Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.4.1.4 K2SO4 280-300% activity at 150-200 mM Aeropyrum pernix K1
1.4.1.4 K3PO4 less effective than K2SO4 and Na3PO4 Aeropyrum pernix K1
1.4.1.4 KCl 170-200% activity at 50-100 mM Aeropyrum pernix K1
1.4.1.4 Na2SO4 less effective than K2SO4 and Na3PO4 Aeropyrum pernix K1
1.4.1.4 Na3PO4 280-300% activity at 150-200 mM Aeropyrum pernix K1
1.4.1.4 NaCl 170-200% activity at 50-100 mM Aeropyrum pernix K1

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.4.1.4 expressed in Escherichia coli Aeropyrum pernix
1.4.1.4 expression in Escherichia coli Aeropyrum pernix
1.4.1.4 expression in Escherichia coli JM109 Aeropyrum pernix K1

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.4.1.4 0.022
-
 NADPH reductive amination at 50°C Aeropyrum pernix K1
1.4.1.4 0.022
-
 NADPH pH 8.3, 50°C Aeropyrum pernix
1.4.1.4 0.039
-
 NADP+ oxidative deamination at 50°C Aeropyrum pernix K1
1.4.1.4 0.039
-
 NADP+ pH 8.3, 50°C Aeropyrum pernix
1.4.1.4 1.7
-
 2-oxoglutarate reductive amination at 50°C Aeropyrum pernix K1
1.4.1.4 1.7
-
 2-oxoglutarate pH 8.3, 50°C Aeropyrum pernix
1.4.1.4 3.3
-
 L-glutamate oxidative deamination at 50°C Aeropyrum pernix K1
1.4.1.4 3.3
-
 L-glutamate pH 8.3, 50°C Aeropyrum pernix
1.4.1.4 83
-
 NH4+ reductive amination at 50°C Aeropyrum pernix K1
1.4.1.4 83
-
 NH3 pH 8.3, 50°C Aeropyrum pernix

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.4.1.4 K2SO4 enhances the activity by a maximum of about 280-300% at a concentration of 150-200 mM Aeropyrum pernix
1.4.1.4 KCl maximum enhancement of about 170–200% of the relative activity at a concentration of 50–100 mM Aeropyrum pernix
1.4.1.4 Na3PO4 enhances the activity by a maximum of about 280-300% at a concentration of 150-200 mM Aeropyrum pernix
1.4.1.4 NaCl maximum enhancement of about 170–200% of the relative activity at a concentration of 50–100 mM Aeropyrum pernix

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.4.1.4 46000
-
 6 * 46000, SDS-PAGE Aeropyrum pernix
1.4.1.4 46000
-
 alpha6, 6 * 46000, SDS-PAGE Aeropyrum pernix K1
1.4.1.4 46170
-
 x * 46170, amino acid analysis Aeropyrum pernix K1
1.4.1.4 46170
-
 6 * 46170, calculated from sequence Aeropyrum pernix
1.4.1.4 270000
-
 gel filtration Aeropyrum pernix
1.4.1.4 270000
-
 gel filtration, expressed in Escherichia coli Aeropyrum pernix K1

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.4.1.4 L-glutamate + NADP+ + H2O Aeropyrum pernix K1
-
 2-oxoglutarate + NADPH + NH3
-
 r

Organism

EC Number Organism UniProt Comment Textmining
1.4.1.4 Aeropyrum pernix
-
-
-
1.4.1.4 Aeropyrum pernix Q9YC65
-
-
1.4.1.4 Aeropyrum pernix DSM 11879 Q9YC65
-
-
1.4.1.4 Aeropyrum pernix K1
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.4.1.4
-
 Aeropyrum pernix
1.4.1.4
-
 Aeropyrum pernix K1

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.4.1.4 5.2
-
 pH 8.3, 50°C Aeropyrum pernix

Storage Stability

EC Number Storage Stability Organism
1.4.1.4 4°C, 2 months, no activity loss Aeropyrum pernix K1
1.4.1.4 4°C, 2 months, no loss of activity Aeropyrum pernix
1.4.1.4 4°C, stable for at least 2 months Aeropyrum pernix

