Evolutionarily homologous alpha 2 beta 2 oligomeric structures in beta-ketoadipate succinyl-CoA transferases from Acinetobacter calcoaceticus and Pseudomonas putida.
1981; Elsevier BV; Volume: 256; Issue: 4 Linguagem: Inglês
10.1016/s0021-9258(19)69841-8
ISSN1083-351X
Autores Tópico(s)HIV/AIDS drug development and treatment
ResumoHomogeneous /?-ketoadipate succinyl-CoA transferase (EC 2.8.3.6)preparations were obtained from extracts of Acinetobacter calcoaceticus and pseudo^^ put& Gel filtration indicated that the respective transferases have similar molecular weights of 108,000 and 109,000; each transferase appears to have an a& oligomeric structure formed by association of nonidentical subunits with a molecular weight of about 25,000.The subunits were separated by sodium dodecyl sulfate-gel electrophoresis, and differences in their primary structures were revealed by determination of the NHz-terminal amino acid sequences of the oligomers.The transferases cross-react immunologically and possess similar amino acid compositions.These are remarkably similar to the amino acid compositions of y- carboxymuconolactone decarboxylases (EC 4.1.1.44)and fl-ketoadipate enol-lactone hydrolases (EC 3.1.1.24),enzymes that mediate consecutive reactions preceding the transferase step in the 8-ketoadipate pathway.
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