Lysine 2,3-aminomutase and the mechanism of the interconversion of lysine and beta-lysine.
Lysine 2,3-aminomutase and the mechanism of the interconversion of lysine and beta-lysine.
复制标题
赖氨酸2,3-氨基变位酶以及赖氨酸和β-赖氨酸相互转化的机制。
DOI：
10.1002/9780470123126.ch1
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发表时间：
1993
期刊：
影响因子：
--
通讯作者：
Reed,GH
中科院分区：
文献类型：
--
作者：
Frey,PA;Reed,GH
H. A. Barker 及其同事于 1966 年观察到梭菌中赖氨酸酶促转化为 P-赖氨酸 (1)。他们于 1970 年纯化并描述了赖氨酸 2, 3-氨基变位酶（催化反应 1 的酶），并表明重排随着底物中氢的保守而进行；也就是说，溶剂中的质子不会掺入赖氨酸或 P-赖氨酸的不可交换位置 (2)。 Barker 及其同事描述了赖氨酸 2, 3-氨基变位酶的分子特性，并报道该酶
H. A. Barker and co-workers observed the enzymatic conversion of lysine into P-lysine in Clostridia in 1966 (1). They purified and described lysine 2, 3-aminomutase, the enzyme that catalyzes reaction 1, in 1970 and showed that the rearrangement proceeds with conservation of hydrogen in the substrate; that is, no protons from the solvent are incorporated into nonexchangeable positions of lysine or P-lysine (2). Barker and co-workers described the molecular properties of lysine 2, 3-aminomutase and reported that the enzyme