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The primary structure of the larger subunit of soluble guanylyl cyclase from bovine lung Homology between the two subunits of the enzyme
Author(s) -
Koesling Doris,
Harteneck Christian,
Humbert Peter,
Bosserhoff Armin,
Frank Rainer,
Schultz Günter,
Böhme Eycke
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)81523-q
Subject(s) - protein subunit , adenylyl cyclase , protein primary structure , biochemistry , peptide sequence , enzyme , open reading frame , soluble guanylyl cyclase , amino acid , homology (biology) , molecular mass , biology , gucy1a3 , microbiology and biotechnology , chemistry , cyclase , gene , guanylate cyclase 2c , guanylate cyclase
The primary structure of the larger subunit of the soluble guanylyl cyclase from bovine lung, which catalyzes the formation of cyclic GMP from GTP, has been determined. Two clones, isolated from two bovine libraries yielded a total of 3261 bp with a coding region of 2073 bp. The open reading frame encodes a protein of 691 amino acids and a molecular mass of 77 500. The deduced amino acid sequence reveals regions which are, to a large extent, homologous to the sequence of the smaller subunit of the enzyme as well as to the sequences of other gyanylyl and adenylyl cyclases.