Murray G J, Clark G E, Parniak M A, Viswanatha T
Can J Biochem. 1977 Jun;55(6):625-9. doi: 10.1139/o77-090.
The conversion of L-lysine to its corresponding epsilon-N-hydroxy derivative has been achieved for the first time by cell-free extracts of Aerobacter aerogenes 62-1. Partial fractionation by differential centrifugation (at 12 000 X g) revealed that both supernatant and pellet are essential for maximum enzymatic activity. The omega-N-hydroxylase (EC 1.14.99) was found to function optimally at pH 7-7.5 and exhibited an apparent Km of about 75 muM for L-lysine. L(+)-Lactate or DL-lactate and pyruvate greatly stimulate the omega-N-hydroxylase activity. The system is strongly inhibited by arsenite and sulfite.
产气气杆菌62 - 1的无细胞提取物首次实现了将L - 赖氨酸转化为其相应的ε - N - 羟基衍生物。通过差速离心（12000×g）进行部分分级分离表明，上清液和沉淀对于最大酶活性都是必不可少的。发现ω - N - 羟化酶（EC 1.14.99）在pH 7 - 7.5时功能最佳，对L - 赖氨酸的表观Km约为75μM。L（+） - 乳酸或DL - 乳酸以及丙酮酸极大地刺激了ω - N - 羟化酶的活性。该系统受到亚砷酸盐和亚硫酸盐的强烈抑制。
