Literature DB >> 2177893

Structural homology among the peroxidase enzyme family revealed by hydrophobic cluster analysis.

B Henrissat1, M Saloheimo, S Lavaitte, J K Knowles.   

Abstract

A number of peroxidase amino acid sequences show limited homology to short regions comprising the known active site cleft of yeast cytochrome c peroxidase. Otherwise no clear homology is visible in linear alignments between this enzyme and other peroxidases. We have subjected eight peroxidase sequences to hydrophobic cluster analysis. Our results suggest that these peroxidases are evolutionary related and that they share many folding characteristics.

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Year:  1990        PMID： 2177893     DOI： 10.1002/prot.340080307

Source DB:  PubMed          Journal:  Proteins        ISSN： 0887-3585


  15 in total

1.  Structure, function, and fate of the BlaR signal transducer involved in induction of beta-lactamase in Bacillus licheniformis.

Authors:  Y Zhu; S Englebert; B Joris; J M Ghuysen; T Kobayashi; J O Lampen
Journal:  J Bacteriol       Date:  1992-10       Impact factor: 3.490

2.  Induction of a Streptomyces cacaoi beta-lactamase gene cloned in S. lividans.

Authors:  V M Lenzini; J Magdalena; C Fraipont; B Joris; A Matagne; J Dusart
Journal:  Mol Gen Genet       Date:  1992-10

3.  A classification of glycosyl hydrolases based on amino acid sequence similarities.

Authors:  B Henrissat
Journal:  Biochem J       Date:  1991-12-01       Impact factor: 3.857

4.  The APX4 locus regulates seed vigor and seedling growth in Arabidopsis thaliana.

Authors:  Ya-Ying Wang; Amanda G Hecker; Bernard A Hauser
Journal:  Planta       Date:  2014-01-10       Impact factor: 4.116

5.  Analysis of the molecular evolutionary history of the ascorbate peroxidase gene family: inferences from the rice genome.

Authors:  Felipe Karam Teixeira; Larissa Menezes-Benavente; Rogério Margis; Márcia Margis-Pinheiro
Journal:  J Mol Evol       Date:  2004-12       Impact factor: 2.395

6.  HomologyPlot: searching for homology to a family of proteins using a database of unique conserved patterns.

Authors:  J M Parker; R S Hodges
Journal:  J Comput Aided Mol Des       Date:  1994-04       Impact factor: 3.686

7.  Primary and predicted secondary structures of the Actinomadura R39 extracellular DD-peptidase, a penicillin-binding protein (PBP) related to the Escherichia coli PBP4.

Authors:  B Granier; C Duez; S Lepage; S Englebert; J Dusart; O Dideberg; J Van Beeumen; J M Frère; J M Ghuysen
Journal:  Biochem J       Date:  1992-03-15       Impact factor: 3.857

8.  Crystal structure of lignin peroxidase.

Authors:  S L Edwards; R Raag; H Wariishi; M H Gold; T L Poulos
Journal:  Proc Natl Acad Sci U S A       Date:  1993-01-15       Impact factor: 11.205

9.  Amino acid sequence of the penicillin-binding protein/DD-peptidase of Streptomyces K15. Predicted secondary structures of the low Mr penicillin-binding proteins of class A.

Authors:  P Palomeque-Messia; S Englebert; M Leyh-Bouille; M Nguyen-Distèche; C Duez; S Houba; O Dideberg; J Van Beeumen; J M Ghuysen
Journal:  Biochem J       Date:  1991-10-01       Impact factor: 3.857

10.  Methods to investigate the expression of lignin peroxidase genes by the white rot fungus Phanerochaete chrysosporium.

Authors:  J Reiser; I S Walther; C Fraefel; A Fiechter
Journal:  Appl Environ Microbiol       Date:  1993-09       Impact factor: 4.792
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