ArticleProteins2011
Structure of an archaeal-type phosphoenolpyruvate carboxylase sensitive to inhibition by aspartate.
Article in Proteins, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 8 citations in OpenAlex.
- The PEP-pyruvate-oxaloacetate node: variation at the heart of metabolism.FEMS microbiology reviews · 2021Article
- Glucose Metabolism and Acetate Switch in Archaea: the Enzymes in Haloferax volcanii.Journal of bacteriology · 2021Article
- Phosphoenolpyruvate carboxylase identified as a key enzyme in erythrocytic Plasmodium falciparum carbon metabolism.PLoS pathogens · 2014Article
- Biochemistry and physiology of the β class carbonic anhydrase (Cpb) from Clostridium perfringens strain 13.Journal of bacteriology · 2013Article
- Greater efficiency of photosynthetic carbon fixation due to single amino-acid substitution.Nature communications · 2013Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The crystal structure of an archaeal-type phosphoenolpyruvate carboxylase from Clostridium perfringens has been determined based on X-ray data extending to 3 Å. The asymmetric unit of the structure includes two tetramers (each a dimer-of-dimers) of the enzyme. The precipitant, malonate, employed for the crystallization is itself a weak inhibitor of phosphoenolpyruvate carboxylase and a malonate molecule is seen in the active-site in the crystal structure. The allosteric binding sites for aspartate (an inhibitor) and glucose-6-phosphate (an activator) observed in the Escherichia coli and Zea mays phosphoenolpyruvate carboxylase structures, respectively, are not conserved in the C. perfringens structure. Aspartate inhibits the C. perfringens enzyme competitively with respect to the substrate, Mg(++.) phosphoenolpyruvate. A mechanism for inhibition is proposed based on the structure and sequence comparisons with other archaeal-type phosphoenolpyruvate carboxylases with differing sensitivity to inhibition by aspartate.
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Registered trials
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