Saccharomyces cerevisiae NRE1 and IRC24 Encode Paralogous Benzil Oxidoreductases

Irc24p is a benzil oxidoreductase encoded on chromosome IX of Saccharomyces cerevisiae . We identified a putative paralog, Nre1p, encoded 284 bp downstream. Both proteins are small, cytoplasmic, and are 52% identical (70% similar). PANTHER and PFAM analysis of the amino acid sequences and rigid pair...

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Detalles Bibliográficos
Autores principales: Garcia, Brandon, Riley, Kasandra J.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Caltech Library 2023
Materias:
New Finding
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10436073/
https://www.ncbi.nlm.nih.gov/pubmed/37602278
http://dx.doi.org/10.17912/micropub.biology.000910
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author Garcia, Brandon
Riley, Kasandra J.
author_facet Garcia, Brandon
Riley, Kasandra J.
author_sort Garcia, Brandon
collection PubMed
description Irc24p is a benzil oxidoreductase encoded on chromosome IX of Saccharomyces cerevisiae . We identified a putative paralog, Nre1p, encoded 284 bp downstream. Both proteins are small, cytoplasmic, and are 52% identical (70% similar). PANTHER and PFAM analysis of the amino acid sequences and rigid pairwise structure alignment predicted a conserved active site and Rossmann folds in both, implicating NADH or NADPH as likely cofactors. We purified hexahistidine-tagged Irc24p and Nre1p. Both proteins catalyze the reduction of the diketone benzil with similar kinetics and a preference for NADPH. This is the first demonstration of in vitro function for Nre1p.
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spelling pubmed-104360732023-08-19 Saccharomyces cerevisiae NRE1 and IRC24 Encode Paralogous Benzil Oxidoreductases Garcia, Brandon Riley, Kasandra J. MicroPubl Biol New Finding Irc24p is a benzil oxidoreductase encoded on chromosome IX of Saccharomyces cerevisiae . We identified a putative paralog, Nre1p, encoded 284 bp downstream. Both proteins are small, cytoplasmic, and are 52% identical (70% similar). PANTHER and PFAM analysis of the amino acid sequences and rigid pairwise structure alignment predicted a conserved active site and Rossmann folds in both, implicating NADH or NADPH as likely cofactors. We purified hexahistidine-tagged Irc24p and Nre1p. Both proteins catalyze the reduction of the diketone benzil with similar kinetics and a preference for NADPH. This is the first demonstration of in vitro function for Nre1p. Caltech Library 2023-08-03 /pmc/articles/PMC10436073/ /pubmed/37602278 http://dx.doi.org/10.17912/micropub.biology.000910 Text en Copyright: © 2023 by the authors https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
spellingShingle New Finding
Garcia, Brandon
Riley, Kasandra J.
Saccharomyces cerevisiae NRE1 and IRC24 Encode Paralogous Benzil Oxidoreductases
title Saccharomyces cerevisiae NRE1 and IRC24 Encode Paralogous Benzil Oxidoreductases
title_full Saccharomyces cerevisiae NRE1 and IRC24 Encode Paralogous Benzil Oxidoreductases
title_fullStr Saccharomyces cerevisiae NRE1 and IRC24 Encode Paralogous Benzil Oxidoreductases
title_full_unstemmed Saccharomyces cerevisiae NRE1 and IRC24 Encode Paralogous Benzil Oxidoreductases
title_short Saccharomyces cerevisiae NRE1 and IRC24 Encode Paralogous Benzil Oxidoreductases
title_sort saccharomyces cerevisiae nre1 and irc24 encode paralogous benzil oxidoreductases
topic New Finding
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10436073/
https://www.ncbi.nlm.nih.gov/pubmed/37602278
http://dx.doi.org/10.17912/micropub.biology.000910
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