Interconverting the Catalytic Activities of (βα)8-barrel Enzymes from Different Metabolic Pathways: Sequence Requirements and Molecular Analysis

@inproceedings{Leopoldseder2004InterconvertingTC,
  title={Interconverting the Catalytic Activities of (βα)8-barrel Enzymes from Different Metabolic Pathways: Sequence Requirements and Molecular Analysis},
  author={Sonja Leopoldseder and J{\"o}rg Claren and Catharina J{\"u}rgens and Reinhard Sterner},
  year={2004}
}
The (betaalpha)(8)-barrel enzymes N'-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide isomerase (tHisA) and imidazole glycerol phosphate synthase (tHisF) from Thermotoga maritima catalyze two successive reactions in the biosynthesis of histidine. In both enzymes, aspartate residues at the C-terminal end of beta-strand 1 (Asp8 in tHisA and Asp11 in tHisF) and beta-strand 5 (Asp127 in tHisA and Asp130 in tHisF) are essential for catalytic activity. It was demonstrated… CONTINUE READING

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