Activating Compound | Comment | Organism | Structure |
---|---|---|---|
K2SO4 | 280-300% activity at 150-200 mM | Aeropyrum pernix K1 | |
K3PO4 | less effective than K2SO4 and Na3PO4 | Aeropyrum pernix K1 | |
KCl | 170-200% activity at 50-100 mM | Aeropyrum pernix K1 | |
Na2SO4 | less effective than K2SO4 and Na3PO4 | Aeropyrum pernix K1 | |
Na3PO4 | 280-300% activity at 150-200 mM | Aeropyrum pernix K1 | |
NaCl | 170-200% activity at 50-100 mM | Aeropyrum pernix K1 |
Cloned (Comment) | Organism |
---|---|
expressed in Escherichia coli | Aeropyrum pernix |
expression in Escherichia coli | Aeropyrum pernix |
expression in Escherichia coli JM109 | Aeropyrum pernix K1 |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.022 | - |
NADPH | reductive amination at 50°C | Aeropyrum pernix K1 | |
0.022 | - |
NADPH | pH 8.3, 50°C | Aeropyrum pernix | |
0.039 | - |
NADP+ | oxidative deamination at 50°C | Aeropyrum pernix K1 | |
0.039 | - |
NADP+ | pH 8.3, 50°C | Aeropyrum pernix | |
1.7 | - |
2-oxoglutarate | reductive amination at 50°C | Aeropyrum pernix K1 | |
1.7 | - |
2-oxoglutarate | pH 8.3, 50°C | Aeropyrum pernix | |
3.3 | - |
L-glutamate | oxidative deamination at 50°C | Aeropyrum pernix K1 | |
3.3 | - |
L-glutamate | pH 8.3, 50°C | Aeropyrum pernix | |
83 | - |
NH4+ | reductive amination at 50°C | Aeropyrum pernix K1 | |
83 | - |
NH3 | pH 8.3, 50°C | Aeropyrum pernix |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
K2SO4 | enhances the activity by a maximum of about 280-300% at a concentration of 150-200 mM | Aeropyrum pernix | |
KCl | maximum enhancement of about 170200% of the relative activity at a concentration of 50100 mM | Aeropyrum pernix | |
Na3PO4 | enhances the activity by a maximum of about 280-300% at a concentration of 150-200 mM | Aeropyrum pernix | |
NaCl | maximum enhancement of about 170200% of the relative activity at a concentration of 50100 mM | Aeropyrum pernix |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
46000 | - |
6 * 46000, SDS-PAGE | Aeropyrum pernix |
46000 | - |
alpha6, 6 * 46000, SDS-PAGE | Aeropyrum pernix K1 |
46170 | - |
x * 46170, amino acid analysis | Aeropyrum pernix K1 |
46170 | - |
6 * 46170, calculated from sequence | Aeropyrum pernix |
270000 | - |
gel filtration | Aeropyrum pernix |
270000 | - |
gel filtration, expressed in Escherichia coli | Aeropyrum pernix K1 |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-glutamate + NADP+ + H2O | Aeropyrum pernix K1 | - |
2-oxoglutarate + NADPH + NH3 | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Aeropyrum pernix | - |
- |
- |
Aeropyrum pernix | Q9YC65 | - |
- |
Aeropyrum pernix DSM 11879 | Q9YC65 | - |
- |
Aeropyrum pernix K1 | - |
- |
- |
Purification (Comment) | Organism |
---|---|
- |
Aeropyrum pernix |
- |
Aeropyrum pernix K1 |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
5.2 | - |
pH 8.3, 50°C | Aeropyrum pernix |
Storage Stability | Organism |
---|---|
4°C, 2 months, no activity loss | Aeropyrum pernix K1 |
4°C, 2 months, no loss of activity | Aeropyrum pernix |
4°C, stable for at least 2 months | Aeropyrum pernix |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2-oxoglutarate + NH4+ + NADPH | - |
Aeropyrum pernix K1 | L-glutamate + NADP+ | - |
? | |
L-glutamate + H2O + NADP+ | the enzyme shows a strict specificity for L-glutamate and NADP+ on oxidative deamination and for 2-oxoglutarate and NADPH on reductive amination. No activity with the following amino acids in oxidative deamination: D-glutamate, L-norvaline, L-2-aminobutyrate, L-valine, L-alanine, L-aspartate, L-serine, L-cysteine, L-lysine, or L-phenylalanin. No activity with the following amino acids in reductive amination: pyruvate, 2-oxovalerate, 2-oxoisocaproate, 2-oxobutyrate, or 2-oxoisovalerate | Aeropyrum pernix | 2-oxoglutarate + NH3 + NADPH + H+ | - |
