TAILIEUCHUNG - Báo cáo khoa học: Purification and sequence identification of anserinase

Anserinase (Xaa-methyl-His dipeptidase, EC ) is a dipeptidase that mainly catalyzes the hydrolysis ofNa-acetylhistidine in the brain, retina and vitreous body of all poikilothermic vertebrates. The gene encoding anserinase has not been previously identified. We report the molecular identification of anserinase, purified from brain of Nile tilapia Oreochromis niloticus. | ềFEBS Journal Purification and sequence identification of anserinase Shoji Yamada Yoshito Tanaka and Seiichi Ando Faculty of Fisheries Kagoshima University Japan Keywords acetylhistidine anserinase carnosinase cytosolic nonspecific dipeptidase MEROPS M20A metallopeptidase Correspondence S. Yamada Faculty of Fisheries Kagoshima University 4-50-20 Shimoarata Kagoshima 890-0056 Japan Fax 81 99 2864015 Tel 81 99 2864172 E-mail yamada@ Enzyme EC recommended name Xaa-methyl-His dipeptidase other names anserinase aminoacyl-methylhistidine dipeptidase acetylhistidine deacetylase N-acetylhistidine deacetylase a-N-acetyl-L-histidine aminohydrolase X-methyl-His dipeptidase Anserinase Xaa-methyl-His dipeptidase EC is a dipeptidase that mainly catalyzes the hydrolysis of Na-acetylhistidine in the brain retina and vitreous body of all poikilothermic vertebrates. The gene encoding anserinase has not been previously identified. We report the molecular identification of anserinase purified from brain of Nile tilapia Oreochromis niloticus. The determination of the N-terminal sequence of the purified anserinase allowed the design of primers permitting the corresponding cDNA to be cloned by PCR. The anserinase cDNA has an ORF of 1485 nucleotides and encodes a signal peptide of 18 amino acids and a mature protein of 476 amino acids with a predicted molecular mass of kDa. Sequence analysis showed that anserinase is a member of the M20A metal-lopeptidase subfamily in MEROPS peptidase database to which serum carnosinase EC and cytosolic nonspecific dipeptidase EC CNDP belong. A cDNA encoding CNDP-like protein was also isolated from tilapia brain. Whereas anserinase mRNA was detected only in brain retina kidney and skeletal muscle CNDP-like protein mRNA was detected in all tissues examined. Note The nucleotide sequences reported in this paper have been submitted to DDBJ EMBL GenBank databank with accession numbers AB179777 .

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