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Literature summary for 1.4.1.4 extracted from

  • Bhuiya, M.W.; Sakuraba, H.; Kujo, C.; Nunoura-Kominato, N.; Kawarabayasi, Y.; Kikuchi, H.; Ohshima, T.
    Glutamate dehydrogenase from the aerobic hyperthermophilic archaeon Aeropyrum pernix K1: enzymatic characterization, identification of the encoding gene, and phylogenetic implications (2000), Extremophiles, 4, 333-341.
    View publication on PubMed
Search for more literature for 1.4.1.4

Activating Compound

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(Commentary)

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 [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

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 170–200% of the relative activity at a concentration of 50–100 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 170–200% of the relative activity at a concentration of 50–100 mM Aeropyrum pernix

Molecular Weight [Da]

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/ Products (Substrates)

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

Organism UniProt Comment Textmining
Aeropyrum pernix
-
-
-
Aeropyrum pernix Q9YC65
-
-
Aeropyrum pernix DSM 11879 Q9YC65
-
-
Aeropyrum pernix K1
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Aeropyrum pernix
-
 Aeropyrum pernix K1

Specific Activity [micromol/min/mg]

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

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 and Products (Substrate)

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

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

Synonyms Comment Organism
APE1386
-
 Aeropyrum pernix
GluDH
-
 Aeropyrum pernix

Temperature Optimum [°C]

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 Range [°C]

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 [°C]

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

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 Range

pH Minimum pH Maximum Comment Organism
5 10 fully active Aeropyrum pernix K1

Cofactor

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