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Fluoride is a strong and specific inhibitor of ( asymmetrical ) Ap 4 A hydrolases
Author(s) -
Guranowski Andrzej
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)80190-t
Subject(s) - hydrolase , fluoride , chemistry , enzyme , biochemistry , phosphodiesterase , hydrolysis , inorganic chemistry
Fluoride acts as a noncompetitive, strong inhibitor of ( asymmetrical ) Ap 4 A hydrolases (EC 3.6.1.17). The K i values estimated for the enzymes isolated from seeds of some higher plants (yellow lupin, sunflower and marrow) are in the range of 2–3 μM and I 50 for the hydrolase from a mammalian tissue (beef liver) is 20 μM. The anion, up to 25 mM, does not affect the following other enzymes which are able to degrade the bis(5'‐nucleosidyl)‐oligophosphates: Escherichia coli ( symmetrical ) Ap 4 A hydrolase (EC 3.6.1.41), yeast Ap 4 A phosphorylase (EC 2.7.7.53), yellow lupin Ap 3 A hydrolase (EC 3.6.1.29) and phosphodiesterase (EC 3.1.4.1). None of halogenic anions but fluoride affects the activity of ( asymmetrical ) Ap 4 A hydrolases. Usefulness of the fluoride effect for the in vivo studies on the Ap 4 A metabolism is shortly discussed.