Multisubstrate inhibition of 4-hydroxybenzoate 3-monooxygenase
FG Salituro, DA Demeter, HJR Weintraub…
Index: Salituro; Demeter; Weintraub; Lippert; Resvick; McDonald Journal of Medicinal Chemistry, 1994 , vol. 37, # 24 p. 4076 - 4078
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Citation Number: 4
Abstract
4-Hydroxybenzoate 3-monooxygenase (p-hydroxybenzoate hydroxylase, PHBH; EC 1.14. 13.21, isolated from Pseudomonas fluorescens, is a very well-characterized NADPH- dependent flavin-mono~ xygenasel-~ which catalyzes the conversion of p-hydroxybenzoate to 3, 4-dihydroxybenzoate (Scheme 1). Extensive enzyme kinetics, 6 inhibition studie~,~-~ and X-ray crystallographic studieslnJ1 have been published. The enzyme mechanism has ...
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