Open AccessProperties of the glyceraldehyde‐3‐P dehydrogenase in heterocysts and vegetative cells of cyanobacteria
Author(s) -
Papen H.,
Neuer G.,
Sauer A.,
Bothe H.
Publication year - 1986
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1986.tb01696.x
Subject(s) - heterocyst , glyceraldehyde 3 phosphate dehydrogenase , biochemistry , dehydrogenase , cyanobacteria , glyceraldehyde , nad+ kinase , biology , citric acid cycle , oxidoreductase , enzyme , anabaena , chemistry , bacteria , genetics
Glyceraldehyde‐3‐P dehydrogenase (GAPDH) in heterocysts and vegetative cells of 3 N 2 ‐fixing cyanobacteria was found to utilize both NAD + and NADP + . The enzyme activity was enhanced by thiols (glutathione, reduced lipoic acid and dithiothreitol). GAPDH of the 3 cyanobacterial species was not activated by thioredoxin. Heterocysts have now been shown to possess all the enzymes of glycolysis and the tricarboxylic acid cycle to convert glyceraldehyde‐3‐phosphate (GAP) to oxoglutarate and glutamate. The GAPDH reaction is a major source for the generation of NADH, which is oxidized by a thylakoid‐bound NADH:plastoquinone oxidoreductase in heterocysts.