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- W2509724639 abstract "Cell-free extracts of Clostridium tetanomorphum convert glutamate via /-methylpartate to mesaconate. The step from glutamate to 0-methylaspartate has an to require a coenzyme that has been isolated from C. tetanomorphum d identified as a derivative of pseudovitamin B12. This coenzyme, which we signate adenine-B12 coenzyme, contains two moles of adenine, one of which is ;ached to ribose as in pseudovitamin B12, whereas the other is probably attached a double bond in the corphyrin ring system in such a way as to greatly modify a spectrum. We now wish to report the isolation of two additional forms of the Bi2 coenzyme. Several bacteria, such as E. coli2 and Propionibacterium species,3 are known to 'm different cobalamins when grown in the presence of different heterocyclic ses. We have found that C. tetanomorphum possesses the ability to utilize nzimidazole and 5,6-dimethylbenzimidazole4 in a similar manner in the formation B12 coenzymes. By growing this bacterium in the presence of one of these mpounds, the formation of the adenine-B12 coenzyme is suppressed, and the rresponding benzimidazole coenzyme is produced in comparable amount. In is way we have prepared, and subsequently isolated by ion exchange methods, cromolar amounts of a benzimidazole-B12 coenzyme and a 5,6-dimethylnzimidazole-BI2 coenzyme. The spectrum of a highly purified sample of the benzimidazole-Bi2 coenzyme is npared with that of the adenine-Bi2 coenzyme in Figure 1. The spectrum of the i-dimethylbenzimidazole-B12 coenzyme is almost identical with that of the nzimidazole coenzyme and therefore is not shown separately. Both of these enzymes have absorption maxima at 261, 375, and 519 m,; the corresponding )lar extinction coefficients in neutral solution are 35.5, 9.90, and 7.55 X 106 L2/mole, respectively. The most conspicuous difference between the spectra of e benzimidazole- and adenine-B12 coenzymes is in the region above 400 m,u. Le adenine coenzyme has a broad peak with a maximum at 458 mA, and a relatively ght absorption above 500 m/n, and it is orange in color. The benzimidazole enzymes have a broad absorption peak with a maximum at about 519 mn and" @default.
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- W2509724639 date "1959-01-01" @default.
- W2509724639 modified "2023-09-27" @default.
- W2509724639 title "BENZIMIDAZOLE OR DIMETHYLBENZIMIDAZOLE" @default.
- W2509724639 hasPublicationYear "1959" @default.
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