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Literature summary for 4.2.2.2 extracted from

  • Soriano, M.; Diaz, P.; Pastor, F.I.J.
    Pectate lyase C from Bacillus subtilis: a novel endo-cleaving enzyme with activity on highly methylated pectin (2006), Microbiology, 152, 617-625.
    View publication on PubMed
Search for more literature for 4.2.2.2

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Bacillus subtilis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information KM-value is 0.13 mg/ml for 22% esterified pectin, the KM-value is 0.15 mg/ml for polygalacturonic acid Bacillus subtilis

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ absolute requirement Bacillus subtilis
Hg2+ 1 mM, can replace Ca2+ in activation Bacillus subtilis

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme Bacillus subtilis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
pectin of methyl esterification degree from 22% to 89%, maximal activity on 22% esterified citrus pectin Bacillus subtilis ?
-
 ?
polygalacturonate
-
 Bacillus subtilis ?
-
 ?

Synonyms

Synonyms Comment Organism
pectate lyase C
-
 Bacillus subtilis
pelC
-
 Bacillus subtilis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
65
-
-
 Bacillus subtilis

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
50 80 50°C: about 60% of maximal activity, 80°C: about 60% of maximal activity Bacillus subtilis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
10
-
-
 Bacillus subtilis

pH Range

pH Minimum pH Maximum Comment Organism
9 11 pH 9: about 40% of maximal activity, pH 11: about 50% of maximal activity Bacillus subtilis