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Literature summary 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

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

Metals/Ions

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

Organism

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

Substrates and Products (Substrate)

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

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
4.1.3.1 additional information
-
KCl, MgCl2, CaCl2 stabilize Bacillus sp. (in: Bacteria)
4.1.3.1 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)
4.1.3.1 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

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.1.3.1 7.5
-
presence of 0.3 M KCl Bacillus sp. (in: Bacteria)
4.1.3.1 8
-
absence of KCl Bacillus sp. (in: Bacteria)