-D-gluco-4-enepyranosyluronic acid)-4-O-sulfo-D-galactose
dermatan sulfate
2-acetamido-2-deoxy-3-O-(3-D-gluco-4-enepyranosyluronic acid)-4-O-sulfo-D-galactose + 2-acetamido-2-deoxy-3-O-(3-D-gluco-4-enepyranosyluronic acid)-6-O-sulfo-D-galactose + 2-acetamido-2-deoxy-3-O-(3-D-gluco-4-enepyranosyluronic acid)-4,6-O-bis-sulfo-D-galactose
-
-
-
-
?
GlcA-beta-(1->3)-GalNAc-beta-(1->4)-GlcA-beta-(1->3)-GalNAc-beta-(1->4)-GlcA-beta-(1->3)-GalNAc-beta-(1->4)-GlcA-beta-(1->3)-GalNAc-beta-2-pyridinaminoside + H2O
GlcA-beta-(1->3)-GalNAc + DELTA4GlcA-beta-(1->3)-GalNAc + GlcA-beta-(1->3)-GalNAc-beta-(1->4)-GlcA-beta-(1->3)-GalNAc-beta-2-pyridinaminoside
-
-
-
-
?
GlcA-beta-(1->3)-GalNAc-beta-(1->4)-GlcA-beta-(1->3)-GalNAc-beta-(1->4)-GlcA-beta-(1->3)-GalNAc-beta-2-pyridinaminoside + H2O
GlcA-beta-(1->3)-GalNAc + DELTA4GlcA-beta-(1->3)-GalNAc-beta-(1->4)-GlcA-beta-(1->3)-GalNAc-beta-2-pyridinaminoside
-
-
-
-
?
GlcA-beta-(1->3)-GalNAc-beta-(1->4)-GlcA-beta-(1->3)-GalNAc-beta-(1->4)-GlcA-beta-(1->3)-GalNAc4S-beta-(1->4)-GlcA-beta-(1->3)-GalNAc4S-beta-(1->4)-GlcA-beta-(1->3)-GalNAc4S-beta-2-pyridinaminoside + 2 H2O
GlcA-beta-(1->3)-GalNAc + DELTA4GlcA-beta-(1->3)-GalNAc + GlcA-beta-(1->3)-GalNAc4S-beta-(1->4)-GlcA-beta-(1->3)-GalNAc4S-beta-(1->4)-GlcA-beta-(1->3)-GalNAc4S-beta-2-pyridinaminoside
-
-
-
-
?
GlcA-beta-(1->3)-GalNAc-beta-(1->4)-GlcA-beta-(1->3)-GalNAc-beta-(1->4)-GlcA-beta-(1->3)-GalNAc6S-beta-(1->4)-GlcA-beta-(1->3)-GalNAc6S-beta-(1->4)-GlcA-beta-(1->3)-GalNAc6S-beta-2-pyridinaminoside + 2 H2O
GlcA-beta-(1->3)-GalNAc + GlcA-beta-(1->3)-GalNAc + DELTA4GlcA-beta-(1->3)-GalNAc6S-beta-(1->4)-GlcA-beta-(1->3)-GalNAc6S-beta-(1->4)-GlcA-beta-(1->3)-GalNAc6S-beta-2-pyridinaminoside
-
-
-
-
?
GlcA-beta-(1->3)-GalNAc-beta-(1->4)-GlcA-beta-(1->3)-GalNAc4S-beta-(1->4)-GlcA-beta-(1->3)-GalNAc4S-beta-(1->4)-GlcA-beta-(1->3)-GalNAc4S-beta-2-pyridinaminoside + H2O
GlcA-beta-(1->3)-GalNAc + DELTA4GlcA-beta-(1->3)-GalNAc4S-beta-(1->4)-GlcA-beta-(1->3)-GalNAc4S-beta-(1->4)-GlcA-beta-(1->3)-GalNAc4S-beta-2-pyridinaminoside
-
-
-
-
?
GlcA-beta-(1->3)-GalNAc-beta-(1->4)-GlcA-beta-(1->3)-GalNAc4S-beta-(1->4)-GlcA-beta-(1->3)-GalNAc4S-beta-(1->4)-GlcA-beta-(1->3)-GalNAc6S-beta-2-pyridinaminoside + H2O
GlcA-beta-(1->3)-GalNAc + DELTA4GlcA-beta-(1->3)-GalNAc4S-beta-(1->4)-GlcA-beta-(1->3)-GalNAc4S-beta-(1->4)-GlcA-beta-(1->3)-GalNAc6S-beta-2-pyridinaminoside
-
-
-
-
?
