Allantoate transport in Saccharomyces cerevisiae.

Abstract:

:Allantoate uptake appears to be mediated by an energy-dependent active transport system with an apparent Michaelis constant of about 50 microM. Cells were able to accumulate allantoate to greater than 3,000 times the extracellular concentration. The rate of accumulation was maximum at pH 5.7 to 5.8. The energy source for allantoate uptake is probably different from that for uptake of the other allantoin pathway intermediates. The latter systems are inhibited by arsenate, fluoride, dinitrophenol, and carboxyl cyanide-m-chlorophenyl hydrazone, whereas allantoate accumulation was sensitive to only dinitrophenol and carboxyl cyanide-m-chlorophenyl hydrazone. Efflux of preloaded allanotate did not occur at detectable levels. However, exchange of intra- and extracellular allantoate was found to occur very slowly. The latter two characteristics are shared with the allantoin uptake system and may result from the sequestering of intracellular allantoate within the cell vacuole. During the course of these studies, we found that, contrary to earlier reports, the reaction catalyzed by allantoinase is freely reversible.

journal_name

J Bacteriol

journal_title

Journal of bacteriology

authors

Turoscy V,Cooper TG

doi

10.1128/JB.140.3.971-979.1979

subject

Has Abstract

pub_date

1979-12-01 00:00:00

pages

971-9

issue

3

eissn

0021-9193

issn

1098-5530

journal_volume

140

pub_type

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