Temperature adaptation in structure and function in lactate dehydrogenase-A reflects convergent evolution in a few key protein regions

Significance Substitutions in a few amino acids can significantly alter the structural and functional responses of enzymes to temperature, traits that are closely related to establishing the thermal optima and limits of organisms. A cross-taxa analysis of 277 fish lactate dehydrogenase-A (LDH-A) orthologs, which incorporated bioinformatic, in silico and in vitro methodologies, reveals striking convergence in the sites of temperature-adaptive evolution of LDH-As. Based on these findings, a deep learning model was developed to predict thermal limits of fish. These results further the understanding of how fish adapt to divergent thermal environments and provide a valuable model for assessing the potential thermal ranges of fish.

• Publication year

  2025

• Venue

  Proceedings of the National Academy of Sciences of the United States of America

• Publication date

  2025-10-10

• Fields of study

  Biology, Medicine, Computer Science, Environmental Science

• Identifiers
  DOI 10.1073/pnas.2517759122PMID 41071662PMCID 12557798
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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