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. 1991 Feb;10(1):43-8.
doi: 10.1007/BF01024654.

Arginyl residues in the NADPH-binding sites of phenol hydroxylase

T Sejlitz  1 , H Y Neujahr
Affiliations

Arginyl residues in the NADPH-binding sites of phenol hydroxylase

T Sejlitz et al. J Protein Chem. 1991 Feb.

Abstract

Phenol hydroxylase was inactivated by the arginine reagents 2,3-butanedione, 1,2-cyclohexanedione, and phenylglyoxal. The cosubstrate NADPH, as well as NADPH+ and several analogues thereof, protected the enzyme against inactivation. Phenol did not protect the activity against any of the reagents used, nor did modification by 2,3-butanedione affect the binding of phenol. We propose the presence of arginyl residues in the binding sites for the adenosine phosphate part of NADPH.

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