Open AccessInactivation of three monohydroxybenzoate mono‐oxygenases from Rhodococcus erythropolis : The role of an arginine residue in the substrate‐binding domain of p ‐hydroxybenzoate 3‐hydroxylase
Author(s) -
Suemori Akio,
Nakajima Kenji,
Kurane Ryuichiro,
Nakamura Yoshihiro
Publication year - 1994
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1994.tb07026.x
Subject(s) - phenylglyoxal , hydroxybenzoate , chemistry , enzyme , oxygenase , arginine , residue (chemistry) , biochemistry , stereochemistry , amino acid
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.