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

BRENDA support

Literature summary extracted from

  • Yamamoto, I.; Abe, A.; Ishimoto, M.
    Properties of glutamate dehydrogenase purified from Bacteroides fragilis (1987), J. Biochem., 101, 1391-1397.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.4.1.3 2-oxoglutarate
-
Bacteroides fragilis
1.4.1.3 D-glutamate 10 mM, 57% inhibition of NADP+-linked activity, 30% inhibition of NADPH-linked activity Bacteroides fragilis
1.4.1.3 glutamate
-
Bacteroides fragilis
1.4.1.3 NaCl 100 mM, 50% inhibition of NADH and NAD+ dependent reactions Bacteroides fragilis
1.4.1.3 oxaloacetate 5 mM, 20-25% inhibition of NADH- and NAD+-dependent activities Bacteroides fragilis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.4.1.3 0.013
-
NADPH NADP-linked reductive amination Bacteroides fragilis
1.4.1.3 0.019
-
NADP+ NADP-linked oxidative deamination Bacteroides fragilis
1.4.1.3 0.14
-
2-oxoglutarate NADP-linked reductive amination Bacteroides fragilis
1.4.1.3 0.2
-
NADH NAD-linked reductive amination Bacteroides fragilis
1.4.1.3 1.7
-
NH3 NADP-linked reductive amination Bacteroides fragilis
1.4.1.3 2.4
-
L-glutamate NADP-linked oxidative deamination Bacteroides fragilis
1.4.1.3 3
-
NAD+ NAD-linked oxidative deamination Bacteroides fragilis
1.4.1.3 4.9
-
NH3 NAD-linked reductive amination Bacteroides fragilis
1.4.1.3 5.1
-
NH3 NADP-linked reductive amination Bacteroides fragilis
1.4.1.3 7.1
-
2-oxoglutarate NAD-linked reductive amination Bacteroides fragilis
1.4.1.3 7.3
-
L-glutamate NAD-linked oxidative deamination Bacteroides fragilis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.4.1.3 300000 350000 polyacrylamide disc gel electrophoresis Bacteroides fragilis

Organism

EC Number Organism UniProt Comment Textmining
1.4.1.3 Bacteroides fragilis
-
strictly anaerobic bacterium
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.4.1.3
-
Bacteroides fragilis

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.4.1.3 18.4
-
-
Bacteroides fragilis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.4.1.3 2-aminobutyrate + H2O + NADP+ 3% of activity with L-glutamate Bacteroides fragilis 2-oxobutyrate + NH3 + NADPH
-
?
1.4.1.3 2-oxoglutarate + NH3 + NADH + H+
-
Bacteroides fragilis L-glutamate + H2O + NAD+
-
r
1.4.1.3 2-oxoglutarate + NH3 + NADH + H+ NH4Cl used in enzyme assay Bacteroides fragilis L-glutamate + H2O + NAD+
-
r
1.4.1.3 L-glutamate + H2O + NAD(P)+
-
Bacteroides fragilis 2-oxoglutarate + NH3 + NAD(P)H
-
r
1.4.1.3 L-glutamate + H2O + NAD+
-
Bacteroides fragilis 2-oxoglutarate + NH3 + NADH + H+
-
r
1.4.1.3 valine + H2O + NADP+ 3% of activity with L-glutamate Bacteroides fragilis 2-oxovalerate + NH3 + NADPH
-
?

Subunits

EC Number Subunits Comment Organism
1.4.1.3 hexamer SDS-PAGE Bacteroides fragilis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.4.1.3 7.4
-
NADH + 2-oxoglutarate + NH3 Bacteroides fragilis
1.4.1.3 8
-
NADPH + 2-oxoglutarate + NH3 Bacteroides fragilis
1.4.1.3 9
-
NADH + NH3 + 2-oxoglutarate Bacteroides fragilis
1.4.1.3 9.5
-
glutamate + NADP+ Bacteroides fragilis

Cofactor

EC Number Cofactor Comment Organism Structure
1.4.1.3 NADPH amination activity is 5fold higher with NADPH than that with NADH Bacteroides fragilis

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.4.1.3 70
-
NaCl
-
Bacteroides fragilis
1.4.1.3 80
-
L-glutamate reductive amination with NADPH, not with NADH is inhibited Bacteroides fragilis