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Literature summary extracted from

  • McClory, J.; Timson, D.J.; Singh, W.; Zhang, J.; Huang, M.
    Reaction mechanism of isopentenyl phosphate kinase A QM/MM study (2017), J. Phys. Chem. B, 121, 11062-11071 .
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.7.4.26 catalytically competent structure in complex with Mg2+ . Substrate binding results in significant conformational change of residues Lys204, Glu207, and Lys211 located on the alphaG helix to form a strong salt bridge network with Asp145, which in turn tethers the invariant Ser142 via H-bond interaction. The conformational change shuts the subtrate entrance channel formed between the alphaG and alphaE helices Thermoplasma acidophilum

Organism

EC Number Organism UniProt Comment Textmining
2.7.4.26 Thermoplasma acidophilum Q9HLX1
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Synonyms

EC Number Synonyms Comment Organism
2.7.4.26 Ta0103
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Thermoplasma acidophilum