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Literature summary extracted from

  • Murata, T.
    Studies on the phosphomannose isomerase of Amorphophallus konjac C. Koch II. Effect of divalent metal ions on the EDTA-treated enzyme (1975), Plant Cell Physiol., 16, 963-970.
No PubMed abstract available

General Stability

EC Number General Stability Organism
5.3.1.8 EDTA-treated enzyme and 1,10-phenanthroline-treated enzyme is more susceptible to heat denaturation, addition of various metal ions causes the recovery of thermal stability. The most effective metal ion is Co2+, which causes the recovery of thermal stability to a level higher than that of the native enzyme Amorphophallus konjac

Inhibitors

EC Number Inhibitors Comment Organism Structure
5.3.1.8 1,10-phenanthroline
-
 Amorphophallus konjac
5.3.1.8 EDTA
-
 Amorphophallus konjac
5.3.1.8 HgCl2
-
 Amorphophallus konjac
5.3.1.8 PCMB
-
 Amorphophallus konjac

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
5.3.1.8 Co2+ can reverse inhibition by a metal binding agent Amorphophallus konjac
5.3.1.8 Fe2+ can reverse inhibition by a metal binding agent Amorphophallus konjac
5.3.1.8 Mn2+ can reverse inhibition by a metal binding agent Amorphophallus konjac
5.3.1.8 Zn2+ at low concentrations complete reactivation of enzyme inhibited by a metal binding agent Amorphophallus konjac

Organism

EC Number Organism UniProt Comment Textmining
5.3.1.8 Amorphophallus konjac
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.3.1.8 D-Mannose 6-phosphate
-
 Amorphophallus konjac D-Fructose 6-phosphate
-
 ?

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
5.3.1.8 45
-
 pH 6.5, 30 min, native enzyme stable Amorphophallus konjac
5.3.1.8 55
-
 pH 6.5, 10 min, about 75% loss of native enzyme Amorphophallus konjac