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 ε-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 × g) revealed that both supernatant and pellet are essential for maximum enzymatic activity. The ω-N-hydroxylase (EC 1.14.99) was found to function optimally at pH 7–7.5 and exhibited an apparent Km of about 75 μM for L-lysine. L(+)-Lactate or DL-lactate and pyruvate greatly stimulate the ω-N-hydroxylase activity. The system is strongly inhibited by arsenite and sulfite.