Literature DB >> 24201353

Relationships among amino acid sequences of animal, microbial and plant peroxidases.

H Tyson1.   

Abstract

Relationships among 18 peroxidases amino acid sequences of animal, microbial and plant origin were examined using optimum alignment of all pairwise sequence combinations to generate a total distance matrix. The matrix was used to cluster the sequences with complete linkage (farthest neighbour) procedures. Specific distances were calculated from the total distances matrix. The patterns of specific distances for each sequence were compared to evaluate the relationships between sequences, check their significance and construct subgroups of related sequences. The results were compared with those from clustering and its resultant dendrogram; good agreement was achieved. The 18 sequences fell into two principal groups, plant peroxidases and animal/microbial peroxidases. Within the plant peroxidases four subgroups were detected; the animal/microbial peroxidases formed a fifth subgroup. Profiles were constructed for the subgroups from lists of matching amino acids generated by the alignment calculations. Superimposed lists were realigned to recognise conserved areas and elements. Individual subgroup profiles for the plant peroxidases were then combined into a single profile which in turn was combined with profiles from the animal/microbial peroxidases. The final profile suggested that numerous sequence features (motifs) were common to peroxidases of widely different function and origins.

Year:  1992        PMID: 24201353     DOI: 10.1007/BF00224164

Source DB:  PubMed          Journal:  Theor Appl Genet        ISSN: 0040-5752            Impact factor:   5.699


  25 in total

1.  Relationships between amino acid sequences determined through optimum alignments, clustering, and specific distance patterns: application to a group of scorpion toxins.

Authors:  H Tyson
Journal:  Genome       Date:  1992-04       Impact factor: 2.166

2.  Cloning and sequencing of cDNA for a highly anionic peroxidase from potato and the induction of its mRNA in suberizing potato tubers and tomato fruits.

Authors:  E Roberts; T Kutchan; P E Kolattukudy
Journal:  Plant Mol Biol       Date:  1988-01       Impact factor: 4.076

3.  Expression of a synthetic gene for horseradish peroxidase C in Escherichia coli and folding and activation of the recombinant enzyme with Ca2+ and heme.

Authors:  A T Smith; N Santama; S Dacey; M Edwards; R C Bray; R N Thorneley; J F Burke
Journal:  J Biol Chem       Date:  1990-08-05       Impact factor: 5.157

4.  The amino-acid sequence of bovine glutathione peroxidase.

Authors:  W A Günzler; G J Steffens; A Grossmann; S M Kim; F Otting; A Wendel; L Flohé
Journal:  Hoppe Seylers Z Physiol Chem       Date:  1984-02

5.  Classification of scorpion toxins according to amino acid composition and sequence.

Authors:  M J Dufton; H Rochat
Journal:  J Mol Evol       Date:  1984       Impact factor: 2.395

6.  Comparative biosequence metrics.

Authors:  T F Smith; M S Waterman; W M Fitch
Journal:  J Mol Evol       Date:  1981       Impact factor: 2.395

7.  Covalent structure of turnip peroxidase 7. Cyanogen bromide fragments, complete structure and comparison to horseradish peroxidase C.

Authors:  G Mazza; K G Welinder
Journal:  Eur J Biochem       Date:  1980-07

8.  Evolution of proteins formed by beta-sheets. II. The core of the immunoglobulin domains.

Authors:  A M Lesk; C Chothia
Journal:  J Mol Biol       Date:  1982-09-15       Impact factor: 5.469

9.  Molecular cloning of complementary DNA encoding the lignin-forming peroxidase from tobacco: Molecular analysis and tissue-specific expression.

Authors:  L M Lagrimini; W Burkhart; M Moyer; S Rothstein
Journal:  Proc Natl Acad Sci U S A       Date:  1987-11       Impact factor: 11.205

10.  Molecular cloning, nucleotide sequence, and abscisic acid induction of a suberization-associated highly anionic peroxidase.

Authors:  E Roberts; P E Kolattukudy
Journal:  Mol Gen Genet       Date:  1989-06
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  1 in total

1.  Two pathogen-responsive genes in parsley encode a tyrosine-rich hydroxyproline-rich glycoprotein (hrgp) and an anionic peroxidase.

Authors:  P Kawalleck; E Schmelzer; K Hahlbrock; I E Somssich
Journal:  Mol Gen Genet       Date:  1995-05-20
  1 in total

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