Inactivation of three monohydroxybenzoate mono-oxygenases from Rhodococcus erythropolis: The role of an arginine residue in the substrate-binding domain of p-hydroxybenzoate 3-hydroxylase

Add time:07/29/2019    Source:sciencedirect.com

p-Hydroxybenzoate 3-hydroxylase from Rhodococcus erythropolis was inactivated by 2,3-butanedione (BD), phenylglyoxal (PGO), and other chemical reagents. p-Hydroxybenzoate and NADH protected the enzyme from inactivation by BD. Judging from the amino acid composition of BD-treated enzyme in the presence and absence of p-hydroxybenzoate, one essential arginine residue in substrate-binding domain of the enzyme was shown to be essential to the binding of p-hydrozybenzoate to the enzyme. Salicylate 5-hydroxylase and m-hydroxybenzoate 6-hydroxylase from R. erythropolis were hardly inactivated. Neither of these two enzymes was considered to have a functional arginine residue required for interaction with the substrate.

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