Cotransport of phosphate and sodium by yeast.
Phosphate uptake by yeast at pH 7.2 is mediated by two mechanisms, one of which has a Km of 30 micronM and is independent of sodium, and a sodium-dependent mechanism with a Km of 0.6 micronM, both Km values with respect to monovalent phosphate. The sodium-dependent mechanism has two sites with affinity for Na+, with affinity constants of 0.04 and 29 mM. Also lithium enhances phosphate uptake; the affinity constants for lithium are 0.3 and 36 mM. Other alkali ions do not stimulate phosphate uptake at pH 7.2. Ribidium has no effect on the stimulation of phosphate uptake by sodium. Phosphate and arsenate enhance sodium uptake at pH 7.2. The Km of this stimulation with regard to monovalent orthophosphate is about equal to that of the sodium-dependent phosphate uptake. The properties of the cation binding sites of the phosphate uptake mechanism and those of the phosphate-dependent cation transport mechanism have been compared. The existence of a separate sodium-phosphate cotransport system is proposed.
D000255:Adenosine Triphosphate / Q000378:metabolism; D000693:Anaerobiosis; D001149:Arsenates / Q000494:pharmacology; D001692:Biological Transport / Q000187:drug effects; D002414:Cations, Monovalent / Q000494:pharmacology; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D010710:Phosphates / Q000378:metabolism* / Q000494:pharmacology; D011188:Potassium / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000187:drug effects / Q000378:metabolism*; D012964:Sodium / Q000378:metabolism*
D001149:Arsenates; D002414:Cations, Monovalent; D010710:Phosphates; D000255:Adenosine Triphosphate; D012964:Sodium; D011188:Potassium