Further studies on anthranilate N-acetyltransferase and the metabolism of N-acetylanthranilic acid in Aerobacter aerogenes |
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Authors: | RC Paul C Ratledge |
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Institution: | Department of Biochemistry, The University of Hull, Hull, Yorkshire, HU6 7RX, Great Britain |
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Abstract: | Antranilate N-acetlytransferase, which is a constitutive enzyme, is responsible for the formation of N-acetylanthranilic acid which accumulated int he culture medium of certain mutants of Aerobacter aerogenes. It has been shown to be dissimilar to serine O-acetyltrasferase and not to be involved in the acetylation of a variety of aliphatic compounds. Aniline and m-aminobenzoic acid are, however, readily acetylated, the Km for the latter compound being the same as that for anthranilic acid, 13 mM. p-Aminobenzoic acid is only slowly acetylated and salicylic acid only acted as an inhibitor of the reaction. acid was prepared but could not be shown to be deacylated for further metabolized when administered to any whole cell, cell extract or toluene-lysed cell preparation. |
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