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1.4.1.2: glutamate dehydrogenase

This is an abbreviated version!
For detailed information about glutamate dehydrogenase, go to the full flat file.

Word Map on EC 1.4.1.2

Reaction

L-glutamate
+
H2O
+
NAD+
=
2-oxoglutarate
+
NH3
+
NADH
+
H+

Synonyms

At5g18170, AtGDH1, BpNADGDH, c, CCNA_00086, CsGDH, dehydrogenase, glutamate, GDH, GDH isoenzyme 1, GDH, NAD-dependent, gdh-1, gdh-2, GDH1, GDH2, Gdh2p, GDH3, GdhA, GDHB, GDHI, GdhZ, Glu dehydrogenase, GluD, GLUD1, GLUD2, GluDH, glutamate dehydrogenase, glutamate dehydrogenase (NAD), glutamate dehydrogenase 2, glutamate dehydrogenase alpha subunit, glutamate dehydrogenase beta subunit, glutamate dehydrogenase isoform 1, glutamate oxidoreductase, glutamic acid dehydrogenase, glutamic dehydrogenase, hGDH1, hGDH2-nerve-specific GDH, house-keeping GDH, L-glutamate dehydrogenase, L-glutamic acid dehydrogenase, More, NAD(+)-dependent glutamate dehydrogenase, NAD(H)-dependent glutamate dehydrogenase, NAD+-dependant glutamate dehydrogenase, NAD+-dependent GDH, NAD+-dependent GDHX, NAD+-dependent GluDH, NAD+-dependent glutamate dehydrogenase, NAD+-GDH, NAD+-glutamate dehydrogenase, NAD+-specific GDH, NAD+-specific glutamate dehydrogenase, NAD-dependent GDH, NAD-dependent glutamate dehydrogenase, NAD-dependent glutamic dehydrogenase, NAD-dependent L-glutamate dehydrogenase, NAD-GDH, NAD-glutamate dehydrogenase, NAD-linked glutamate dehydrogenase, NAD-linked glutamic dehydrogenase, NAD-specific glutamate dehydrogenase, NAD-specific glutamic dehydrogenase, NAD-ylGdh2p, NAD:glutamate oxidoreductase, NADH-dependent GDH, NADH-dependent glutamate dehydrogenase, NADH-GDH, NADH-glutamate dehydrogenase, NADH-linked glutamate dehydrogenase, OsGDH1, OsGDH2, OsGDH3, Pcal_1031, RocG, sco2999, Surface-associated protein PGAG1, t-GDH, type I GDH, YALI0E09603g, ylGDH2

ECTree

     1 Oxidoreductases
         1.4 Acting on the CH-NH2 group of donors
             1.4.1 With NAD+ or NADP+ as acceptor
                1.4.1.2 glutamate dehydrogenase

General Stability

General Stability on EC 1.4.1.2 - glutamate dehydrogenase

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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
2-oxoglutarate stabilizes
-
ADP stabilizes
-
ammonium sulfate improves stability
-
DTT stabilizes
-
extremely unstable at 0°C to 4°C due to the dissociation of the holoenzyme into catalytically inactive subunits
-
guanidine hydrochloride, 1.0 M, complete denaturation
-
high salt tolerance
-
isophthalate stabilizes
-
NaCl, 0.1 M, stabilizes
-
NADH stabilizes
-
potassium phosphate buffer, high concentration, stabilizes
-
presence of sulfhydryl groups in the environment stabilizes
-
repeated freezing and thawing: loss of activity
-
strong dependence on high salt concentrations for stability
-
the enzyme resists proteolysis by trypsin, chymotrypsin or endoproteinase Glu-C at 25°C. Above 30°C the enzyme became cleavable by chymotrypsin, at a single site. Proteolysis is accompanied by the loss of enzyme activity. Proteolysis is prevented by either of the substrates 2-oxoglutarate or L-glutamate but not by the coenzymes NAD+ or NADH
the enzyme resists proteolysis by trypsin, chymotrypsin or endoproteinase Glu-C at 25°C. Above 30°C the enzyme becomes cleavable by chymotrypsin, at a single site. Proteolysis is accompanied by the loss of enzyme activity. Proteolysis is prevented by either of the substrates 2-oxoglutarate or L-glutamate but not by the coenzymes NAD+ or NADH