Effect of metabolites on ε-N-hydroxylysine formation in cell-free extracts of Aerobacter aerogenes 62-1

Abstract
The conversion of L-lysine to its corresponding .epsilon.-N-hydroxy derivative was achieved for the 1st time by cell-free extracts of A. aerogenes 62-1. Partial fractionation by differential centrifugation (at 12,000 .times. g) revealed that both supernatant and pellet are essential for maximum enzymatic activity. The .omega.-N-hydroxylase functioned optimally at pH 7-7.5 and exhibited an apparent Km of about 75 .mu.M 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.