ZIB

Hits per page

hit 1 - 1 | 1 hit

Select All Export

Electronic Resource

Properties of the glyceraldehyde-3-P dehydrogenase in heterocysts and vegetative cells of cyanobacteria (1986)

Papen, H. ; Neuer, G. ; Sauer, A. ; [et al.]

Oxford, UK : Blackwell Publishing Ltd

FEMS microbiology letters 36 (1986), S. 0

add to mindlist on the mindlist

Details

ISSN: 1574-6968

Source: Blackwell Publishing Journal Backfiles 1879-2005

Topics: Biology

Notes: Abstract Glyceraldehyde-3-P dehydrogenase (GAPDH) in heterocysts and vegetative cells of 3 N2-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.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1111/j.1574-6968.1986.tb01696.x

Library	Location	Call Number	Volume/Issue/Year	Availability

Others were also interested in ...

Paper (German National Licenses)

Fulltext

hit 1 - 1 | 1 hit