Studies on the metabolism of benoxinate by human pseudocholinesterase.

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Dubbels R, Schloot W

Studies on the metabolism of benoxinate by human pseudocholinesterase.

Metab Pediatr Syst Ophthalmol. 1983;7(1):37-43.

PubMed ID

6621359 [ View in PubMed

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Abstract

The local anesthetic drug benoxinate (oxybuprocaine, Novesine) is hydrolyzed to 3-butoxy-4-aminobenzoic acid. A rapid and simple spectrophotometric method for benoxinate hydrolysis by human plasma was developed. Benoxinate is hydrolyzed enzymatically by an esterase present in the serum. Heat stability characteristics and apparent affinity values of the benoxinate metabolizing enzyme were in the same range compared to benzoylcholine chloride hydrolysis. Apparent Vmax-values differ by a mean factor of about 18 between the hydrolysis of both substrates. Considerable interindividual variability of benoxinate hydrolysis and inhibition of the enzymatic reaction by dibucaine and sodium fluoride has been observed. Furthermore, enzyme activity with benoxinate as substrate is positively correlated (P less than 0.001) with benzoylcholine chloride hydrolysis. Therefore, we assume that benoxinate is metabolized by human pseudocholinesterase (PCHE, E.C. 3.1.1.8) and that ocular side effects after benoxinate application may be caused by altered metabolism of this drug, depending on genetically determined variants of pseudocholinesterase.

DrugBank Data that Cites this Article

Drug Enzymes

Drug	Enzyme	Kind	Organism	Pharmacological Action	Actions
Oxybuprocaine	Cholinesterase	Protein	Humans	Unknown	Substrate	Details