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Literature summary for 4.2.2.5 extracted from

  • Rye, C.S.; Matte, A.; Cygler, M.; Withers, S.G.
    An atypical approach identifies TYR234 as the key base catalyst in chondroitin AC lyase (2006), ChemBioChem, 7, 631-637.
    View publication on PubMed
Search for more literature for 4.2.2.5

Protein Variants

Protein Variants Comment Organism
Y234F mutant enzyme is inactive with chondroitin 6-sulfate Pedobacter heparinus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.6
-
 chondroitin 6-sulfate pH 6.8, 30°C, mutant enzyme Y234F Pedobacter heparinus
0.66
-
 chondroitin 6-sulfate pH 6.8, 30°C, wild-type enzyme Pedobacter heparinus
6.9
-
 4-O-(2',4'-dinitrophenyl)-beta-D-glucopyranosiruronic acid pH 6.8, 30°C, wild-type enzyme Pedobacter heparinus

Organism

Organism UniProt Comment Textmining
Pedobacter heparinus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-O-(2',4'-dinitrophenyl)-beta-D-glucopyranosiruronic acid
-
 Pedobacter heparinus ?
-
 ?
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 Pedobacter heparinus ?
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.041
-
 4-O-(2',4'-dinitrophenyl)-beta-D-glucopyranosiruronic acid pH 6.8, 30°C, wild-type enzyme Pedobacter heparinus
855
-
 chondroitin 6-sulfate pH 6.8, 30°C, wild-type enzyme Pedobacter heparinus