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BRENDA support

Literature summary for 1.4.1.3 extracted from

  • Nassar, O.M.; Wong, K.Y.; Lynch, G.C.; Smith, T.J.; Pettitt, B.M.
    Allosteric discrimination at the NADH/ADP regulatory site of glutamate dehydrogenase (2019), Protein Sci., 28, 2080-2088 .
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
ADP modeling of the NADH/ADP site for allosteric effects induced at a single site of binding inhibitor NADH versus activator ADP to GDH. ADP shows dissimilar binding conformations at each NADH/ADP site in the GDH trimer, while NADH shows similar inhibitory binding conformations at each NADH/ADP site Bos taurus

Inhibitors

Inhibitors Comment Organism Structure
NADH modeling of the NADH/ADP site for allosteric effects induced at a single site of binding inhibitor NADH versus activator ADP to GDH. ADP shows dissimilar binding conformations at each NADH/ADP site in the GDH trimer, while NADH shows similar inhibitory binding conformations at each NADH/ADP site Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus P00366
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