GlcA-beta-(1->3)-GalNAc-beta-(1->4)-GlcA-beta-(1->3)-GalNAc6S-beta-(1->4)-GlcA-beta-(1->3)-GalNAc6S-beta-(1->4)-GlcA-beta-(1->3)-GalNAc6S-beta-2-pyridinaminoside + H2O
GlcA-beta-(1->3)-GalNAc + DELTA4GlcA-beta-(1->3)-GalNAc6S-beta-(1->4)-GlcA-beta-(1->3)-GalNAc6S-beta-(1->4)-GlcA-beta-(1->3)-GalNAc6S-beta-2-pyridinaminoside
-
-
-
-
?
GlcA-beta-(1->3)-GalNAc4S-beta-(1->4)-GlcA-beta-(1->3)-GalNAc4S-beta-(1->4)-GlcA-beta-(1->3)-GalNAc-beta-(1->4)-GlcA-beta-(1->3)-GalNAc-beta-(1->4)-GlcA-beta-(1->3)-GalNAc-beta-2-pyridinaminoside + 2 H2O
GlcA-beta-(1->3)-GalNAc4S-beta-(1->4)-GlcA-beta-(1->3)-GalNAc4S-beta-(1->4)-GlcA-beta-(1->3)-GalNAc + DELTA4GlcA-beta-(1->3)-GalNAc-beta-(1->4)-GlcA-beta-(1->3)-GalNAc-beta-2-pyridinaminoside
-
-
-
-
?
GlcA-beta-(1->3)-GalNAc6S-beta-(1->4)-GlcA-beta-(1->3)-GalNAc6S-beta-(1->4)-GlcA-beta-(1->3)-GalNAc-beta-(1->4)-GlcA-beta-(1->3)-GalNAc-beta-(1->4)-GlcA-beta-(1->3)-GalNAc-beta-2-pyridinaminoside + 2 H2O
GlcA-beta-(1->3)-GalNAc6S-beta-(1->4)-GlcA-beta-(1->3)-GalNAc6S-beta-(1->4)-GlcA-beta-(1->3)-GalNAc + DELTA4GlcA-beta-(1->3)-GalNAc-beta-(1->4)-GlcA-beta-(1->3)-GalNAc-beta-2-pyridinaminoside
-
-
-
-
?
GlcA-beta-(1->3)-GlcNAc-beta-(1->4)-GlcA-beta-(1->3)-GalNAc6S-beta-(1->4)-GlcA-beta-(1->3)-GalNAc6S-beta-(1->4)-GlcA-beta-(1->3)-GalNAc6S-beta-2-pyridinaminoside + H2O
GlcA-beta-(1->3)-GlcNAc + DELTA4GlcA-beta-(1->3)-GalNAc6S-beta-(1->4)-GlcA-beta-(1->3)-GalNAc6S-beta-(1->4)-GlcA-beta-(1->3)-GalNAc6S-beta-2-pyridinaminoside
-
-
-
-
?
high molecular weight hyaluronic acid D
?
relative activity: 1.1%
-
-
?
IdoA-beta-(1->3)-GalNAc-beta-(1->4)-GlcA-beta-(1->3)-GalNAc6S-beta-(1->4)-GlcA-beta-(1->3)-GalNAc6S-beta-(1->4)-GlcA-beta-(1->3)-GalNAc6S-beta-2-pyridinaminoside + H2O
IdoA-beta-(1->3)-GalNAc + DELTA4GlcA-beta-(1->3)-GalNAc6S-beta-(1->4)-GlcA-beta-(1->3)-GalNAc6S-beta-(1->4)-GlcA-beta-(1->3)-GalNAc6S-beta-2-pyridinaminoside
-
-
-
-
?
low molecular weight hyaluronic acid D
?
relative activity: 1.1%
-
-
?
bovine nasal cartilage proteoglycan
2-acetamido-2-deoxy-3-O-(3-D-gluco-4-enepyranosyluronic acid)-4-O-sulfo-D-galactose + bovine nasal cartilage proteoglycan core
-
-
-
-
?
bovine nasal cartilage proteoglycan
2-acetamido-2-deoxy-3-O-(3-D-gluco-4-enepyranosyluronic acid)-4-O-sulfo-D-galactose + bovine nasal cartilage proteoglycan core
-
-
-
-
?
chondroitin
?
