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Chemical modification of opiate receptors with ethoxyformic anhydride and photo-oxidation: evidence for essential histidyl residues
Authors:B P Roy  A Y Ng
Affiliation:Department of Clinical Chemistry, University of Gothenburg Sahlgren''s Hospital, S-413 45 Gothenburg, Sweden
Abstract:In the presence of D=-carnitine significant decarboxylation of 2-oxoglutarate occurs with γ-butyrobetaine hydroxylase (EC 1.14.11.1) both from Pseudomonas sp AK 1 and from human kidney. No product was formed from carnitine when D=L=-carnitine was incubated with either enzyme but succinate was formed in 1:1 stoichiometry to decarboxylation using D=-carnitine and the human enzyme. L=-Carnitine is also an uncoupler for the human enzyme. There is no significant decarboxylation of 2-oxoglutarate in the absence of a substrate, but during normal catalysis in the presence of γ-butyrobetaine the formation of CO2 from 2-oxoglutarate exceeds carnitine formation with 20% for the human enzyme.
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