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Transport of lysine and hydroxylysine in Streptococcus faecalis.

Data are presented which support the view that l-lysine is transported by two systems in Streptococcus faecalis. The system with the higher affinity for l-lysine appears to be specific for l-lysine among the common amino acids and to require an energy source. The second system transports both l-lysine and l-arginine and does not appear to require an energy source. Both of these systems will accept hydroxy-l-lysine as a substrate as shown by the energy requirement for hydroxy-l-lysine transport and by the inhibition of uptake by l-arginine as well as by l-lysine. The affinity of both systems appears to be considerably lower for hydroxy-l-lysine than for l-lysine. A mutant of S. faecalis which is resistant to the growth inhibitory action of hydroxy-l-lysine appears to differ from the parent strain by having a defective l-lysine-specific transport system. In this mutant, hydroxy-l-lysine is not readily transported via the l-lysine-specific system because of the mutation or via the second system because of the high concentration of l-arginine present in the growth medium. This overall lack of transport prevents hydroxy-l-lysine from reaching inhibitory levels within the cell.

Arginine↗

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

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.

Arsenic↗