Open AccessA phosphate‐stimulated NAD(P) + ‐dependent glyceraldehyde‐3‐phosphate dehydrogenase in Bacillus cereus
Author(s) -
Iddar Abdelghani,
Serrano Aurelio,
Soukri Abdelaziz
Publication year - 2002
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.1574-6968.2002.tb11199.x
Subject(s) - glyceraldehyde 3 phosphate dehydrogenase , bacillus cereus , dehydrogenase , nad+ kinase , biochemistry , cereus , enzyme , glyceraldehyde , cofactor , bacillales , biology , bacillaceae , phosphate , microbiology and biotechnology , chemistry , bacteria , genetics , bacillus subtilis
Glyceraldehyde‐3‐phosphate dehydrogenase (GAPDH), a key enzyme of central carbon metabolism, was studied in a Bacillus cereus strain isolated from the phosphate layer from Morocco. Enzymatic assays with cell extracts demonstrated that when grown on Luria–Bertani (LB) medium, B. cereus contains a major NAD + ‐dependent GAPDH activity and only traces of NADP + ‐dependent activity, but in cells grown on Pi‐supplemented LB medium a strong increase of the NADP + ‐dependent activity, that became predominant, occurs concurrently with a GAPDH protein increase. Our results show that B. cereus possesses two GAPDH activities, namely NAD + ‐ and NADP + ‐dependent, catalyzed by two enzymes with distinct coenzyme specificity and different phosphate regulation patterns. The finding of a phosphate‐stimulated NADP + ‐dependent GAPDH in B. cereus indicates that this bacterium can modulate its primary carbon metabolism according to phosphate availability.