Amino acid sequence of guinea pig liver transglutaminase from its cDNA sequence

摘要: Transglutaminases (EC 2.3.2.13) catalyze the formation of epsilon-(gamma-glutamyl)lysine cross-links and substitution a variety primary amines for gamma-carboxamide groups protein-bound glutaminyl residues. These enzymes are involved in many biological phenomena. In this paper, complete amino acid sequence guinea pig liver transglutaminase, typical tissue-type nonzymogenic was predicted by cloning analysis DNA complementary to its mRNA. The cDNA clones carrying sequences 5'- 3'-end regions mRNA were obtained use partial-length transglutaminase [Ikura, K., Nasu, T., Yokota, H., Sasaki, R., & Chiba, H. (1987) Agric. Biol. Chem. 51, 957-961]. A total 3695 bases identified from data four overlapping clones. Northern blot poly(A+) RNA showed single species with 3.7-3.8 kilobases, indicating that almost all analyzed. composite contained 68 5'-untranslated region, 2073 an open reading frame encoded 691 acids, stop codon (TAA), 1544 3'-noncoding part poly(A) tail (7 bases). molecular weight calculated be 76,620 deduced, excluding initiator Met. This enzyme no carbohydrate [Folk, J. E., Chung, S. I. (1973) Adv. Enzymol. Relat. Areas Mol. 38, 109-191], but six potential Asn-linked glycosylation sites found deduced.(ABSTRACT TRUNCATED AT 250 WORDS)