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Literature summary extracted from

  • Karnawat, V.; Mehrotra, S.; Balaram, H.; Puranik, M.
    Exquisite modulation of the active site of Methanocaldococcus jannaschii adenylosuccinate synthetase in forward reaction complexes (2016), Biochemistry, 55, 2491-2499 .
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
6.3.4.4 analysis of high-resolution vibrational spectral fingerprints of each substrate and intermediate. The bound IMP is distorted toward its N1-deprotonated form even in the absence of any other ligands. Specific interactions between GTP and active-site amino acid residues result in large Raman shifts and contribute substantially to intrinsic binding energy. When both IMP and GTP are simultaneously bound, IMP is converted into an intermediate 6-phosphoryl inosine 5'-monophosphate. The intermediate complex is stable upon binding of the third ligand, L-aspartae analogue hadaicin. In the absence of hadaicin, 6-phosphoryl inosine 5'-monophosphate is quickly released from ADSS, is unstable in solution, and converts back into IMP. Hadaicin allosterically stabilizes ADSS through local conformational rearrangements Methanocaldococcus jannaschii

Organism

EC Number Organism UniProt Comment Textmining
6.3.4.4 Methanocaldococcus jannaschii Q57981
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6.3.4.4 Methanocaldococcus jannaschii DSM 2661 Q57981
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Synonyms

EC Number Synonyms Comment Organism
6.3.4.4 purA
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 Methanocaldococcus jannaschii