Evidence that peroxiredoxins are novel members of the thioredoxin fold superfamily

E Schröder; C P Ponting

doi:10.1002/pro.5560071125

Evidence that peroxiredoxins are novel members of the thioredoxin fold superfamily

E Schröder, C P Ponting

Deanery of Molecular, Genetic and Population Health Sciences

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

Abstract / Description of output

Peroxiredoxins catalyze reduction of hydrogen peroxide or alkyl peroxide, to water or the corresponding alcohol. Detailed analysis of their sequences indicates that these enzymes possess a thioredoxin (Trx)-like fold and consequently are homologues of both thioredoxin and glutathione peroxidase (GPx). Sequence- and structure-based multiple sequence alignments indicate that the peroxiredoxin active site cysteine and GPx active site selenocysteine are structurally equivalent. Homologous peroxiredoxin and GPx enzymes are predicted to catalyze equivalent reactions via similar reaction intermediates.

Original language	English
Pages (from-to)	2465-8
Number of pages	4
Journal	Protein Science
Volume	7
Issue number	11
DOIs	https://doi.org/10.1002/pro.5560071125
Publication status	Published - Nov 1998

Keywords / Materials (for Non-textual outputs)

Amino Acid Sequence
Antioxidants
Binding Sites
Catalysis
Cysteine
Glutathione Peroxidase
Molecular Sequence Data
Oxidation-Reduction
Peroxidases
Peroxiredoxins
Protein Folding
Selenocysteine
Sequence Alignment
Thioredoxins

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10.1002/pro.5560071125

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@article{40cc09f743ef49a68e758071be1462be,

title = "Evidence that peroxiredoxins are novel members of the thioredoxin fold superfamily",

abstract = "Peroxiredoxins catalyze reduction of hydrogen peroxide or alkyl peroxide, to water or the corresponding alcohol. Detailed analysis of their sequences indicates that these enzymes possess a thioredoxin (Trx)-like fold and consequently are homologues of both thioredoxin and glutathione peroxidase (GPx). Sequence- and structure-based multiple sequence alignments indicate that the peroxiredoxin active site cysteine and GPx active site selenocysteine are structurally equivalent. Homologous peroxiredoxin and GPx enzymes are predicted to catalyze equivalent reactions via similar reaction intermediates.",

keywords = "Amino Acid Sequence, Antioxidants, Binding Sites, Catalysis, Cysteine, Glutathione Peroxidase, Molecular Sequence Data, Oxidation-Reduction, Peroxidases, Peroxiredoxins, Protein Folding, Selenocysteine, Sequence Alignment, Thioredoxins",

author = "E Schr{\"o}der and Ponting, {C P}",

year = "1998",

month = nov,

doi = "10.1002/pro.5560071125",

language = "English",

volume = "7",

pages = "2465--8",

journal = "Protein Science",

issn = "0961-8368",

publisher = "Cold Spring Harbor Laboratory Press",

number = "11",

}

TY - JOUR

T1 - Evidence that peroxiredoxins are novel members of the thioredoxin fold superfamily

AU - Schröder, E

AU - Ponting, C P

PY - 1998/11

Y1 - 1998/11

N2 - Peroxiredoxins catalyze reduction of hydrogen peroxide or alkyl peroxide, to water or the corresponding alcohol. Detailed analysis of their sequences indicates that these enzymes possess a thioredoxin (Trx)-like fold and consequently are homologues of both thioredoxin and glutathione peroxidase (GPx). Sequence- and structure-based multiple sequence alignments indicate that the peroxiredoxin active site cysteine and GPx active site selenocysteine are structurally equivalent. Homologous peroxiredoxin and GPx enzymes are predicted to catalyze equivalent reactions via similar reaction intermediates.

AB - Peroxiredoxins catalyze reduction of hydrogen peroxide or alkyl peroxide, to water or the corresponding alcohol. Detailed analysis of their sequences indicates that these enzymes possess a thioredoxin (Trx)-like fold and consequently are homologues of both thioredoxin and glutathione peroxidase (GPx). Sequence- and structure-based multiple sequence alignments indicate that the peroxiredoxin active site cysteine and GPx active site selenocysteine are structurally equivalent. Homologous peroxiredoxin and GPx enzymes are predicted to catalyze equivalent reactions via similar reaction intermediates.

KW - Amino Acid Sequence

KW - Antioxidants

KW - Binding Sites

KW - Catalysis

KW - Cysteine

KW - Glutathione Peroxidase

KW - Molecular Sequence Data

KW - Oxidation-Reduction

KW - Peroxidases

KW - Peroxiredoxins

KW - Protein Folding

KW - Selenocysteine

KW - Sequence Alignment

KW - Thioredoxins

U2 - 10.1002/pro.5560071125

DO - 10.1002/pro.5560071125

M3 - Article

C2 - 9828014

SN - 0961-8368

VL - 7

SP - 2465

EP - 2468

JO - Protein Science

JF - Protein Science

IS - 11

ER -

Evidence that peroxiredoxins are novel members of the thioredoxin fold superfamily

Abstract / Description of output

Keywords / Materials (for Non-textual outputs)

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