Literature DB >> 35696080

Bioinformatic Analyses of Peroxiredoxins and RF-Prx: A Random Forest-Based Predictor and Classifier for Prxs.

Hussam Al-Barakati1, Robert H Newman2, Dukka B Kc3, Leslie B Poole4.   

Abstract

Peroxiredoxins (Prxs) are a protein superfamily, present in all organisms, that play a critical role in protecting cellular macromolecules from oxidative damage but also regulate intracellular and intercellular signaling processes involving redox-regulated proteins and pathways. Bioinformatic approaches using computational tools that focus on active site-proximal sequence fragments (known as active site signatures) and iterative clustering and searching methods (referred to as TuLIP and MISST) have recently enabled the recognition of over 38,000 peroxiredoxins, as well as their classification into six functionally relevant groups. With these data providing so many examples of Prxs in each class, machine learning approaches offer an opportunity to extract additional information about features characteristic of these protein groups.In this study, we developed a novel computational method named "RF-Prx" based on a random forest (RF) approach integrated with K-space amino acid pairs (KSAAP) to identify peroxiredoxins and classify them into one of six subgroups. Our process performed in a superior manner compared to other machine learning classifiers. Thus the RF approach integrated with K-space amino acid pairs enabled the detection of class-specific conserved sequences outside the known functional centers and with potential importance. For example, drugs designed to target Prx proteins would likely suffer from cross-reactivity among distinct Prxs if targeted to conserved active sites, but this may be avoidable if remote, class-specific regions could be targeted instead.
© 2022. The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature.

Entities:  

Keywords:  Feature selection; Machine learning; Peroxiredoxin classification; Prx bioinformatics; Random forest

Mesh:

Substances:

Year:  2022        PMID: 35696080     DOI: 10.1007/978-1-0716-2317-6_8

Source DB:  PubMed          Journal:  Methods Mol Biol        ISSN: 1064-3745


  55 in total

1.  Structural evidence that peroxiredoxin catalytic power is based on transition-state stabilization.

Authors:  Andrea Hall; Derek Parsonage; Leslie B Poole; P Andrew Karplus
Journal:  J Mol Biol       Date:  2010-07-17       Impact factor: 5.469

Review 2.  Discovering mechanisms of signaling-mediated cysteine oxidation.

Authors:  Leslie B Poole; Kimberly J Nelson
Journal:  Curr Opin Chem Biol       Date:  2008-03-07       Impact factor: 8.822

Review 3.  Cysteine-mediated redox signaling: chemistry, biology, and tools for discovery.

Authors:  Candice E Paulsen; Kate S Carroll
Journal:  Chem Rev       Date:  2013-03-20       Impact factor: 60.622

4.  Analysis of the kinetic mechanism of enterococcal NADH peroxidase reveals catalytic roles for NADH complexes with both oxidized and two-electron-reduced enzyme forms.

Authors:  E J Crane; D Parsonage; L B Poole; A Claiborne
Journal:  Biochemistry       Date:  1995-10-31       Impact factor: 3.162

5.  Cloning and sequencing of thiol-specific antioxidant from mammalian brain: alkyl hydroperoxide reductase and thiol-specific antioxidant define a large family of antioxidant enzymes.

Authors:  H Z Chae; K Robison; L B Poole; G Church; G Storz; S G Rhee
Journal:  Proc Natl Acad Sci U S A       Date:  1994-07-19       Impact factor: 11.205

Review 6.  Protein-sulfenic acids: diverse roles for an unlikely player in enzyme catalysis and redox regulation.

Authors:  A Claiborne; J I Yeh; T C Mallett; J Luba; E J Crane; V Charrier; D Parsonage
Journal:  Biochemistry       Date:  1999-11-23       Impact factor: 3.162

Review 7.  The Conundrum of Hydrogen Peroxide Signaling and the Emerging Role of Peroxiredoxins as Redox Relay Hubs.

Authors:  Sarah Stöcker; Koen Van Laer; Ana Mijuskovic; Tobias P Dick
Journal:  Antioxid Redox Signal       Date:  2017-07-17       Impact factor: 8.401

Review 8.  Peroxiredoxins: guardians against oxidative stress and modulators of peroxide signaling.

Authors:  Arden Perkins; Kimberly J Nelson; Derek Parsonage; Leslie B Poole; P Andrew Karplus
Journal:  Trends Biochem Sci       Date:  2015-06-09       Impact factor: 13.807

9.  Evidence for a single active-site cysteinyl residue in the streptococcal NADH peroxidase.

Authors:  L B Poole; A Claiborne
Journal:  Biochem Biophys Res Commun       Date:  1988-05-31       Impact factor: 3.575

10.  An alkyl hydroperoxide reductase from Salmonella typhimurium involved in the defense of DNA against oxidative damage. Purification and properties.

Authors:  F S Jacobson; R W Morgan; M F Christman; B N Ames
Journal:  J Biol Chem       Date:  1989-01-25       Impact factor: 5.157

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