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1.
Biochem J ; 218(3): 811-8, 1984 Mar 15.
Artigo em Inglês | MEDLINE | ID: mdl-6426463

RESUMO

Dihydrolipoamide dehydrogenase has been discovered in the halophilic archaebacteria for the first time. The enzyme from both classical and alkaliphilic halobacteria has been investigated. (1) The enzyme specifically catalysed the stoichiometric oxidation of dihydrolipoamide by NAD+. Enzymic activity was optimal at 2 M-NaCl and was remarkably resistant to thermal denaturation. (2) The relative molecular masses (Mr) of the native enzyme from the various species of halobacteria were determined to be within the range 112000-120000. (3) The enzyme exhibited a hyperbolic dependence of catalytic activity on both dihydrolipoamide and NAD+ concentrations. From these steady-state kinetic measurements the dissociation constant (Ks) of dihydrolipoamide was determined to be 57 (+/- 5) microM. (4) The enzyme was only susceptible to inactivation by iodoacetic acid in the presence of its reducing ligands, dihydrolipoamide or NADH. The rate of inactivation followed a hyperbolic dependence on the concentration of dihydrolipoamide, from which the Ks of this substrate was calculated to be 55 (+/- 7) microM. Together with the steady-state kinetic data, the pattern of inactivations is consistent with the involvement in catalysis of a reversibly reducible disulphide bond, as has been found in dihydrolipoamide dehydrogenase from non-archaebacterial species. In eubacterial and eukaryotic organisms, dihydrolipoamide dehydrogenase functions in the 2-oxo acid dehydrogenase complexes. These multienzyme systems have not been detected in the archaebacteria, and, in the context of this apparent absence, the possible function and evolutionary significance of archaebacterial dihydrolipoamide dehydrogenase are discussed.


Assuntos
Archaea/enzimologia , Bactérias/enzimologia , Di-Hidrolipoamida Desidrogenase/metabolismo , Halobacterium/enzimologia , Cromatografia em Gel , Di-Hidrolipoamida Desidrogenase/antagonistas & inibidores , Iodoacetatos/farmacologia , Ácido Iodoacético , Cinética , Peso Molecular , Temperatura
2.
Proc Natl Acad Sci U S A ; 70(8): 2261-5, 1973 Aug.
Artigo em Inglês | MEDLINE | ID: mdl-16592103

RESUMO

We previously explored automimicry assuming that a species of prey was so unpalatable as to promote conditioned avoidance for a period of time after a predator encountered a single individual (Case 1). In this paper, we assume that the prey is less noxious and that two encounters are required. Case 2 allows the two encounters with unpalatables to be separated by any number of palatables, while in Case 3 the predator must encounter two unpalatables, consecutively.The general relationships in the three cases are similar, but the automimetic advantage is reduced moderately in Case 2 and greatly in Case 3. To attain the same automimetic advantage as in Case 1 requires an increase in the proportion of unpalatables, or in the induced rejection period, or both. Consequently, selection will tend to increase the unpalatability so that Cases 2 and 3 converge to Case 1.Species that are uniformly and highly unpalatable can afford to be more dispersed than automimetic species. Case-2 and -3 automimetic species will benefit greatly from gregariousness, while in Case-1 automimicry situations this is less important.

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