Evolutionary Dynamics of Thiamine Pyrophosphate-Dependent Enzymes in Plants Revealed

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A team of researchers from the Chinese Academy of Sciences has conducted a comprehensive genome-wide phylogenetic analysis to investigate the evolutionary relationships of thiamine pyrophosphate (TPP)-dependent enzymes in plants. The study found that these enzymes are present in all domains of life, but their evolutionary dynamics in plants are not well understood. The researchers identified 103 plant TPP-dependent enzyme sequences in 16 plant species and grouped them into three major categories. The study revealed that plants have fewer TPP-dependent genes compared to other living organisms, with many types lost during evolution. The findings provide important insights into the evolution and function of the TPP-dependent gene family in plants.

Key Takeaways:

  • 103 plant TPP-dependent enzyme sequences were identified in 16 plant species.
  • The plant TPP-dependent genes fell into three major groups: acetolactate synthase, pyruvate dehydrogenase, and 2-hydroxyphytanoyl-CoA lyase.
  • The study revealed that plants have fewer TPP-dependent genes compared to other living organisms.
  • Many types of TPP-dependent genes were lost during evolution in plants.
  • Seed plants have more TPP genes compared to non-seed basal plants.
  • The results imply that seed plants developed more TPP genes to adapt to their environment.
  • The study provides important information for understanding the evolution and function of the TPP-dependent gene family in plants.

Statistics:

  • 103 plant TPP-dependent enzyme sequences were identified.
  • 16 plant species were analyzed in the study.
  • 3 major groups of plant TPP-dependent genes were identified: acetolactate synthase, pyruvate dehydrogenase, and 2-hydroxyphytanoyl-CoA lyase.
  • Plants have fewer TPP-dependent genes compared to other living organisms.

Sources:

  • Ye, Y., et al. (2015) Gene loss in plants: Evidence from genome-wide phylogenetic analysis of thiamine pyrophosphate-dependent enzymes. Journal of Systematics and Evolution, 2015;53(3):221-227.
  • Wiley-Blackwell, 111 River St, Hoboken 07030-5774, NJ, USA (www.wiley.com/)
  • Chinese Academy of Sciences, Institute of Oceanology, Key Lab of Experimental Marine Biology, Qingdao 266071, Shandong, People's Republic of China (X.M. Tian)
  • Additional authors: P. Wang, W.B. Hu, D.H. Gao, and Q. Li (Enzymes and Coenzymes)