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Literature summary extracted from

  • Treberg, J.R.; Brosnan, M.E.; Brosnan, J.T.
    The simultaneous determination of NAD(H) and NADP(H) utilization by glutamate dehydrogenase (2010), Mol. Cell. Biochem., 344, 253-259.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.4.1.3 ADP allosteric activator, addition of ADP or leucine to the single cofactor assay results in a marked activation of NADPH oxidation, about 1100% activation by ADP. Relative activation by ADP of GDH-catalyzed NAD+reduction is 36%, compared with 198% for NADP+ reduction Bos taurus
1.4.1.3 L-leucine allosteric activator, addition of ADP or leucine to the single cofactor assay results in a marked activation of NADPH oxidation, about 725% activation by L-leucine, respectively. Activation of NAD+ and NADP+ reduction by 40% and 135%, respectively Bos taurus

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.4.1.3 GTP
-
 Bos taurus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.4.1.3 mitochondrion
-
 Bos taurus 5739
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.4.1.3 L-glutamate + H2O + NAD+ Bos taurus
-
 2-oxoglutarate + NH3 + NADH + H+
-
 r
1.4.1.3 L-glutamate + H2O + NADP+ Bos taurus
-
 2-oxoglutarate + NH3 + NADPH + H+
-
 r
1.4.1.3 additional information Bos taurus the similarity in relative activation when both cofactors are present, combined with consistently greater GDH product formation from equimolar NADH than with NADPH, does not support the idea that there is a preferential utilization of NADPH by bovine GDH ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.4.1.3 Bos taurus
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.4.1.3 liver
-
 Bos taurus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.4.1.3 L-glutamate + H2O + NAD+
-
 Bos taurus 2-oxoglutarate + NH3 + NADH + H+
-
 r
1.4.1.3 L-glutamate + H2O + NADP+
-
 Bos taurus 2-oxoglutarate + NH3 + NADPH + H+
-
 r
1.4.1.3 additional information the similarity in relative activation when both cofactors are present, combined with consistently greater GDH product formation from equimolar NADH than with NADPH, does not support the idea that there is a preferential utilization of NADPH by bovine GDH Bos taurus ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.4.1.3 GDH
-
 Bos taurus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.4.1.3 37
-
 assay at Bos taurus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.4.1.3 8
-
 assay at Bos taurus

Cofactor

EC Number Cofactor Comment Organism Structure
1.4.1.3 additional information the similarity in relative activation when both cofactors are present, combined with consistently greater GDH product formation from equimolar NADH than with NADPH, does not support the idea that there is a preferential utilization of NADPH by bovine GDH. In the reductive amination direction, the rates of product formation are always greater for NADH oxidation than NADPH oxidation Bos taurus
1.4.1.3 NAD+
-
 Bos taurus
1.4.1.3 NADH
-
 Bos taurus
1.4.1.3 NADP+
-
 Bos taurus
1.4.1.3 NADPH
-
 Bos taurus

General Information

EC Number General Information Comment Organism
1.4.1.3 physiological function allosteric activation and inhibition is important for enzyme regulation, overview Bos taurus