TY  - JOUR
TI  - Measurement of Glucose-6-phosphate Dehydrogenase Activity in Bacterial Cell-free Extracts
AU  - Karakaya, Haydar 
AU  - Özkul, Kübra 
VL  - 6
IS  - 19
PY  - 2016
DA  - 2016/10/05
SP  - e1949
C1  - Bio-protocol 2016;6:e1949
DO  - 10.21769/BioProtoc.1949
UR  - https://doi.org/10.21769/BioProtoc.1949
AB  - Glucose-6-phosphate dehydrogenase (G6PDH) (EC 1.1.1.49) is the first enzyme of the oxidative pentose phosphate cycle and catalyses the conversion of glucose-6-phosphate (G6P) to 6-phosphoglucono-δ-lactone and transfers one electron to NADP+ producing one NADPH. Conversion of G6P to 6-phosphoglucono-δ-lactone is proportional to the production of NADPH. The increase in NADPH concentration results in an increase in absorbance at 340 nm. To assay G6PDH activity, therefore, production of NADPH is determined by measuring increase in absorbance at 340 nm spectrophotometrically. This increase rate is then converted to unit of activity and specific activity of G6PDH. In this procedure, a generalized method is given for bacterial G6PDH assays emphasizing on a cyanobacterium Synechocystis sp. PCC6803 (Schaeffer and Stanier, 1978; Karakaya et al., 2008, 2012) and a heterotrophic bacterium E.coli (Hylemon and Phibbs, 1972; Barnel et al., 1990).
KW  - Cyanobacteria
KW  - Glucose-6-phosphate dehydrogenase
KW  - Specific activity
KW  - Cell-free extract
JF  - Bio-protocol
SN  - 2331-8325
PB  - Bio-protocol LLC.
BIO101  - False