-
reaction is less efficient than for chondroitin sulfates
-
-
?
chondroitin 4-sulfate
?
liquid chromatography-mass spectrometry is applied to determine the action pattern of different chondroitin lyases: products afforded by chondroitinase ABC from Bacteroides thetaiotaomicron and chondroitinase ACII from Arthrobacter aurescens, contain primarily unsatuated disaccharide. These two exolytic enzymes showed different minor products, suggesting some subtle specificity differences between the actions of these two exolytic lyases on chondroitin sulfate A
-
-
?
chondroitin 4-sulfate
?
-
liquid chromatography-mass spectrometry is applied to determine the action pattern of different chondroitin lyases: products afforded by chondroitinase ABC from Bacteroides thetaiotaomicron and chondroitinase ACII from Arthrobacter aurescens, contain primarily unsatuated disaccharide. These two exolytic enzymes showed different minor products, suggesting some subtle specificity differences between the actions of these two exolytic lyases on chondroitin sulfate A
-
-
?
chondroitin 4-sulfate
unsaturated chondroitin 4-sulfate disaccharide
-
-
-
-
?
chondroitin 4-sulfate
unsaturated chondroitin 4-sulfate disaccharide
-
-
the major product
-
?
chondroitin 6-sulfate
unsaturated chondroitin 6-sulfate disaccharide
-
-
-
-
?
chondroitin 6-sulfate
unsaturated chondroitin 6-sulfate disaccharide
-
-
-
-
?
chondroitin sulfate A
?
bovine trachea, relative activity: 100%
-
-
?
chondroitin sulfate A
DELTA4,5-unsaturated chondroitin sulfate A disaccharide
-
-
-
-
?
chondroitin sulfate A
DELTA4,5-unsaturated chondroitin sulfate A disaccharide
-
-
-
-
?
chondroitin sulfate B
DELTA4,5-unsaturated chondroitin sulfate B disaccharide
-
-
-
-
?
chondroitin sulfate B
DELTA4,5-unsaturated chondroitin sulfate B disaccharide
-
-
contains 2-acetamido-2-deoxy-3-O-(P-n-gluco-4-enepyranosyluronic acid)-4-O-sulfo-n-galactose
-
?
chondroitin sulfate C
?
shark cartilage, relative activity: 61.1%
-
-
?
chondroitin sulfate C
DELTA4,5-unsaturated chondroitin sulfate C disaccharide
-
-
-
-
?
chondroitin sulfate C
DELTA4,5-unsaturated chondroitin sulfate C disaccharide
-
-
-
-
?
chondroitin sulfate D
?
skate cartilage, relative activity: 18.5%
-
-
?
chondroitin sulfate E
?
skate cartilage, relative activity: 36.7%
-
-
?
chondroitin sulfate proteoglycan
?
-
67% of the rate with chondroitin-6-sulfate
-
-
?
chondroitin sulfate proteoglycan
?
-
ChABC digests the glycosaminoglycan side chain of chondroitin sulfate proteoglycan
-
-
?
chondroitin sulfate proteoglycan
?
-
ChABC digests the glycosaminoglycan side chain of chondroitin sulfate proteoglycan to promote axonal re-growth across the injured site
-
-
?
chondroitin-4-sulfate
2-acetamido-2-deoxy-3-O-(3-D-gluco-4-enepyranosyluronic acid)-4-O-sulfo-D-galactose
-
-
-
-
?
chondroitin-4-sulfate
2-acetamido-2-deoxy-3-O-(3-D-gluco-4-enepyranosyluronic acid)-4-O-sulfo-D-galactose
-
-
-
-
?
dermatan sulfate
?
porcine intestinal mucosa, relative activity: 9.1%
-
-
?
additional information
?
-
-
no substrate: chondroitin sulfate B, keratosulfate, heparin, or heparitin sulfate
-
-
?
additional information
?
-
-
no substrate: keratan sulfate, heparin, heparan sulfate. Activity of enzyme increases with decreasing of chain size from poly-, hexa-, to tetrasaccharide substrates
-
-
?
additional information
?
-
-
no substrate: keratosulfate, heparin, or heparitin sulfate
-
-
?
additional information
?
