Glutamate uptake in Thiobacillus novellus.
Properties of the glutamate uptake system of Thiobacillus novellus were investigated using intact cells. Two kinetically distiguishable components were found and designated at the high-affinity (HA) component with an apparent Km of 33 micronM, and the low-affinity (LA) component with a Km of 18 mM. Glutamate accumulation was temperature-sensitive and could be inhibited by the addition of wide range of inhibitors including cyanide, dinitrophenol (DNP), iodoacetate, mercuric chloride, sodium azide, carbonyl cyanide m-chlorophenyl hydrazone (CCCP), and dicyclhexylcarbodiimide (DCCD). The complex kinetics of the uptake process may be due to the rapid incorporation of added glutamate into a small peptide. This soluble peptide was formed rapidly after glutamate addition, and accumulated in whole cells.
D001224:Aspartic Acid / Q000378:metabolism; D001693:Biological Transport, Active / Q000187:drug effects; D003486:Cyanides / Q000494:pharmacology; D004024:Dicyclohexylcarbodiimide / Q000494:pharmacology; D005459:Fluorides / Q000494:pharmacology; D005971:Glutamates / Q000378:metabolism*; D007700:Kinetics; D009566:Nitrates / Q000494:pharmacology; D013696:Temperature; D013855:Thiobacillus / Q000378:metabolism*; D014475:Uncoupling Agents / Q000494:pharmacology
D003486:Cyanides; D005971:Glutamates; D009566:Nitrates; D014475:Uncoupling Agents; D001224:Aspartic Acid; D004024:Dicyclohexylcarbodiimide; D005459:Fluorides