r | |
L-glutamate + H2O + NADP+ | the enzyme shows a strict specificity for L-glutamate and NADP+ on oxidative deamination and for 2-oxoglutarate and NADPH on reductive amination | Aeropyrum pernix | 2-oxoglutarate + NH3 + NADPH + H+ | - |
? | |
L-glutamate + H2O + NADP+ | the enzyme shows a strict specificity for L-glutamate and NADP+ on oxidative deamination and for 2-oxoglutarate and NADPH on reductive amination | Aeropyrum pernix DSM 11879 | 2-oxoglutarate + NH3 + NADPH + H+ | - |
? | |
L-glutamate + NADP+ + H2O | - |
Aeropyrum pernix K1 | 2-oxoglutarate + NADPH + NH3 | - |
r |
Subunits | Comment | Organism |
---|---|---|
? | x * 46170, amino acid analysis | Aeropyrum pernix K1 |
hexamer | 6 * 46000, SDS-PAGE | Aeropyrum pernix |
hexamer | 6 * 46170, calculated from sequence | Aeropyrum pernix |
homohexamer | alpha6, 6 * 46000, SDS-PAGE | Aeropyrum pernix K1 |
Synonyms | Comment | Organism |
---|---|---|
APE1386 | - |
Aeropyrum pernix |
GluDH | - |
Aeropyrum pernix |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
50 | - |
assay at | Aeropyrum pernix |
50 | - |
assay at 50°C because of instability of NADP+ under assay conditions | Aeropyrum pernix |
100 | - |
- |
Aeropyrum pernix |
100 | - |
oxidative deamination | Aeropyrum pernix K1 |
100 | - |
maximum activity in L-glutamate deamination | Aeropyrum pernix |
Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|
50 | 100 | the activity of the enzyme increases with an increase in temperature from 50° to 100°C. The highest activity is observed at 100°C and is about 15 times than that at 50°C | Aeropyrum pernix |
50 | 100 | the activity of the enzyme increases with an increase in temperature from 50° to 100°C. The highest activity is observed at 100°C and is about 15 times that at 50°C | Aeropyrum pernix |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
85 | - |
recombinant enzyme fully active after 30 min | Aeropyrum pernix K1 |
95 | - |
fully active after 30 min | Aeropyrum pernix K1 |
95 | - |
30 min, the enzyme retains its full activity | Aeropyrum pernix |
95 | - |
30 min, the enzyme retains full activity | Aeropyrum pernix |
100 | - |
30 min, 5% loss of activity | Aeropyrum pernix |
100 | - |
fully active after 30 min | Aeropyrum pernix K1 |
100 | - |
30 min, enzyme loses 5% of its activity | Aeropyrum pernix |
115 | - |
10 min, complete loss of activity | Aeropyrum pernix |
115 | - |
inactivation after 10 min | Aeropyrum pernix K1 |
115 | - |
10 min, the enzyme completely loses activity | Aeropyrum pernix |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8.1 | 8.4 | reductive amination at 50°C | Aeropyrum pernix K1 |
8.1 | 8.4 | amination of 2-oxoglutarate. Determined at 50°C in 125 mM glycylglycine/NaOH buffer | Aeropyrum pernix |
8.1 | 8.4 | amination of 2-oxoglutarate, at 50°C in 125 mM glycylglycine/NaOH buffer | Aeropyrum pernix |
8.3 | - |
assay at | Aeropyrum pernix |
8.3 | 8.7 | oxidative deamination at 50°C | Aeropyrum pernix K1 |
8.3 | 8.7 | deamination of L-glutamate. Determined at 50°C in 125 mM glycylglycine/NaOH buffer | Aeropyrum pernix |
8.3 | 8.7 | deamination of L-glutamate, at 50°C in 125 mM glycylglycine/NaOH buffer | Aeropyrum pernix |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
5 | 10 | fully active | Aeropyrum pernix K1 |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NADP+ | - |
Aeropyrum pernix K1 | |
NADP+ | the enzyme requires NADP+ as the coenzyme for the oxidation of L-glutamate, which can not be replaced by NAD+ | Aeropyrum pernix | |
NADP+ | no acrivity with NAD+ | Aeropyrum pernix | |
NADPH | - |
Aeropyrum pernix K1 | |
NADPH | no activity with NADP+ | Aeropyrum pernix | |
NADPH | for the reduction of 2-oxoglutarate, NADPH is the coenzyme and NADH is inert | Aeropyrum pernix |