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Literature summary for 1.4.1.2 extracted from

  • Aghajanian, S.; Hovsepyan, M.; Geoghegan, K.F.; Chrunyk, B.A.; Engel, P.C.
    A thermally sensitive loop in clostridial glutamate dehydrogenase detected by limited proteolysis (2003), J. Biol. Chem., 278, 1067-1074.
    View publication on PubMed
Search for more literature for 1.4.1.2

General Stability

General Stability Organism
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 [Clostridium] symbiosum
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 [Clostridium] symbiosum

Organism

Organism UniProt Comment Textmining
[Clostridium] symbiosum P24295
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-glutamate + H2O + NAD+
-
 [Clostridium] symbiosum 2-oxoglutarate + NH3 + NADH + H+
-
 ?

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 [Clostridium] symbiosum
NADH
-
 [Clostridium] symbiosum