The charge state of substrates and inhibitors when bound to Lactobacillus casei dihydrofolate reductase [proceedings].

نویسندگان

  • K Hood
  • G C Roberts
چکیده

is strictly non-competitive with 3-phospho-~-glycerate at the catalytic centre and strictly competitive with the corresponding MgATP2-. Analogous product-inhibition patterns were previously obtained with ADP, being non-competitive with MgATPZand competitive with 3-phospho-~-glycerate (Larsson-Rainikiewicz & Arvidsson, 1971). ADP and 1,3-diphospho-~-glycerate appear preferentially to bind to sites that are involved in the substrate activation observed at elevated concentrations of MgATP2or 3-phosphoD-glycerate. The kinetic properties of the enzyme offer possibilities for the substrates, even at ‘low’ concentrations, to control very effectively the direction of the reversible reaction under, for example, conditions in vivo.

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عنوان ژورنال:
  • Biochemical Society transactions

دوره 5 3  شماره 

صفحات  -

تاریخ انتشار 1977