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.4.1.4 2-oxoglutarate + NH4+ + NADPH
-
 Aeropyrum pernix K1 L-glutamate + NADP+
-
 ?
1.4.1.4 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
1.4.1.4 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+
-
 ?
1.4.1.4 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+
-
 ?
1.4.1.4 L-glutamate + NADP+ + H2O
-
 Aeropyrum pernix K1 2-oxoglutarate + NADPH + NH3
-
 r

Subunits

EC Number Subunits Comment Organism
1.4.1.4 ? x * 46170, amino acid analysis Aeropyrum pernix K1
1.4.1.4 hexamer 6 * 46000, SDS-PAGE Aeropyrum pernix
1.4.1.4 hexamer 6 * 46170, calculated from sequence Aeropyrum pernix
1.4.1.4 homohexamer alpha6, 6 * 46000, SDS-PAGE Aeropyrum pernix K1

Synonyms

EC Number Synonyms Comment Organism
1.4.1.4 APE1386
-
 Aeropyrum pernix
1.4.1.4 GluDH
-
 Aeropyrum pernix

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.4.1.4 50
-
 assay at Aeropyrum pernix
1.4.1.4 50
-
 assay at 50°C because of instability of NADP+ under assay conditions Aeropyrum pernix
1.4.1.4 100
-
-
 Aeropyrum pernix
1.4.1.4 100
-
 oxidative deamination Aeropyrum pernix K1
1.4.1.4 100
-
 maximum activity in L-glutamate deamination Aeropyrum pernix

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
1.4.1.4 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
1.4.1.4 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]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.4.1.4 85
-
 recombinant enzyme fully active after 30 min Aeropyrum pernix K1
1.4.1.4 95
-
 fully active after 30 min Aeropyrum pernix K1
1.4.1.4 95
-
 30 min, the enzyme retains its full activity Aeropyrum pernix
1.4.1.4 95
-
 30 min, the enzyme retains full activity Aeropyrum pernix
1.4.1.4 100
-
 30 min, 5% loss of activity Aeropyrum pernix
1.4.1.4 100
-
 fully active after 30 min Aeropyrum pernix K1
1.4.1.4 100
-
 30 min, enzyme loses 5% of its activity Aeropyrum pernix
1.4.1.4 115
-
 10 min, complete loss of activity Aeropyrum pernix
1.4.1.4 115
-
 inactivation after 10 min Aeropyrum pernix K1
1.4.1.4 115
-
 10 min, the enzyme completely loses activity Aeropyrum pernix

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.4.1.4 8.1 8.4 reductive amination at 50°C Aeropyrum pernix K1
1.4.1.4 8.1 8.4 amination of 2-oxoglutarate. Determined at 50°C in 125 mM glycylglycine/NaOH buffer Aeropyrum pernix
1.4.1.4 8.1 8.4 amination of 2-oxoglutarate, at 50°C in 125 mM glycylglycine/NaOH buffer Aeropyrum pernix
1.4.1.4 8.3
-
 assay at Aeropyrum pernix
1.4.1.4 8.3 8.7 oxidative deamination at 50°C Aeropyrum pernix K1
1.4.1.4 8.3 8.7 deamination of L-glutamate. Determined at 50°C in 125 mM glycylglycine/NaOH buffer Aeropyrum pernix
1.4.1.4 8.3 8.7 deamination of L-glutamate, at 50°C in 125 mM glycylglycine/NaOH buffer Aeropyrum pernix

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.4.1.4 5 10 fully active Aeropyrum pernix K1

Cofactor

EC Number Cofactor Comment Organism Structure
1.4.1.4 NADP+
-
 Aeropyrum pernix K1
1.4.1.4 NADP+ the enzyme requires NADP+ as the coenzyme for the oxidation of L-glutamate, which can not be replaced by NAD+ Aeropyrum pernix
1.4.1.4 NADP+ no acrivity with NAD+ Aeropyrum pernix
1.4.1.4 NADPH
-
 Aeropyrum pernix K1
1.4.1.4 NADPH no activity with NADP+ Aeropyrum pernix
1.4.1.4 NADPH for the reduction of 2-oxoglutarate, NADPH is the coenzyme and NADH is inert Aeropyrum pernix