N-acetylamino acid utilization by kidney aminoacylase-1

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DOIResolve DOI: http://doi.org/10.1016/j.biochi.2007.12.006
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TypeArticle
Journal titleBiochimie
Volume90
Issue5
Pages773780; # of pages: 8
SubjectAmino acid salvage; Aminoacylase-1; genome; kidney tubular epithelium; N-acetylamino acids; pha; Substrate specifity
AbstractMammalian aminoacylase-1 (Acy1) participates in the breakdown of N-acetylated amino acids during intracellular protein catabolism. Acy1is most abundantly expressed in the kidney tubular epithelium. Lately, Acy1 deficiency was identified in children with increased urinary excretionof several N-acetylamino acids. Here we report detailed N-acetylamino acid specificity profiles for human and porcine Acy1 based on steadystate kinetic measurements. We found that LLC-PK1 cells, a model of the porcine kidney proximal tubular epithelium, robustly express Acy1.For the first time, we demonstrate uptake and utilization of N-acteylleucine and -methionine in replacement of the free amino acid, respectively,in cultured epithelial cells. Our data are consistent with a specific role of kidney Acy1 in the salvage of amino acids originating from systemicdegradation of N-acetylated proteins.
Publication date
LanguageEnglish
AffiliationNRC Biotechnology Research Institute; National Research Council Canada
Peer reviewedNo
NRC number49556
NPARC number3539777
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Record identifierf4470cd1-9694-47bd-a16b-3efefee5b97d
Record created2009-03-01
Record modified2016-05-09
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