In vivo deacetylation of N-acetyl amino acids by kidney acylases in mice and rats. A possible role of acylase system in mammalian kidneys.
Deacetylations of N-acetylhistidine and N-acetyltryptophan were examined in vivo by their administration to mice and rats. N-Acetylhistidine accumulated preferentially in the kidney and was converted to histidine effectively by acylase I. Similar deacetylation of N-acetyltryptophan by acylase III was also observed. Acylase I and III activities in mouse kidney increased in parallel remarkably at the period of weaning. A hypothesis that the acylase system in mammalian kidneys is a mechanism acquired to utilize amino acids from exogenous and endogenous acyl derivatives including those derived from protein hydrolysis was offered.
D000375:Aging; D000581:Amidohydrolases / Q000378:metabolism*; D000818:Animals; D006639:Histidine / Q000031:analogs & derivatives; D007668:Kidney / Q000201:enzymology* / Q000254:growth & development; D007700:Kinetics; D008099:Liver / Q000201:enzymology / Q000254:growth & development; D051379:Mice; D051381:Rats; D014018:Tissue Distribution; D014364:Tryptophan / Q000031:analogs & derivatives
C006392:N-acetyltryptophan; D006639:Histidine; D014364:Tryptophan; D000581:Amidohydrolases; C023495:N-acetylhistidine