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Literature summary extracted from

  • Chen, S.; Tomchick, D.R.; Wolle, D.; Hu, P.; Smith, J.L.; Switzer, R.L.; Zalkin, H.
    Mechanism of the synergistic end-product regulation of Bacillus subtilis glutamine phosphoribosylpyrophosphate amidotransferase by nucleotides (1997), Biochemistry, 36, 10718-10726.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.4.2.14 crystals of the ternary enzyme-ADP-GMP complex are grown in glass melting point capillaries by the microbath method, 20 mg/ml enzyme are incubated with 1 mM ADP, 1 mM GMP, and 5 mM MgCl2 and mixed with an equal volume of 24% polyethylene glycol 8000, 200 mM KCl, 50 mM N-(2-hydroxyethyl)piperazine-N'-3-propanesulfonic acid, pH 7.9, brown crystals emerge after 6-12 weeks Bacillus subtilis

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.4.2.14 ADP 50% inhibition of wild-type, S283A, K305Q, R307Q and S347A mutant enzyme at 4.7 mM, 24 mM, 31 mM, 28 mM and 8.1 mM respectively Bacillus subtilis
2.4.2.14 AMP 50% inhibition of wild-type, S283A, K305Q, R307Q and S347A mutant enzyme at 0.9 mM, 6.1 mM, 2.5 mM, 2.6 mM and 1.5 mM respectively Bacillus subtilis
2.4.2.14 GMP 50% inhibition of wild-type, S283A, K305Q, R307Q and S347A mutant enzyme at 9.4 mM, 6.6 mM, 50 mM, 50 mM and 145 mM respectively Bacillus subtilis
2.4.2.14 IMP 50% inhibition of wild-type and S347A mutant enzyme at 26 mM and 41 mM respectively Bacillus subtilis
2.4.2.14 additional information strong synergistic inhibition with ADP and GMP Bacillus subtilis

Organism

EC Number Organism UniProt Comment Textmining
2.4.2.14 Bacillus subtilis P00497
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