a-Amino acids (glycine, serine, histidine, aspartic acid and cysteine) and dithiothreitol (DTT) have been shown to activate both activities of the NAD(NADP)-dependent glyceraldehyde-3-phosphate dehydrogenase from Chlorella. The activation is allosteric and reaches 200-700%. The Hill coefficient values are close to 2 with all activators. ATP activates NADP-dependent but inhibits NAD-dependent activity, napp and K values being the same for both enzyme activities. In this case positive cooperativity is also observed (naPr, = 2.2). The present findings reveal the possible regulation of GAPD function in Chlorella with each of the coenzymes.
Allosteric regulationGlyceraldehyde-3-phosphate dehydrogenase Chlorella a-Amino acid Dithiothreitol
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.