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Uncovering malate dehydrogenase: structure, function and role in disease.
Peterson, Celeste N; Cornely, Kathleen; Parente, Amy D; Springer, Amy L; Provost, Joseph J.
Afiliação
  • Peterson CN; Department of Biology, Suffolk University, Boston, MA U.S.A.
  • Cornely K; Department of Chemistry and Biochemistry, Providence College, Providence, RI, U.S.A.
  • Parente AD; Department of Chemistry and Biochemistry, Mercyhurst University, Eerie, PA U.S.A.
  • Springer AL; Department of Biochemistry and Molecular Biology, University of Massachusetts, Amherst, MA U.S.A.
  • Provost JJ; Department of Chemistry and Biochemistry, University of San Diego, San Diego, CA U.S.A.
Essays Biochem ; 68(2): 53-55, 2024 Oct 03.
Article em En | MEDLINE | ID: mdl-39361129
ABSTRACT
Malate dehydrogenases (MDHs) have been extensively studied since the 1960s due to their key roles in carbon metabolism and pathways such as redox balance and lipid synthesis. Recently, there has been renewed interest in these enzymes with the discovery of their role in the metabolic changes that occur during cancer and a widespread community of undergraduate teaching laboratories addressing MDH research questions, the Malate Dehydrogenase CUREs Community (MCC). This special issue describes different facets of MDH, including its physiological role, its structure-function relationships, its regulation through post-translational modifications, and perspectives on its evolutionary history. There are two human isoforms a cytoplasmic isoform that carries out formation of NAD+ for glycolysis, and a mitochondrial isoform that plays a major role in the citric acid cycle. Although the sequences of these two isoforms vary, the structures of the enzymes are similar, and studies suggest that each isoform may form complexes with other enzymes in common pathways. Experimental and theoretical advances have helped to characterize the post-translational modifications of MDH, allowing us to ask more complex questions involving the regulation of the enzyme and substrate promiscuity in the context of cancer. Additionally, there are many unresolved questions on the role of malate dehydrogenase in other organisms, especially in parasites. The review articles in this issue seek to shed light on the latest advances in our understanding of MDH and highlight areas for future studies.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Processamento de Proteína Pós-Traducional / Malato Desidrogenase Limite: Animals / Humans Idioma: En Revista: Essays Biochem Ano de publicação: 2024 Tipo de documento: Article País de publicação: Reino Unido
Texto completo
Adicionar na Minha BVS
Imprimir
XML
PubMed Links
Buscar no Google

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Processamento de Proteína Pós-Traducional / Malato Desidrogenase Limite: Animals / Humans Idioma: En Revista: Essays Biochem Ano de publicação: 2024 Tipo de documento: Article País de publicação: Reino Unido