Ethanolamine ammonia-lyase (EC 4.3.1.7) catalyzes the adenosylcobalamin-dependent deamination of ethanolamine and 2-aminopropanol. Incubation of the enzyme.cofactor complex with 2-aminoacetaldehyde leads to rapid cleavage of the carbon--cobalt bond accompanied by the destruction of the corrinoid portion of the cofactor. During this reaction the adenosyl portion of the cofactor is oxidized to 4',5'-anhydroadenosine, and the aminoacetaldehyde is converted to acetic acid, which remains associated with the enzyme as a noncovalent complex which survives gel filtration. There is no evidence for the alkylation of the corrin metal by the substrate analog. The enzyme.AdoCbl complex is thus able to eliminate an amino group from a substrate analog without the formation of a new alkyl cobalamin in which the analog is a ligand. These observations do not support the participation of what might be termed "substratylcobalamin" as an intermediate in the ammonia migration occurring in reactions catalyzed by ethanolamine ammonia-lyase.

中文翻译：

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乙醇胺氨裂解酶（一种腺苷钴胺素依赖性酶）的作用机理。酶辅因子复合物与2-氨基乙醛的反应。

乙醇胺氨裂解酶（EC 4.3.1.7）催化乙醇胺和2-氨基丙醇的腺苷钴胺素依赖性脱氨反应。酶辅因子复合物与2-氨基乙醛的孵育导致碳-钴键的快速断裂，同时辅因子的类rinrinoid部分被破坏。在该反应过程中，辅助因子的腺苷部分被氧化为4'，5'-脱水腺苷，氨基乙醛被转化为乙酸，该乙酸作为非共价复合物与酶结合，可在凝胶过滤中幸存。没有证据表明底物类似物使柯林金属烷基化。因此，酶.AdoCbl复合物能够从底物类似物中消除氨基，而不会形成新的烷基钴胺素，其中类似物是配体。