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Literature summary for 4.1.3.1 extracted from

  • Griffiths, M.W.; Sundaram, T.K.
    Isocitrate lyase from a thermophilic Bacillus: effect of salts on enzyme activity (1973), J. Bacteriol., 116, 1160-1169.
    View publication on PubMedView publication on EuropePMC

Inhibitors

Inhibitors Comment Organism Structure
KCl at pH-values above 8.6 inhibition, below pH 8.6 activation by KCl Bacillus sp. (in: Bacteria)
NaCl activation by NaCl Bacillus sp. (in: Bacteria)

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
Bacillus sp. (in: Bacteria)

Organism

Organism UniProt Comment Textmining
Bacillus sp. (in: Bacteria)
-
thermophilic
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
isocitrate
-
Bacillus sp. (in: Bacteria) succinate + glyoxylate
-
r

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
KCl, MgCl2, CaCl2 stabilize Bacillus sp. (in: Bacteria)
55.5
-
50% activity lost after 43 min, in presence of 0.4 M KCl 50% activity lost after 129 min Bacillus sp. (in: Bacteria)
60
-
50% activity lost after 5 min, in presence of 0.4 M KCl 50% activity lost after 4 min Bacillus sp. (in: Bacteria)

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
presence of 0.3 M KCl Bacillus sp. (in: Bacteria)
8
-
absence of KCl Bacillus sp. (in: Bacteria)