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Hydroxylysine Metabolism in Rats, Mice, and Chickens^1,2,

Department of Biochemistry, College of Biological Sciences, University of Minnesota, St. Paul, Minnesota 55101

Rats deficient in vitamin B₆ exhibited a decreased ability to metabolize 5-hydroxy-L-lysine-6-¹⁴C to ¹⁴CO₂ as compared to normal animals. Under vitamin B₆-deficient conditions, phosphohydroxylysine accumulated in the kidneys and liver. Administration of pyridoxine to the deficient rats prior to the hydroxy-L-lysine reduced the phosphate ester concentration to normal levels. These experiments confirm the in vivo involvement of hydroxylysine kinase and O-phosphohydroxylysine phospho-lyase in the degradation of hydroxylysine. Using the four individual isomers of hydroxylysine-6-¹⁴C, the general patterns of hydroxylysine degradation in the rat, the mouse and the chicken were compared. All three species degraded the L-isomers to CO₂ via glutarate. Allohydroxy-D-lysine, which is metabolized to the terminal product, hydroxypipecolate, in the rat, was not metabolized by the mouse, but was degraded to CO₂ by the chicken. In all three species, hydroxy-D-lysine formed little CO₂ or compounds found in the urine.

KEY WORDS: • vitamin B₆ • hydroxy-L-lysine • hydroxy-D-lysine • O-phosphohydroxylysine

¹ Supported in part by National Institutes of Health Grant AM 07984.

² A preliminary report of a portion of these results has been presented: Federation Proc. 30: 463 (1971, abstr.).

³ Present address: Miami Valley Laboratories, Procter and Gamble Co., Cincinnati, Ohio.

⁴ To whom reprint requests should be sent.

Manuscript received 8 September 1971.