A structural perspective on enzymes activated by monovalent cations.
نویسنده
چکیده
Enzymes activated by monovalent cations are abundantly represented in plants and the animal world. They have evolved to exploit Na+ and K+, readily available in biological environments, as major driving forces for substrate binding and catalysis. Recent progress in the structural biology of such enzymes has answered long standing questions about the molecular mechanism of activation and the origin of monovalent cation selectivity. That enables a simple classification of these functionally diverse enzymes and reveals unanticipated connections with ion transporters.
منابع مشابه
Redesigning allosteric activation in an enzyme.
Enzyme activation by monovalent cations is widely documented in plants and the animal world. In type II enzymes, activation entails two steps: binding of the monovalent cation to its allosteric site and transduction of this event into enhanced catalytic activity. The effect has exquisite specificity for either Na(+) or K(+), the most abundant cations present in physiological environments. Enzym...
متن کاملSwitching cation-binding loops paves the way for redesigning allosteric activation.
A n extensive number of enzymes found in both plants and animals are activated by monovalent cations (1, 2). Pioneering work in the 1940s and 1950s revealed a critical K requirement for pyruvate kinase and the existence of Na-dependent activation of β-galactosidase (3, 4). Enzymes requiring K often can be activated by NH4 + and Rb but have more difficulties accommodating the larger Cs, and the ...
متن کاملMonovalent cation effects on intermolecular purine-purine-pyrimidine triple-helix formation.
The binding of a 19-mer guanosine-rich oligodeoxyribonucleotide, TG3TG4TG4TG3T (ODN 1), to a complementary polypurine DNA target was investigated by DNase I footprinting and restriction endonuclease protection assays. Monovalent cations inhibited intermolecular purine-purine-pyrimidine triple-helical DNA formation, with K+ and Rb+ being most effective, followed by NH4+ and Na+. Li+ and Cs+ had ...
متن کاملSecond-Shell Basic Residues Expand the Two-Metal-Ion Architecture of DNA and RNA Processing Enzymes
Synthesis and scission of phosphodiester bonds in DNA and RNA regulate vital processes within the cell. Enzymes that catalyze these reactions operate mostly via the recognized two-metal-ion mechanism. Our analysis reveals that basic amino acids and monovalent cations occupy structurally conserved positions nearby the active site of many two-metal-ion enzymes for which high-resolution (<3 Å) str...
متن کاملMonovalent Cation Activation of the Radical SAM Enzyme Pyruvate Formate-Lyase Activating Enzyme
Pyruvate formate-lyase activating enzyme (PFL-AE) is a radical S-adenosyl-l-methionine (SAM) enzyme that installs a catalytically essential glycyl radical on pyruvate formate-lyase. We show that PFL-AE binds a catalytically essential monovalent cation at its active site, yet another parallel with B12 enzymes, and we characterize this cation site by a combination of structural, biochemical, and ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
- The Journal of biological chemistry
دوره 281 3 شماره
صفحات -
تاریخ انتشار 2006