The steady state kinetics of pig liver glucose 6 phosphate dehydrogenase is consistent with an ordered, sequential mechanism in which NADP is bound first and NADPH released last. K(ia) is 9.0 μM, K(a) is 4.8 μM, and K(b) is 36 μM. Glucosamine 6 phosphate, a substrate analogue and competitive inhibitor, is used to help rule out a possible random mechanism. ADP is seen to form a complex with the free form of the enzyme whereas ATP forms a complex with both the free and E.NADP forms of the enzyme. The K(I) for the E.ADP complex is 1.9 mM, while the K(I) values for the E.ATP and E.NADP.ATP complexes are 7.2 and 4.5 mM, respectively.
|Original language||English (US)|
|Number of pages||5|
|Journal||Journal of Biological Chemistry|
|State||Published - 1976|
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology