Studies on the formation of [formula omitted] in cell-free extracts of Aerobacter aerogenes 62-1

Abstract

We have investigated conditions optimal for the conversion of l-lysine to its N 6- 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 N 2 - or N 6- derivatives of lysine, and α-amino acids were not hydroxylated. Most of the latter compounds had little effect on the hydroxylation of l-lysine. However, l-glutamic acid and l-glutamine enhanced the hydroxylation. With half-maximal activation achieved at 100 μM concentration of the effector. The K m values for pyruvate and l-(+)-lactate (compounds known to stimulate N- hydroxylysine formation ) were found to be approx. 100 μM. The data show that N-hydroxylation of the amino acid precedes acylation in the biosynthesis of hydroxamic acid in A. aerogenes 62-1.