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- W1993207768 abstract "Activated phenylalanine 4-monooxygenase, phenylalanine hydroxylase (PAH), is known to be involved in the S-oxidation of a number of sulfide compounds. One of these compounds, S-carboxymethyl-l-cysteine (SCMC), is currently used for the treatment of chronic obstructive pulmonary disease and otitis media with effusion as a mucolytic agent, and the S-oxides are the major metabolites found in urine. However, the enzyme catalyzing the S-oxidation of SCMC has yet to be identified. Here we report on the role of nonactivated phenylalanine 4-monooxygenase activity in rat liver cytosol in the S-oxidation of SCMC. Linearity of the enzyme assays was seen for both time (0–16 min) and cytosolic protein concentration (0.1–0.5 mg/ml). The calculated Km and Vmax values for the formation of SCMC (S) S-oxide were 3.92 ± 0.15 mM and 1.10 ± 0.12 nmol SCMC (S) S-oxide formed/mg protein/min, respectively. The calculated Km and Vmax values for the formation of SCMC (R) S-oxide were 9.18 ± 1.13 mM and 0.46 ± 0.11 nmol SCMC (R) S-oxide formed/mg protein/min, respectively. These results indicate that in the female Wistar rat, nonactivated PAH showed a stereospecific preference for the formation of the (S) S-oxide metabolite of SCMC against the (R) S-oxide metabolite of SCMC." @default.
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- W1993207768 date "2004-12-01" @default.
- W1993207768 modified "2023-10-18" @default.
- W1993207768 title "Phenylalanine hydroxylase: possible involvement in the S-oxidation of S-carboxymethyl-l-cysteine" @default.
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- W1993207768 doi "https://doi.org/10.1016/j.ab.2004.08.003" @default.
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