BRENDA - Enzyme Database

Studies on the phosphomannose isomerase of Amorphophallus konjac C. Koch II. Effect of divalent metal ions on the EDTA-treated enzyme

Murata, T.; Plant Cell Physiol. 16, 963-970 (1975)
No PubMed abstract available

Data extracted from this reference:

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
Commentary
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
Commentary
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
Primary Accession No. (UniProt)
Commentary
Textmining
5.3.1.8
Amorphophallus konjac
-
-
-
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
5.3.1.8
D-Mannose 6-phosphate
-
2809
Amorphophallus konjac
D-Fructose 6-phosphate
-
2809
Amorphophallus konjac
-
Temperature Stability [C]
EC Number
Temperature Stability Minimum [C]
Temperature Stability Maximum [C]
Commentary
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
General Stability (protein specific)
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 (protein specific)
EC Number
Inhibitors
Commentary
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 (protein specific)
EC Number
Metals/Ions
Commentary
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
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
5.3.1.8
D-Mannose 6-phosphate
-
2809
Amorphophallus konjac
D-Fructose 6-phosphate
-
2809
Amorphophallus konjac
-
Temperature Stability [C] (protein specific)
EC Number
Temperature Stability Minimum [C]
Temperature Stability Maximum [C]
Commentary
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