The charge state of substrates and inhibitors when bound to Lactobacillus casei dihydrofolate reductase [proceedings].
نویسندگان
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.
منابع مشابه
Binding to Lactobacillus casei Dihydrofolate Reductase
The u.v. difference spectra generated when methotrexate, trimethoprim or folate bind to Lactobacillus casei dihydrofolate reductase were analysed. The difference spectrum produced by methotrexate binding is shown to consist of three components: (a) one closely resembling that observed on protonation of methotrexate, reflecting an increased degree of protonation on binding; (b) a pH-independent ...
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ورودعنوان ژورنال:
- Biochemical Society transactions
دوره 5 3 شماره
صفحات -
تاریخ انتشار 1977