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Literature summary for 1.4.1.4 extracted from

  • Geng, F.; Ma, C.W.; Zeng, A.P.
    Reengineering substrate specificity of E. coli glutamate dehydrogenase using a position-based prediction method (2017), Biotechnol. Lett., 39, 599-605 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
-
Escherichia coli

Protein Variants

Protein Variants Comment Organism
K92C altering substrate specificity from glutamate to homoserine for a de novo 1,3-propanediol biosynthetic pathway, 5.5fold increase in speific activity with homoserine Escherichia coli
K92M altering substrate specificity from glutamate to homoserine for a de novo 1,3-propanediol biosynthetic pathway, 2.8fold increase in speific activity with homoserine Escherichia coli
K92V altering substrate specificity from glutamate to homoserine for a de novo 1,3-propanediol biosynthetic pathway, 7.2fold increase in speific activity with homoserine Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli Q8XDW9
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-glutamate + H2O + NADP+
-
Escherichia coli 2-oxoglutarate + NH3 + NADPH + H+
-
?
L-homoserine + H2O + NAD+
-
Escherichia coli 4-hydroxy-2-oxobutanoate + NH3 + NADH
-
?