Dyer J K, Costilow R N
J Bacteriol. 1970 Jan;101(1):77-83. doi: 10.1128/jb.101.1.77-83.1970.
The oxidation of ornithine in the presence of proline by crude extracts of Clostridium sticklandii cells was stimulated by nicotinamide adenine dinucleotide, coenzyme A, alpha-ketoglutarate, dimethylbenzimidazolyl cobamide (DBC) coenzyme, MgCl(2), 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.
在丁酸梭菌细胞的粗提取物存在下，鸟氨酸在脯氨酸存在时的氧化反应受到烟酰胺腺嘌呤二核苷酸、辅酶A、α-酮戊二酸、二甲基苯并咪唑基钴胺素（DBC）辅酶、MgCl₂和二磷酸腺苷的刺激。去除各种辅因子会导致一种新的二碱基氨基酸积累，该氨基酸被鉴定为2,4-二氨基戊酸。添加DBC辅酶会刺激鸟氨酸氧化为丙氨酸和乙酸以及鸟氨酸转化为2,4-二氨基戊酸，而这两种反应均受到钴胺素辅酶依赖性反应抑制剂内因子的抑制。添加DBC辅酶可逆转这种抑制作用。然而，2,4-二氨基戊酸的氧化对添加的内因子不敏感。数据表明，2,4-二氨基戊酸是丁酸梭菌氧化鸟氨酸过程中的首个中间产物。