-
-
cABCII is an exolytic enzyme that cleaves the substrate only at the nonreducing end of the polysaccharide
-
-
?
additional information
?
-
-
the recombinant protein with the sequence discrepancies is unable to effectively process galactosaminoglycan substrates, the enzyme does not react with hyaluronan, heparin/heparan sulfate, and keratan sulfate
-
-
?
additional information
?
-
-
no substrate: keratosulfate, heparin, or heparitin sulfate
-
-
?
additional information
?
-
no substrate: 2-aminobenzamide-labeled hyaluronan oligosaccharides, 2-aminobenzamide-labeled unsulfated chondroitin oligisaccharides, 2-aminobenzamide-labeled dermatan sulfate oligisaccharides
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Mg2+
additional information
Ca2+
addition of Mg2+ or Ca2+ has a dramatically different effect on activity toward CS (glucuronic acid) and DS (iduronic acid). The specific activity for CS substrates increases only moderately (2fold) while an increase of 25fold is observed for DS
Ca2+
stimulates activity, particularly against dermatan sulfate
Mg2+
addition of Mg2+ or Ca2+ has a dramatically different effect on activity toward CS (glucuronic acid) and DS (iduronic acid). The specific activity for CS substrates increases only moderately (2fold) while an increase of 25fold is observed for DS
Mg2+
stimulates activity, particularly against dermatan sulfate
additional information
for the monovalent ions tested, increasing the concentration of Na+, K+, or CS+ chloride from 0 to 0.1 M increases the activity against all substrates. Further increases in salt concentration reduces the activity dramatically, with 50% inhibition occurring at 0.15 M and a nearly complete inhibition at 0.4 M salt
additional information
-
for the monovalent ions tested, increasing the concentration of Na+, K+, or CS+ chloride from 0 to 0.1 M increases the activity against all substrates. Further increases in salt concentration reduces the activity dramatically, with 50% inhibition occurring at 0.15 M and a nearly complete inhibition at 0.4 M salt
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
N-desulfated heparin
-
50% inhibition at 0.150 mg/ml for enzyme I and 0.025 mg/ml for enzyme II
-
NaCl
-
optimal concentration 62.5 mM for substrate chondroitin 6-sulfate, 50% inhibition at 125 mM, optimal concentration 125 mM for substrate dermatan sulfate, 50% inhibition at 250 mM
heparin
-
50% inhibition at 0.050 mg/ml for enzyme I and 0.005 mg/ml for enzyme II
additional information
-
not inhibitory: Ni2+, Fe2+, Cu2+, Ca2+, Mg2+, Ba2+, Mn2+
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NaCl
-
optimal concentration 62.5 mM for substrate chondroitin 6-sulfate, inhibitory above 125 mM, optimal concentration 125 mM for substrate dermatan sulfate, inhibitory above 250 mM
phosphate
-
activity in 20 mM phosphate buffer is less than half of the activity in 50 mM phosphate buffer, maximum activity for isoenzyme I in 50 mM, isoenzyme II in 50-100 mM phosphate
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Intervertebral Disc Degeneration
Immunoselected STRO-3(+)mesenchymal precursor cells and restoration of the extracellular matrix of degenerate intervertebral discs.
Mucopolysaccharidoses
Liquid-chromatographic determination of urinary glycosaminoglycans for differential diagnosis of genetic mucopolysaccharidoses.
