Abstract
The oxidation of ornithine in the presence of proline by crude extracts of Clostridium sticklandii cells was stimulated by nicotinamide adenine dinucleotide, coenzyme A, α-ketoglutarate, dimethylbenzimidazolyl cobamide (DBC) coenzyme, MgCl2, and adenosine diphosphate. Deletion of various cofactors resulted in the accumulation of a new dibasic amino acid which was identified as 2,4-diaminovaleric acid. Both the oxidation of ornithine to alanine and acetate and the conversion of ornithine to 2,4-diaminovaleric acid were stimulated by addition of DBC coenzyme, and both were inhibited by intrinsic factor, an inhibitor of cobamide coenzyme-dependent reactions. This inhibition was reversed by addition of DBC coenzyme. However, the oxidation of 2,4-diaminovaleric acid was insensitive to added intrinsic factor. The data indicate that 2,4-diaminovaleric acid represents the first intermediate in the oxidation of ornithine by C. sticklandii.
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