The crystal structure and identification of NQM1/YGR043C, a transaldolase from Saccharomyces cerevisiae.

@article{Huang2008TheCS,
  title={The crystal structure and identification of NQM1/YGR043C, a transaldolase from Saccharomyces cerevisiae.},
  author={Hua Huang and Hui Rong and Xin Li and Shuilong Tong and Zhiqiang Zhu and Liwen Niu and Maikun Teng},
  journal={Proteins},
  year={2008},
  volume={73 4},
  pages={1076-81}
}
Transaldolase belongs to the class I aldolase family, whose members are the pivotal enzymes catalyzing the most important carbon-carbon bond-forming reactions and aldol condensation reactions.1 Different from the members of the class II adolase family, transaldolase is characterized by the formation of a covalent Schiff base intermediate between a lysine residue within the active site and the substrate.2–4 As a key enzyme in the pentose phosphate pathway, transaldolase catalyzes the reversible… CONTINUE READING

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