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Literature summary for 4.2.2.20 extracted from

  • Chen, Z.; Li, Y.; Yuan, Q.
    Expression, purification and thermostability of MBP-chondroitinase ABC I from Proteus vulgaris (2014), Int. J. Biol. Macromol., 72, 6-10.
    View publication on PubMed
Search for more literature for 4.2.2.20

Cloned(Commentary)

Cloned (Comment) Organism
fusion protein with maltose-binding protein, expression in Escherichia coli Proteus vulgaris

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.073
-
 chondroitin sulfate A recombinant protein fused to maltose-binding protein, pH 7.4, 50°C Proteus vulgaris

Organism

Organism UniProt Comment Textmining
Proteus vulgaris P59807
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant protein Proteus vulgaris

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3180
-
 recombinant protein fused to maltose-binding protein, pH 7.4, 50°C Proteus vulgaris

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
chondroitin sulfate A
-
 Proteus vulgaris ?
-
 ?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
55
-
-
 Proteus vulgaris

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
30
-
 210 min, 78% residual activity Proteus vulgaris

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
587
-
 chondroitin sulfate A recombinant protein fused to maltose-binding protein, pH 7.4, 50°C Proteus vulgaris

pH Range

pH Minimum pH Maximum Comment Organism
7.7
-
 degeneration of protein above Proteus vulgaris