Abstract
Publisher Summary This chapter provides information on enzyme salicylate hydroxylase. Salicylate hydroxylase is a flavoprotein hydroxylase, a member of a class of enzymes elaborated by some soil bacteria, typically pseudomonads. These enzymes are induced by the presence of phenolic compounds. The activity of the enzyme was determined spectrophotometrically by following the rate of substrate-dependent oxidation of NADH in a Cary 14 or Gilford 2400 spectrophotometer at 340 nm. Salicylate hydroxylate is established as a flavoprotein containing flavin adenine dinucleotide (FAD) as the sole prosthetic group. The purified hydroxylase migrates as one homogeneous and symmetrical peak in the Model E analytical untracentrifuge with 0.1 M KCl as solvent. Enzyme activity can also be assayed by measuring the rate of oxygen consumption using an oxygen electrode. This enzyme, in addition to its FAD prosthetic group, has three substrates: salicylate or other aromatic compound, pyridine nucleotide, and oxygen. Its kinetics, therefore, can be expected to be complex.
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