Abstract
The coenzyme-non-specific glutamate dehydrogenase (EC 1.4.1.3) from Scenedesmus acutus in inhibited by p-hydroxymercuribenzoate only in the deamination reaction. From this result and from its stability in the presence of urea it is concluded that this enzyme exhibits and equilibrium between three conformations: aminating and deaminating conformations induced by NADH-2-oxoglutarate and NAD+-glutamate, respectively, and the “native” conformation in the absence of substrates.
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Abbreviations
- PHMB:
-
p-hydroxymercuribenzoate
- Tris:
-
2-amino-2-(hydroxymethyl)-1,3-propanediol
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This work has been described in a preliminary report [Shatilov, V., Sund, H. (1980) Hoppe Seylers Z. Physiol. Chem. 361, 1345]. For the previous paper in this series see: Dieter et al. (1981)
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Shatilov, V.R., Sund, H. Glutamate dehydrogenase of the unicellular green alga Scenedesmus acutus . Planta 157, 367–370 (1983). https://doi.org/10.1007/BF00397409
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DOI: https://doi.org/10.1007/BF00397409