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Literature summary for 4.2.2.2 extracted from

  • Herron, S.R.; Benen, J.A.E.; Scavetta, R.D.; Visser, J.; Jurnak, F.
    Structure and function of pectic enzymes: virulence factors of plant pathogens (2000), Proc. Natl. Acad. Sci. USA, 97, 8762-8769.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 4.2.2.2

Protein Variants

Protein Variants Comment Organism
D154E mutant enzyme with 44% of the activity of the wild-type enzyme, the Km-value for the substrate lime pectin (with 75% methyl esterification) is 1.2fold higher than the Km-value of the wild-type enzyme Dickeya chrysanthemi
D154N mutant enzyme with 44% of the activity of the wild-type enzyme, the Km-value for the substrate lime pectin (with 75% methyl esterification) is 2.3fold higher than the Km-value of the wild-type enzyme. The pH-optimum is higher than that of the wild-type enzyme Dickeya chrysanthemi
R236K mutant enzyme with 0.2% of the activity of the wild-type enzyme Dickeya chrysanthemi
R236Q inactive mutant enzyme Dickeya chrysanthemi

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information Km-value for lime pectin with 75% methyl esterification: 6.3 mg/ml for wild-type enzyme, 7.8 mg/ml for mutant enzyme D154E, 14.8 mg/ml for mutant enzyme D154N, at 30°C and pH 8.5 Dickeya chrysanthemi

Organism

Organism UniProt Comment Textmining
Dickeya chrysanthemi
-
-
-

Purification (Commentary)

Purification (Comment) Organism
wild-type and mutant enzymes Dickeya chrysanthemi

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
lime pectin with 75% methyl esterification Dickeya chrysanthemi ?
-
 ?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5
-
 wild-type enzyme, mutant enzyme R236K and mutant enzyme D154E, lime pectin as substrate Dickeya chrysanthemi
9.5
-
 above, mutant enzyme D154N, lime pectin as substrate Dickeya chrysanthemi