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Literature summary for 5.3.1.8 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
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General Stability

General Stability Organism
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

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

Metals/Ions

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

Organism

Organism UniProt Comment Textmining
Amorphophallus konjac
-
-
-

Substrates and Products (Substrate)

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

Temperature Stability [°C]

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