Porphobilinogen synthase from pea: expression from an artificial gene, kinetic characterization, and novel implications for subunit interactions.

@article{Kervinen2000PorphobilinogenSF,
  title={Porphobilinogen synthase from pea: expression from an artificial gene, kinetic characterization, and novel implications for subunit interactions.},
  author={Jukka Kervinen and Roland L. Dunbrack and Silvana Litwin and Jacob Martins and Robert C. Scarrow and Michael V.. Volin and Anthony T. Yeung and Eun-ja Yoon and Eileen K Jaffe},
  journal={Biochemistry},
  year={2000},
  volume={39 30},
  pages={
          9018-29
        }
}
Porphobilinogen synthase (PBGS) is present in all organisms that synthesize tetrapyrroles such as heme, chlorophyll, and vitamin B(12). The homooctameric metalloenzyme catalyzes the condensation of two 5-aminolevulinic acid molecules to form the tetrapyrrole precursor porphobilinogen. An artificial gene encoding PBGS of pea (Pisum sativum L.) was designed to overcome previous problems during bacterial expression caused by suboptimal codon usage and was constructed by recursive polymerase chain… CONTINUE READING

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