What is it about?
The purpose of this investigation was to reaction phenotype the identity of the cytosolic enzyme responsible for the S-oxidation of S-carboxymethyl-L-cysteine (SCMC) in female human hepatic cytosolic fractions. The identity of this enzyme in the female Wistar rat hepatic cytosolic fraction was found to be phenylalanine 4-monooxygenase (PAH). In pooled female human hepatic cytosolic fractions the calculated Km and Vmax for substrate (SCMC) activated PAH was 16.22 ± 11.31 mM and 0.87 ± 0.41 nmoles.rmVmg"1. The experimental data modelled to the Michaelis-Menten equation with non-competitive substrate inhibition. When the cytosolic fractions were activated with lysophophatidylcholine the Vmax increased to 52.31 ± 11.72 nmoles.min"'mg"1 but the Km remained unchanged at 16.53 ± 2.32 mM. A linear correlation was seen in the production of Tyr and SCMC.
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Why is it important?
First reports of the role of phenylalanine 4-monoxygenase in the S-oxidation of S-carboxymethyl-L-cysteine in human hepatic cytosolic fractions.
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This page is a summary of: Phenylalanine 4-monooxygenase and the S-Oxidation of S-Carboxymethyl-L-cysteine by Human Cytosolic Fractions, Drug Metabolism and Drug Interactions, January 2008, De Gruyter,
DOI: 10.1515/dmdi.2008.23.3-4.261.
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