Trauma, Nervous System
Recombinant expression, purification, and biochemical characterization of chondroitinase ABC II from Proteus vulgaris.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0161
chondroitin 4-sulfate
-
wild type enzyme, in 50mM Tris/HCl, pH 8.0, at 37°C
0.0077
chondroitin 6-sulfate
-
mutant enzyme H452A, in 50mM Tris/HCl, pH 8.0, at 37°C
0.0098
chondroitin 6-sulfate
-
wild type enzyme, in 50mM Tris/HCl, pH 8.0, at 37°C
0.0104
chondroitin 6-sulfate
-
mutant enzyme H456A, in 50mM Tris/HCl, pH 8.0, at 37°C
0.0076
dermatan sulfate
-
mutant enzyme H456A, in 50mM Tris/HCl, pH 8.0, at 37°C
0.0091
dermatan sulfate
-
mutant enzyme H452A, in 50mM Tris/HCl, pH 8.0, at 37°C
0.0192
dermatan sulfate
-
wild type enzyme, in 50mM Tris/HCl, pH 8.0, at 37°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
16.67
chondroitin 4-sulfate
-
wild type enzyme, in 50mM Tris/HCl, pH 8.0, at 37°C
0.17
chondroitin 6-sulfate
-
mutant enzyme H452A, in 50mM Tris/HCl, pH 8.0, at 37°C
7.13
chondroitin 6-sulfate
-
mutant enzyme H456A, in 50mM Tris/HCl, pH 8.0, at 37°C
21.67
chondroitin 6-sulfate
-
wild type enzyme, in 50mM Tris/HCl, pH 8.0, at 37°C
0.072
dermatan sulfate
-
mutant enzyme H452A, in 50mM Tris/HCl, pH 8.0, at 37°C
2.4
dermatan sulfate
-
mutant enzyme H456A, in 50mM Tris/HCl, pH 8.0, at 37°C
19.17
dermatan sulfate
-
wild type enzyme, in 50mM Tris/HCl, pH 8.0, at 37°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1000
chondroitin 4-sulfate
-
wild type enzyme, in 50mM Tris/HCl, pH 8.0, at 37°C
23.3
chondroitin 6-sulfate
-
mutant enzyme H452A, in 50mM Tris/HCl, pH 8.0, at 37°C
683.3
chondroitin 6-sulfate
-
mutant enzyme H456A, in 50mM Tris/HCl, pH 8.0, at 37°C
2200
chondroitin 6-sulfate
-
wild type enzyme, in 50mM Tris/HCl, pH 8.0, at 37°C
8.3
dermatan sulfate
-
mutant enzyme H452A, in 50mM Tris/HCl, pH 8.0, at 37°C
316.7
dermatan sulfate
-
mutant enzyme H456A, in 50mM Tris/HCl, pH 8.0, at 37°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
micromethods for the measurement of as little as 3 pg of chondroitin sulfate A, B, or C in mixtures with other mucopolysaccharides or in urine
additional information
-
micromethods for the measurement of as little as 3 pg of chondroitin sulfate A, B, or C in mixtures with other mucopolysaccharides or in urine
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.6
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 40
no significant reduction in activity at temperatures in the range of 25-40 °C
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
growth on medium containing chondroitin sulfate C
-
-
brenda
isoform chondroitinase AC, upon growth on peptone with or without the inducer chondroitin sulfate, high specific activities for chondroitinases during the initial 6 h, which decreased thereafter. In contrast, in tryptic soy broth, high specific activities were obtained after 24 h growth in the presence of the inducer, generating large amounts of chondroitinase-rich extracts
-
-
brenda
induction of enzyme by addition of chondroitin sulfate C to growth medium
-
-
brenda
NCTC 4636, induced by chondroitin sulfate, isoenzyme ChS ABC lyase II
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
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). CABC2_BACTN
Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / VPI-5482 / E50)
1014
0
114839
Swiss-Prot
-
A0A1Q2MEB8_9BACT
1036
1
118223
TrEMBL
-
A0A7Y9EPQ0_9ACTN
1058
0
115458
TrEMBL
-
A0A1Q2MED2_9BACT
1459
0
161708
TrEMBL
-
A0A644WH06_9ZZZZ
1021
0
115732
TrEMBL
Secretory Pathway (Reliability: 1)
A0A644VGU6_9ZZZZ
1075
1
121456
TrEMBL
Secretory Pathway (Reliability: 1)
A0A077ERI8_9VIBR
811
0
90183
TrEMBL
Mitochondrion (Reliability: 2)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
104000
-
x * 108000, isoenzyme I, x * 104000, isoenzyme II, SDS-PAGE
108000
-
x * 108000, isoenzyme I, x * 104000, isoenzyme II, SDS-PAGE
150000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure identifies additional structurally conserved residues potentially involved in catalysis. A conserved cluster located 12 A from the catalytic tetrad is shown. A His in this cluster is essential for catalysis of dermatane sulfate but not chondroitin sulfate. The enzyme utilizes a single substrate-binding site while having two partially overlapping active sites catalyzing the respective reactions. The spatial separation of the two sets of residues suggests a substrate-induced conformational change that brings all catalytically essential residues close together
