title: Substrate specificity of ascorbate oxidase: unexpected similarity to the reduction site of dopamine beta-monooxygenase.
abstract: A series of ascorbate derivatives has been used to examine the specificity of the reduction site of ascorbate oxidase. Replacement of the 6-OH group of ascorbic acid with either hydrogen or bromine does not alter the substrate activity significantly. 6-Amino-6-deoxy-L-ascorbic acid is a weak substrate for the enzyme, suggesting that positively charged groups at the 6-position are not well tolerated by the enzyme. The modification of the 5-OH reduces the effective interaction with the enzyme and the replacement of 6-OH with 6-S-phenyl- or 6-O-phenyl groups significantly increases the affinity for the enzyme. Both 2-Amino-6-S-phenyl-L-ascorbic acid and imino-D-glucoascorbic acid are not substrates for the enzyme. The stereoelectronic properties and alternate binding modes of these molecules are being considered to explain these observations. The substrate specificity of the enzyme is compared to the specificity of the reduction site of dopamine beta-monooxygenase.
authors.affiliation: Department of Chemistry, Wichita State University, KS 67260-0051.
authors.forename: K
authors.initials: K
authors.lastname: Wimalasena
authors.forename: S
authors.initials: S
authors.lastname: Dharmasena
mesh_terms: D001204:Ascorbate Oxidase / Q000378:metabolism*; D001205:Ascorbic Acid / Q000031:analogs & derivatives* / Q000138:chemical synthesis / Q000737:chemistry / Q000378:metabolism*; D001665:Binding Sites; D004299:Dopamine beta-Hydroxylase / Q000378:metabolism*; D007202:Indicators and Reagents; D007700:Kinetics; D009682:Magnetic Resonance Spectroscopy; D015394:Molecular Structure; D010084:Oxidation-Reduction; D013379:Substrate Specificity
chemical_list: D007202:Indicators and Reagents; D001204:Ascorbate Oxidase; D004299:Dopamine beta-Hydroxylase; D001205:Ascorbic Acid