Distinct effects of pyridoxal phosphate on NAD- and NADP- linked malic enzymes of Escherichia coli.
NADP-linked malic enzyme from Escherichia coli W was inactivated by pyridoxal 5'-phosphate (PLP) following pseudo-first order kinetics. The inactivation was, however, reversed upon addition of an aminothiol, such as penicillamine and cysteamine, whereas the activity was not restored, when the PLP-inactivated enzyme was treated with NaBH4 prior to the addition of aminothiol. The inactivating effect was specific to PLP and no other structural analogs of PLP tested inactivated the enzyme, except that pyridoxal exhibited a similar effect, though to a lesser extent. In contrast, NAD-linked malic enzyme from the same micro-organism was insensitive to PLP, even in the presence of 0.8 M guanidine hydrochloride.
D004926:Escherichia coli / Q000201:enzymology*; D007700:Kinetics; D008291:Malate Dehydrogenase / Q000378:metabolism*; D009243:NAD / Q000378:metabolism*; D009249:NADP / Q000378:metabolism*; D011732:Pyridoxal Phosphate / Q000494:pharmacology*
D009243:NAD; D009249:NADP; D011732:Pyridoxal Phosphate; D008291:Malate Dehydrogenase