title: Primary structure of the inorganic pyrophosphatase from thermophilic bacterium PS-3.
abstract: The complete amino acid sequence of the inorganic pyrophosphatase from thermophilic bacterium PS-3 was determined by automated Edman analysis of the intact protein and of peptides derived from digests obtained with lysylendopeptidase, Staphylococcus aureus strain V8 protease, and arginylendopeptidase. The monomer peptide chain comprises 164 amino acid residues and has a calculated molecular weight of 18,792. The sequence is identical at about 46% of the amino acid positions with that of the Escherichia coli enzymes.
authors.affiliation: Institute of High Polymer Research, Faculty of Textile Science and Technology, Shinshu University, Nagano.
authors.forename: T
authors.initials: T
authors.lastname: Ichiba
authors.forename: O
authors.initials: O
authors.lastname: Takenaka
authors.forename: T
authors.initials: T
authors.lastname: Samejima
authors.forename: A
authors.initials: A
authors.lastname: Hachimori
mesh_terms: D000595:Amino Acid Sequence; D001322:Autoanalysis; D001419:Bacteria / Q000187:drug effects / Q000201:enzymology*; D004926:Escherichia coli / Q000187:drug effects / Q000201:enzymology*; D006868:Hydrolysis; D008969:Molecular Sequence Data; D008970:Molecular Weight; D011755:Pyrophosphatases / Q000737:chemistry*; D012697:Serine Endopeptidases / Q000378:metabolism / Q000494:pharmacology
chemical_list: D012697:Serine Endopeptidases; C028344:glutamyl endopeptidase; C036813:lysyl endopeptidase; D011755:Pyrophosphatases