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E628Q
Km (mM) (chondroitin sulfate A) 0.158, (chondroitin sulfate C) 0.035, kcat (1/sec) (chondroitin sulfate A) 10.38, (chondroitin sulfate B) 4.41, no activity toward dermatan sulfate
H344A
Km (mM) (chondroitin sulfate A) 0.202, (chondroitin sulfate C) 0.134, kcat (1/sec) (chondroitin sulfate A) 92.66, (chondroitin sulfate B) 35.71, no activity toward dermatan sulfate
H344N
Km (mM) (chondroitin sulfate A) 0.039, (chondroitin sulfate C) 0.084, (dermatan sulfate) 0.09, kcat (1/sec) (chondroitin sulfate A) 42.2, (chondroitin sulfate B) 18.7, (dermatan sulfate) 9.06
H344Q
Km (mM) (chondroitin sulfate A) 0.073, kcat (1/sec) (chondroitin sulfate A) 16.78, no activity toward dermatan sulfate or chondroitin sulfate C
H345A
Km (mM) (chondroitin sulfate A) 0.171, (chondroitin sulfate C) 0.195, kcat (1/sec) (chondroitin sulfate A) 63, (chondroitin sulfate B) 30.88, no activity toward dermatan sulfate
H345N
Km (mM) (chondroitin sulfate A) 0.061, (chondroitin sulfate C) 0.026, kcat (1/sec) (chondroitin sulfate A) 21, (chondroitin sulfate B) 6.6, no activity toward dermatan sulfate
H345Q
Km (mM) (chondroitin sulfate A) 0.045, (chondroitin sulfate C) 0.102, kcat (1/sec) (chondroitin sulfate A) 23.46, (chondroitin sulfate B) 10.85, no activity toward dermatan sulfate
H453A
Km (mM) (chondroitin sulfate A) 0.038, (chondroitin sulfate C) 0.02, (dermatan sulfate) 0.044, kcat (1/sec) (chondroitin sulfate A) 17, (chondroitin sulfate B) 6.41, (dermatan sulfate) 5.8
H453N
Km (mM) (chondroitin sulfate A) 0.034, (chondroitin sulfate C) 0.012, kcat (1/sec) (chondroitin sulfate A) 13.15, (chondroitin sulfate B) 6.8, no activity toward dermatan sulfate
Q173A
Km (mM) (chondroitin sulfate A) 0.102, (chondroitin sulfate C) 0.050, (dermatan sulfate) 0.071, kcat (1/sec) (chondroitin sulfate A) 123, (chondroitin sulfate B) 33, (dermatan sulfate) 6.8
R267A
Km (mM) (chondroitin sulfate A) 0.109, (chondroitin sulfate C) 0.098, (dermatan sulfate) 0.071, kcat (1/sec) (chondroitin sulfate A) 205, (chondroitin sulfate B) 61.7, (dermatan sulfate) 4.1
E608A
-
the mutant does not show detectable activity on either chondroitin 6-sulfate or dermatan sulfate
H452A
-
the mutant shows similar Km values to the wild type enzyme but a 100fold reduced catalytic efficiency
H453A
-
the mutant does not show detectable activity on either chondroitin 6-sulfate or dermatan sulfate
R500A
R513A
-
the mutant does not show detectable activity on either chondroitin 6-sulfate or dermatan sulfate
Y460A
-
the mutant does not show detectable activity on either chondroitin 6-sulfate or dermatan sulfate
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
-
chABC loses ist enzymatic activity rapidly at 37°C, while thermostabilized chABC remains active at 37°C in vitro for up to 4 weeks
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
sensitive to lyophilization and freezing and thawing, both isoenzyme I and II
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, two weeks, 70-80% residual activity, both isoenzyme I and II
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
isoform chondroitinase AC, cell disruption by ultrasound, under mild conditions, solubilization of most of enzyme activity
-
using a combination of DEAE-, Ni-NTA-, Mono-S HR 10/10, and HiLoad 16/60 Superdex 200-columns
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli as a His-tagged fusion protein
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
biotechnology
-
preservation of ChABC activity during release by immobilizing ChABC in chitosan nerve conduits and encapsulating ChABC in poly(DL-lactic acid) microspheres using an appropriate stabilizer. Immobilizing ChABC in nerve conduitss markedly improves its stability. The activity of ChABC that is immobilized in chitosan nerve conduits by ionic bonding is 0.07 U/mg. 48% of this activity is retained at 48 h after immobilization. Poly(DL-lactic acid) microspheres, fabricated by the double emulsion method, are applied as carriers in the controlled release of ChABC. Stabilizers, including nanogold of 10 nm, polylysine of Mw 500-2000 and polylysine of Mw 20000-30000, are added to microspheres to maintain the activity of ChABC. Polylysine stabilizes ChABC most effectively. The ChABC activity is 0.0162 U/ml after seven days of release
