@article{mbs:/content/journal/micro/10.1099/00221287-133-4-857, author = "Cartwright, Charles P. and Verzey, Felicity J. and Rose, Anthony H.", title = "Effect of Ethanol on Activity of the Plasma-membrane ATPase in, and Accumulation of Glycine by, Saccharomyces Cerevisiae", journal= "Microbiology", year = "1987", volume = "133", number = "4", pages = "857-865", doi = "https://doi.org/10.1099/00221287-133-4-857", url = "https://www.microbiologyresearch.org/content/journal/micro/10.1099/00221287-133-4-857", publisher = "Microbiology Society", issn = "1465-2080", type = "Journal Article", abstract = "SUMMARY: The pH optimum of the ATPase activity in plasma membranes from Saccharomyces cerevisiae NCYC 431 from 8 h cultures was around 65 and that in membranes from organisms from 16 h cultures near 6ยท0. The K m[ATP] of the enzyme was virtually unaffected by the age of the culture from which organisms were harvested, although the V max of the enzyme in membranes from organisms from 8 h cultures was higher than that for organisms from 16 h cultures. Ethanol noncompetitively inhibited ATPase activity in membranes, although the inhibition constant for the enzyme from organisms from 8 h cultures was lower than that from organisms from 16 h cultures. Glycine accumulation by the general amino acid permease was non-competitively inhibited by ethanol. Inhibition constants were virtually the same for glycine uptake by deenergized organisms from 8 h and 16 h cultures, but under energized conditions the value was greater for organisms from 16 h rather than 8 h cultures. The data indicate that inhibition of plasma-membrane ATPase activity by ethanol could account, at least in part, for inhibition of glycine accumulation by ethanol.", }