Studies on the formation of N6-hydroxylysine in cell-free extracts of Aerobacter aerogenes 62-1.
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.
D000963:Antimetabolites / Q000494:pharmacology; D002474:Cell-Free System; D004754:Enterobacter / Q000201:enzymology*; D004755:Enterobacteriaceae / Q000201:enzymology*; D004789:Enzyme Activation; D005971:Glutamates / Q000494:pharmacology; D005973:Glutamine / Q000494:pharmacology; D006900:Hydroxylation; D006901:Hydroxylysine / Q000096:biosynthesis*; D007651:Keto Acids / Q000494:pharmacology; D007700:Kinetics; D007773:Lactates / Q000502:physiology; D008239:Lysine / Q000502:physiology; D009994:Osmolar Concentration; D011773:Pyruvates / Q000502:physiology; D013379:Substrate Specificity; D013696:Temperature; D013997:Time Factors
D000963:Antimetabolites; D005971:Glutamates; D007651:Keto Acids; D007773:Lactates; D011773:Pyruvates; D005973:Glutamine; D006901:Hydroxylysine; D008239:Lysine