medicine
synthesis
-
Production of enzyme for industrial use. Induction of enzyme by addition of chondroitin sulfate C to growth medium. Optimal conditions are pH 8.0, 25°C, plus the addition of yeast extract, peptone and casamino acid. Induction is inhibited by chloramphenicol and actinomycin D
analysis
-
micromethods for the measurement of as little as 3 pg of chondroitin sulfate A, B, or C in mixtures with other mucopolysaccharides or in urine
analysis
-
micromethods for the measurement of as little as 3 pg of chondroitin sulfate A, B, or C in mixtures with other mucopolysaccharides or in urine
analysis
enzyme combined with chodroitin sulfatase ABC, EC 4.2.2.4, can be applied for the sequencing of chondroitin sulfate hexa- and octasaccharides with complex structures
analysis
-
micromethods for the measurement of as little as 3 pg of chondroitin sulfate A, B, or C in mixtures with other mucopolysaccharides or in urine
-
medicine
-
sustained delivery of thermostabilized chABC enhances axonal sprouting and functional recovery after spinal cord injury. Animals treated with thermostabilized chABC in combination with sustained neurotrophin-3 delivery show significant improvement in locomotor function and enhanced growth of cholera toxin B subunit-positive sensory axons and sprouting of serotonergic fibers
medicine
-
the combination of cell transplantation with ChABC may be a potent therapeutic strategy for spinal cord injury
medicine
-
preservation of ChABC activity during release by immobilizing ChABC in chitosan nerve conduits and encapsulating ChABC in poly(DL-lactic acid) microspheres using an appropriate stabilizer. Immobilizing ChABC in nerve conduitss markedly improves its stability. The activity of ChABC that is immobilized in chitosan nerve conduits by ionic bonding is 0.07 U/mg. 48% of this activity is retained at 48 h after immobilization. Poly(DL-lactic acid) microspheres, fabricated by the double emulsion method, are applied as carriers in the controlled release of ChABC. Stabilizers, including nanogold of 10 nm, polylysine of Mw 500-2000 and polylysine of Mw 20000-30000, are added to microspheres to maintain the activity of ChABC. Polylysine stabilizes ChABC most effectively. The ChABC activity is 0.0162 U/ml after seven days of release
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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, Proteus vulgaris
brenda
Michelacci, Y.M.; Horton, D.S.P.Q.; Poblacion, C.A.
Isolation and characterization of an induced chondroitinase ABC from Flavobacterium heparinum
Biochim. Biophys. Acta
923
291-301
1987
Pedobacter heparinus
brenda
Sato, N.; Murata, K.; Kimura, A.
Cultural conditions for the induction of chondroitinase ABC in Proteus vulgaris cells
J. Ferment. Technol.
64
155-159
1986
Proteus vulgaris
-
brenda
Sato, N.; Murata, K.; Kimura, A.
Subunit structure of chondroitinase ABC from Proteus vulgaris
Agric. Biol. Chem.
50
1057-1059
1986
Proteus vulgaris
-
brenda
Yamagata, T.; Saito, H.; Habuchi, O.; Suzuki, S.
Purification and properties of bacterial chondroitinases and chondrosulfatases
J. Biol. Chem.
243
1523-1535
1968
Pedobacter heparinus, Proteus vulgaris, Proteus vulgaris NCTC 4636
brenda
Linn, S.; Chan, T.; Lipeski, L.; Salyers, A.A.
Isolation and characterization of two chondroitin lyases from Bacteroides thetaiotaomicron
J. Bacteriol.
156
859-866
1983
Bacteroides thetaiotaomicron
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
Takagaki, K.; Munakata, H.; Majima, M.; Kakizaki, I.; Endo, M.
Chimeric glycosaminoglycan oligosaccharides synthesized by enzymatic reconstruction and their use in substrate specificity determination of Streptococcus hyaluronidase
J. Biochem.
127
695-702
2000
Streptococcus dysgalactiae
brenda
Hamai, A.; Hashimoto, N.; Mochizuki, H.; Kato, F.; Makiguchi, Y.; Horie, K.; Suzuki, S.
