Literature DB >> 1963432

Primary structure of the inorganic pyrophosphatase from thermophilic bacterium PS-3.

T Ichiba1, O Takenaka, T Samejima, A Hachimori.   

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.

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Year:  1990        PMID： 1963432     DOI： 10.1093/oxfordjournals.jbchem.a123244

Source DB:  PubMed          Journal:  J Biochem        ISSN： 0021-924X            Impact factor:   3.387


  4 in total

1.  An unusual route to thermostability disclosed by the comparison of Thermus thermophilus and Escherichia coli inorganic pyrophosphatases.

Authors:  T Salminen; A Teplyakov; J Kankare; B S Cooperman; R Lahti; A Goldman
Journal:  Protein Sci       Date:  1996-06       Impact factor: 6.725

2.  Crystal structure of inorganic pyrophosphatase from Thermus thermophilus.

Authors:  A Teplyakov; G Obmolova; K S Wilson; K Ishii; H Kaji; T Samejima; I Kuranova
Journal:  Protein Sci       Date:  1994-07       Impact factor: 6.725

3.  Effect of replacement of His-118, His-125 and Trp-143 by alanine on the catalytic activity and subunit assembly of inorganic pyrophosphatase from thermophilic bacterium PS-3.

Authors:  M Aoki; T Uchiumi; E Tsuji; A Hachimori
Journal:  Biochem J       Date:  1998-04-01       Impact factor: 3.857

4.  The role of histidine-118 of inorganic pyrophosphatase from thermophilic bacterium PS-3.

Authors:  N Hirano; T Ichiba; A Hachimori
Journal:  Biochem J       Date:  1991-09-01       Impact factor: 3.857
  4 in total

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