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Literature summary for 1.4.1.2 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
Search for more literature for 1.4.1.2

Activating Compound

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

Crystallization (Commentary)

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

Protein Variants

Protein Variants Comment Organism
D165H site-directed mutagenesis, catalytically inactive mutant [Clostridium] symbiosum
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
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
W243F site-directed mutagenesis, catalytically impaired enzyme due to hindered glutamate binding, the mutant shows Michaelis-Menten kinetics [Clostridium] symbiosum
W310F site-directed mutagenesis, the mutant shows Michaelis-Menten kinetics [Clostridium] symbiosum
W393F site-directed mutagenesis [Clostridium] symbiosum
W449F site-directed mutagenesis, the mutation does not affect the allosteric behaviour of the enzyme [Clostridium] symbiosum
W64F site-directed mutagenesis, the mutation does not affect the allosteric behaviour of the enzyme [Clostridium] symbiosum

Inhibitors

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

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information cofactor kinetics, overview Homo sapiens
additional information
-
 additional information cofactor kinetics, overview Bos taurus
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)

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

Organism

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

Substrates and Products (Substrate)

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

Synonyms

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

Cofactor

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

General Information

General Information Comment Organism
evolution the enzyme belongs to the family of amino acid dehydrogenases Homo sapiens
evolution the enzyme belongs to the family of amino acid dehydrogenases Bos taurus
evolution the enzyme belongs to the family of amino acid dehydrogenases [Clostridium] symbiosum
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
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
additional information Trp243 is located in the active-site cleft. Neither Trp64 nor Trp449 are strictly required for pH-dependent inactivation [Clostridium] symbiosum
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
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
physiological function CsGDH lacks the regulation by ADP and GTP seen in bovine GDH [Clostridium] symbiosum