[Functionally important residues of glutamic acid in E. coli pyrophosphatase. I. Chemical modification and localization in the primary structure].

Inorganic pyrophosphatase of E. coli is rapidly and irreversibly inactivated by 5-ethyl-5-phenylisoxazolium-3'-sulfonate (Woodward's reagent K). The appearance in the absorption spectrum of a maximum at 340 nm testifies to the formation of an enzyme enol ester with the inhibitor.

Tyrosine-89 is important for enzymatic activity of S. cerevisiae inorganic pyrophosphatase.

7-Chloro-4-nitro-benzofurazan selectively modifies one PPase Tyr residue per subunit and lowers the enzyme activity. Hydrolysis of the modified protein by trypsin and then by chymotrypsin produces the 82-89 peptide which possesses modified Tyr-89. Substrate analog (CaPPi) and the product of the enzyme reaction, MgPi, protect the enzyme against inactivation.

[A functionally important Tyr-89 residue in Saccharomyces cerevisiae pyrophosphatase. II. A possible role in the mechanism of enzyme action].

Earlier it has been demonstrated that inactivation of inorganic pyrophosphatase (PPase) of S. cerevisiae by 7-chloro-4-nitronbenzofurasane is due to modification of Tyr89. The effect of pH and active center ligands on this reaction has been studied.

[Functionally important tyrosine residues in Saccharomyces cerevisiae pyrophosphatase. I. Chemical modification and localization in the primary structure].

Inorganic pyrophosphatase (PPase) of S. cerevisiae is effectively inactivated by 7-chloro-4-nitrobenzofuran; the CaPP1 substrate analog has a protective effect. The modified enzyme separated from low molecular weight contaminants has an adsorption maximum at 345 nm.