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Literature summary extracted from

  • Michel, G.; Pojasek, K.; Li, Y.; Sulea, T.; Linhardt, R.J.; Raman, R.; Prabhakar, V.; Sasisekharan, R.; Cygler, M.
    The structure of chondroitin B lyase complexed with glycosaminoglycan oligosaccharides unravels a calcium-dependent catalytic machinery (2004), J. Biol. Chem., 279, 32882-32896.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.2.2.19 purified recombinant wild-type enzyme complexed with dermatan sulfate pentasaccharide and hexasaccharide, or chondroitin-4-sulfate tetrasacharide, X-ray diffraction structure determination and analysis at 1.7-1.8 A resolution, modeling of substrate binding in the active site groove Pedobacter heparinus

Protein Variants

EC Number Protein Variants Comment Organism
4.2.2.19 E243A site-directed mutagenesis, Ca2+-binding residue, about 3.6fold reduced activity compared to the wild-type enzyme Pedobacter heparinus
4.2.2.19 E243A/E245A site-directed mutagenesis, Ca2+-binding residue, about 4fold reduced activity compared to the wild-type enzyme Pedobacter heparinus
4.2.2.19 E245A site-directed mutagenesis, Ca2+-binding residue, about 6fold reduced activity compared to the wild-type enzyme Pedobacter heparinus
4.2.2.19 N213Q site-directed mutagenesis, Ca2+-binding residue, about 6fold reduced activity compared to the wild-type enzyme Pedobacter heparinus
4.2.2.19 R271E site-directed mutagenesis, active site mutant, catalytically inactive Pedobacter heparinus
4.2.2.19 R271K site-directed mutagenesis, active site mutant, about 10fold reduced activity compared to the wild-type enzyme Pedobacter heparinus

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.2.2.19 EGTA complete inhibition Pedobacter heparinus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.2.2.19 0.0012
-
 dermatan sulfate recombinant wild-type enzyme, pH 8.0, 30°C, in presence of 5 mM Ca2+ Pedobacter heparinus
4.2.2.19 0.0043
-
 dermatan sulfate recombinant wild-type enzyme, pH 8.0, 30°C, in presence of 0.01 mM Ca2+ Pedobacter heparinus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.2.2.19 Ca2+ dependent on, required for catalysis, activates, protein-Ca2+-oligosaccharide complex Pedobacter heparinus

Organism

EC Number Organism UniProt Comment Textmining
4.2.2.19 Pedobacter heparinus Q46079 i.e. Flavobacterium heparinum
-

Reaction

EC Number Reaction Comment Organism Reaction ID
4.2.2.19 [dermatan sulfate]n = [dermatan sulfate]n-1 + 4-deoxy-beta-D-gluc-4-enuronosyl-1,3-GalNAc acts on dermatan sulfate as sole substrate, enzyme cleaves the beta(1,4)-linkage of dermatan sulfate in a random manner, yielding 4,5-unsaturated dermatan sulfate disaccharides, calcium-dependent catalytic mechanism, active site structure Pedobacter heparinus
a

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.2.2.19 additional information
-
-
 Pedobacter heparinus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.2.19 dermatan sulfate strictly specific for Pedobacter heparinus ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.2.2.19 ChonB
-
 Pedobacter heparinus
4.2.2.19 chondroitinase B
-
 Pedobacter heparinus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.2.2.19 30
-
 assay at Pedobacter heparinus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.2.2.19 210
-
 dermatan sulfate recombinant wild-type enzyme, pH 8.0, 30°C, in presence of 0.01 mM Ca2+ Pedobacter heparinus
4.2.2.19 410
-
 dermatan sulfate recombinant wild-type enzyme, pH 8.0, 30°C, in presence of 5 mM Ca2+ Pedobacter heparinus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.2.2.19 8
-
 assay at Pedobacter heparinus