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

Bernard Henrissat; Markku Saloheimo; Stephanie Lavaitte; Jonathan Knowles

doi:10.1002/prot.340080307

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

Bernard Henrissat
, Markku Saloheimo
, Stephanie Lavaitte
, Jonathan Knowles

Centre de Recherches sur les Macromolécules Végétales (CERMAV-CNRS)

Research output: Contribution to journal › Article › Scientific › peer-review

51 Citations (Scopus)

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.

Original language	English
Pages (from-to)	251-257
Journal	Proteins: Structure, Function, and Bioinformatics
Volume	8
Issue number	3
DOIs	https://doi.org/10.1002/prot.340080307
Publication status	Published - 1990
MoE publication type	A1 Journal article-refereed

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10.1002/prot.340080307

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title = "Structural homology among the peroxidase enzyme family revealed by hydrophobic cluster analysis",

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.",

author = "Bernard Henrissat and Markku Saloheimo and Stephanie Lavaitte and Jonathan Knowles",

year = "1990",

doi = "10.1002/prot.340080307",

language = "English",

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pages = "251--257",

journal = "Proteins: Structure, Function, and Bioinformatics",

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T1 - Structural homology among the peroxidase enzyme family revealed by hydrophobic cluster analysis

AU - Henrissat, Bernard

AU - Saloheimo, Markku

AU - Lavaitte, Stephanie

AU - Knowles, Jonathan

PY - 1990

Y1 - 1990

N2 - 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.

AB - 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.

U2 - 10.1002/prot.340080307

DO - 10.1002/prot.340080307

M3 - Article

SN - 0887-3585

VL - 8

SP - 251

EP - 257

JO - Proteins: Structure, Function, and Bioinformatics

JF - Proteins: Structure, Function, and Bioinformatics

IS - 3

ER -

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

Abstract

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