Parniak M A, Jackson G E, Murray G J, Viswanatha T
Biochim Biophys Acta. 1979 Jul 11;569(1):99-108. doi: 10.1016/0005-2744(79)90085-8.
We have investigated conditions optimal for the conversion of L-lysine to its N6-hydroxy derivative by partially purified cell-free extracts of Aerobacter aerogenes 62-1. The enzyme system was highly specific to L-lysine: the D-isomer and, the N2- or N6-derivatives of lysine, and alpha-amino acids were not hydroxylated. Most of the latter compounds had little effect onthe hydroxylation of L-lysine. However, -l-glutamic acid and L-glutamine enhanced the hydroxylation, with half-maximal activation achieved at 100 micrometers concentration of the effector. The Km values for pyruvate and L-(+)-lactate (compounds known to stimulate N-hydroxylysine formation) were found to be approx. 100 micrometers. The data show that N-hydroxylation of the amino acid precedes acylation in the biosynthesis of hydroxamic acid in A. aerogenes 62-1.
我们已经研究了产气气杆菌62 - 1部分纯化的无细胞提取物将L - 赖氨酸转化为其N6 - 羟基衍生物的最佳条件。该酶系统对L - 赖氨酸具有高度特异性：赖氨酸的D - 异构体、N2 - 或N6 - 衍生物以及α - 氨基酸均不会被羟基化。大多数后一类化合物对L - 赖氨酸的羟基化作用很小。然而，L - 谷氨酸和L - 谷氨酰胺可增强羟基化作用，效应物浓度为100微摩尔时达到最大激活的一半。发现丙酮酸和L -（+） - 乳酸（已知可刺激N - 羟基赖氨酸形成的化合物）的Km值约为100微摩尔。数据表明，在产气气杆菌62 - 1中，氨基酸的N - 羟基化在异羟肟酸生物合成中先于酰化反应。