Two distinct chondroitin sulfate ABC lyases. An endoeliminase yielding tetrasaccharides and an exoeliminase preferentially acting on oligosaccharides
J. Biol. Chem.
272
9123-9130
1997
Proteus vulgaris
brenda
Prabhakar, V.; Capila, I.; Bosques, C.J.; Pojasek, K.; Sasisekharan, R.
Chondroitinase ABC I from Proteus vulgaris: cloning, recombinant expression and active site identification
Biochem. J.
386
103-112
2005
Proteus vulgaris
brenda
Prabhakar, V.; Raman, R.; Capila, I.; Bosques, C.J.; Pojasek, K.; Sasisekharan, R.
Biochemical characterization of the chondroitinase ABC I active site
Biochem. J.
390
395-405
2005
Proteus vulgaris
brenda
Saito, H.; Yamagata, T.; Suzuki, S.
Enzymatic methods for the determination of small quantities of isomeric chondroitin sulfates
J. Biol. Chem.
243
1536-1542
1968
Pedobacter heparinus, Proteus vulgaris, Proteus vulgaris NCTC 4636
brenda
Suzuki, S.; Saito, H.; Yamagata, T.; Anno, K.; Seno, N.; Kawai, Y.; Furuhashi, T.
Formation of three types of disulfated disaccharides from chondroitin sulfates by chondroitinase digestion
J. Biol. Chem.
243
1543-1550
1968
Proteus vulgaris
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, Bacteroides thetaiotaomicron (Q8A2I1)
brenda
Shaya, D.; Hahn, B.; Park, N.Y.; Sim, J.; Kim, Y.S.; Cygler, M.
Characterization of Chondroitin Sulfate Lyase ABC from Bacteroides thetaiotaomicron WAL2926
Biochemistry
47
6650-6661
2008
Bacteroides thetaiotaomicron (Q8A2I1), Bacteroides thetaiotaomicron
brenda
Shaya, D.; Hahn, B.; Bjerkan, T.M.; Kim, W.S.; Park, N.Y.; Sim, J.; Kim, Y.; Cygler, M.
Composite active site of chondroitin lyase ABC accepting both epimers of uronic acid
Glycobiology
18
270-277
2008
Bacteroides thetaiotaomicron (Q8A2I1)
brenda
Prabhakar, V.; Capila, I.; Soundararajan, V.; Raman, R.; Sasisekharan, R.
Recombinant expression, purification, and biochemical characterization of chondroitinase ABC II from Proteus vulgaris
J. Biol. Chem.
284
974-982
2009
Proteus vulgaris
brenda
Huang, W.C.; Kuo, W.C.; Hsu, S.H.; Cheng, C.H.; Liu, J.C.; Cheng, H.
Gait analysis of spinal cord injured rats after delivery of chondroitinase ABC and adult olfactory mucosa progenitor cell transplantation
Neurosci. Lett.
472
79-84
2010
Proteus vulgaris
brenda
Nakamae, T.; Tanaka, N.; Nakanishi, K.; Kamei, N.; Sasaki, H.; Hamasaki, T.; Yamada, K.; Yamamoto, R.; Izumi, B.; Ochi, M.
The effects of combining chondroitinase ABC and NEP1-40 on the corticospinal axon growth in organotypic co-cultures
Neurosci. Lett.
476
14-17
2010
Proteus vulgaris
brenda
Lee, H.; McKeon, R.J.; Bellamkonda, R.V.
Sustained delivery of thermostabilized chABC enhances axonal sprouting and functional recovery after spinal cord injury
Proc. Natl. Acad. Sci. USA
107
3340-3345
2010
Proteus vulgaris
brenda
Huang, Y.; Hsu, S.; Chen, M.; Hsieh, C.; Kuo, W.; Cheng, H.; Huang, Y.
Controlled release of chondroitinase ABC in chitosan-based scaffolds and PDLLA microspheres
Carbohydr. Polym.
84
788-793
2011
Proteus vulgaris
brenda
Wang, W.; Cai, X.; Han, N.; Han, W.; Sugahara, K.; Li, F.
Sequencing of chondroitin sulfate oligosaccharides using a novel exolyase from a marine bacterium that degrades hyaluronan and chondroitin sulfate/dermatan sulfate
Biochem. J.
474
3831-3848
2017
Vibrio sp. FC509 (A0A077ERI8)
brenda
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