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Purification and sequence identification of anserinase
Author(s) -
Yamada Shoji,
Tanaka Yoshito,
Ando Seiichi
Publication year - 2005
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/j.1742-4658.2005.04991.x
Subject(s) - complementary dna , dipeptidase , biology , biochemistry , amino acid , subfamily , cdna library , microbiology and biotechnology , molecular mass , peptide sequence , signal peptide , gene , enzyme
Anserinase (Xaa‐methyl‐His dipeptidase, EC 3.4.13.5) is a dipeptidase that mainly catalyzes the hydrolysis of N α‐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 53.3 kDa. Sequence analysis showed that anserinase is a member of the M20A metallopeptidase subfamily in MEROPS peptidase database, to which ‘serum’ carnosinase (EC 3.4.13.20) and cytosolic nonspecific dipeptidase (EC 3.4.13.18, 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.