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Literature summary extracted from

  • Engel, P.C.
    Making biochemistry count: life among the amino acid dehydrogenases (2011), Biochem. Soc. Trans., 39, 425-429.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.4.1.2 ADP
-
 Homo sapiens
1.4.1.2 ADP
-
 Bos taurus
1.4.1.2 additional information no activation by ADP [Clostridium] symbiosum

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.4.1.2 crystal structure determination and analysis [Clostridium] symbiosum

Protein Variants

EC Number Protein Variants Comment Organism
1.4.1.2 D165H site-directed mutagenesis, catalytically inactive mutant [Clostridium] symbiosum
1.4.1.2 additional information site-directed mutagenesis to alter substrate specificity in phenylalanine dehydrogenase and varying strengths of binding of the wrong enantiomer in engineered mutant enzyme and implications for resolution of racemates, overview Homo sapiens
1.4.1.2 additional information site-directed mutagenesis to alter substrate specificity in phenylalanine dehydrogenase and varying strengths of binding of the wrong enantiomer in engineered mutant enzyme and implications for resolution of racemates, overview Bos taurus
1.4.1.2 W243F site-directed mutagenesis, catalytically impaired enzyme due to hindered glutamate binding, the mutant shows Michaelis-Menten kinetics [Clostridium] symbiosum
1.4.1.2 W310F site-directed mutagenesis, the mutant shows Michaelis-Menten kinetics [Clostridium] symbiosum
1.4.1.2 W393F site-directed mutagenesis [Clostridium] symbiosum
1.4.1.2 W449F site-directed mutagenesis, the mutation does not affect the allosteric behaviour of the enzyme [Clostridium] symbiosum
1.4.1.2 W64F site-directed mutagenesis, the mutation does not affect the allosteric behaviour of the enzyme [Clostridium] symbiosum

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.4.1.2 GTP
-
 Bos taurus
1.4.1.2 GTP
-
 Homo sapiens
1.4.1.2 additional information no inhibition by GTP [Clostridium] symbiosum

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.4.1.2 additional information
-
 additional information cofactor kinetics, overview Homo sapiens
1.4.1.2 additional information
-
 additional information cofactor kinetics, overview Bos taurus
1.4.1.2 additional information
-
 additional information cofactor kinetics, overview. Even without the heterotropic antenna responsible for allosteric regulation in mammalian enzymes, the GDH is emphatically still allosteric. The Eadie-Hofstee plot for NAD+ is strongly non-linear.Att pH 9.0 there is almost total positive co-operativity with glutamate, with a Hill coefficient close to the theoretical maximum of 6 for a hexamer [Clostridium] symbiosum

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.4.1.2 L-glutamate + H2O + NAD+ Homo sapiens
-
 2-oxoglutarate + NH3 + NADH + H+
-
 r
1.4.1.2 L-glutamate + H2O + NAD+ Bos taurus
-
 2-oxoglutarate + NH3 + NADH + H+
-
 r
1.4.1.2 L-glutamate + H2O + NAD+ [Clostridium] symbiosum
-
 2-oxoglutarate + NH3 + NADH + H+
-
 r

Organism

EC Number Organism UniProt Comment Textmining
1.4.1.2 Bos taurus
-
-
-
1.4.1.2 Homo sapiens
-
-
-
1.4.1.2 [Clostridium] symbiosum
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.4.1.2 L-glutamate + H2O + NAD+
-
 Homo sapiens 2-oxoglutarate + NH3 + NADH + H+
-
 r
1.4.1.2 L-glutamate + H2O + NAD+
-
 Bos taurus 2-oxoglutarate + NH3 + NADH + H+
-
 r
1.4.1.2 L-glutamate + H2O + NAD+
-
 [Clostridium] symbiosum 2-oxoglutarate + NH3 + NADH + H+
-
 r

Synonyms

EC Number Synonyms Comment Organism
1.4.1.2 GDH
-
 Homo sapiens
1.4.1.2 GDH
-
 Bos taurus
1.4.1.2 GDH
-
 [Clostridium] symbiosum

Cofactor

EC Number Cofactor Comment Organism Structure
1.4.1.2 NAD+
-
 Homo sapiens
1.4.1.2 NAD+
-
 Bos taurus
1.4.1.2 NAD+
-
 [Clostridium] symbiosum
1.4.1.2 NADH
-
 Homo sapiens
1.4.1.2 NADH
-
 Bos taurus
1.4.1.2 NADH
-
 [Clostridium] symbiosum

General Information

EC Number General Information Comment Organism
1.4.1.2 evolution the enzyme belongs to the family of amino acid dehydrogenases Homo sapiens
1.4.1.2 evolution the enzyme belongs to the family of amino acid dehydrogenases Bos taurus
1.4.1.2 evolution the enzyme belongs to the family of amino acid dehydrogenases [Clostridium] symbiosum
1.4.1.2 metabolism together with glutamine synthetase, the glutamate synthase, i.e. enzyme GOGAT, EC 1.4.1.14, offers the same net reaction as GDH, but with a much lower Km for ammonia, and driven by the splitting of ATP Homo sapiens
1.4.1.2 metabolism together with glutamine synthetase, the glutamate synthase, i.e. enzyme GOGAT, EC 1.4.1.14, offers the same net reaction as GDH, but with a much lower Km for ammonia, and driven by the splitting of ATP Bos taurus
1.4.1.2 additional information Trp243 is located in the active-site cleft. Neither Trp64 nor Trp449 are strictly required for pH-dependent inactivation [Clostridium] symbiosum
1.4.1.2 physiological function complex regulatory behaviour in mammalian GDH, involving negative co-operativity in coenzyme binding. Main heterotropic regulators are ADP and GTP, and ADP is a fragment of the coenzyme. NAD(H) mediates homotropic interaction via heterotropic sites or conversely, ADP uses homotropic coenzyme sites Homo sapiens
1.4.1.2 physiological function complex regulatory behaviour in mammalian GDH, involving negative co-operativity in coenzyme binding. Main heterotropic regulators are ADP and GTP, and ADP is a fragment of the coenzyme. NAD(H) mediates homotropic interaction via heterotropic sites or conversely, ADP uses homotropic coenzyme sites Bos taurus
1.4.1.2 physiological function CsGDH lacks the regulation by ADP and GTP seen in bovine GDH [Clostridium] symbiosum