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Literature summary for 1.4.1.3 extracted from

  • Saito, H.; Yamamoto, I.; Ishimoto, M.
    Reversible inactivation of glutamate dehydrogenase in Bacteroides fragilis: purification and characterization of high activity- and low activity-enzymes (1988), J. Gen. Appl. Microbiol., 34, 377-385.
No PubMed abstract available
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KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.011
-
 NADPH reductive amination, low-activity form of the enzyme Bacteroides fragilis
0.013
-
 NADPH reductive amination, high-activity form of the enzyme Bacteroides fragilis
0.013
-
 NADP+ oxidative deamination, low-activity form of the enzyme Bacteroides fragilis
0.029
-
 NADP+ oxidative deamination, high-activity form of the enzyme Bacteroides fragilis
0.13
-
 NADH reductive amination, low-activity form of the enzyme Bacteroides fragilis
0.18
-
 2-oxoglutarate reductive amination, low-activity form of the enzyme Bacteroides fragilis
0.2
-
 2-oxoglutarate reductive amination, high-activity form of the enzyme Bacteroides fragilis
0.43
-
 NAD+ oxidative deamination, low-activity form of the enzyme Bacteroides fragilis
0.52
-
 NADH reductive amination, high-activity form of the enzyme Bacteroides fragilis
1.25
-
 NH3 reductive amination, high-activity form of the enzyme Bacteroides fragilis
1.31
-
 NH3 reductive amination, low-activity form of the enzyme Bacteroides fragilis
2.44
-
 NAD+ oxidative deamination, high-activity form of the enzyme Bacteroides fragilis
3.65
-
 L-glutamate oxidative deamination, low-activity form of the enzyme Bacteroides fragilis
3.83
-
 L-glutamate oxidative deamination, high-activity form of the enzyme Bacteroides fragilis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
49000
-
 6 * 49000, SDS-PAGE Bacteroides fragilis
290000
-
 hig- and low-activity form, gel filtration Bacteroides fragilis

Organism

Organism UniProt Comment Textmining
Bacteroides fragilis
-
 high activity-form and low-activity form
-

Purification (Commentary)

Purification (Comment) Organism
-
 Bacteroides fragilis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
5.9
-
 low-activity form of the enzyme, NADP+ dependent deamination Bacteroides fragilis
32.3
-
 high-activity form of the enzyme, NADP+-dependent deamination Bacteroides fragilis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-oxoglutarate + NH3 + NADH + H+
-
 Bacteroides fragilis L-glutamate + H2O + NAD+
-
 r
2-oxoglutarate + NH3 + NADH + H+ NH4Cl used in enzyme assay Bacteroides fragilis L-glutamate + H2O + NAD+
-
 r
L-glutamate + H2O + NAD(P)+
-
 Bacteroides fragilis 2-oxoglutarate + NH3 + NAD(P)H
-
 r
L-glutamate + H2O + NAD+
-
 Bacteroides fragilis 2-oxoglutarate + NH3 + NADH + H+
-
 r

Subunits

Subunits Comment Organism
hexamer 6 * 49000, SDS-PAGE Bacteroides fragilis