The Metabolism of Xanthine-8-carboxylic Acid by Alcaligenes Faecalis.
نویسندگان
چکیده
Alcaligenes jaecalis is capable of growing in response to simple pteridines as the sole source of nitrogen (1). Simple pteridines appear to be metabolized in this organism through the common intermediate, tetraoxypteridine (1, 2)) and cell-free extracts of the organism catalyze the conversion of tetraoxypteridine to xanthine-8-carboxylic acid (1). In these conversions the nitrogen atoms of the rings have not been utilized; yet the nitrogen atoms of the pteridine ring system are used as effectively as the nitrogen atoms of ammonium nitrate (1). It is of interest, therefore, to investigate the further metabolism of xanthine-8 carboxylic acid. Evidence is presented in this article to show that xanthine-8carboxylic acid may be converted enzymatically to xanthine and that the latter in the presence of 5-phosphoribosyl l-pyrophosphate may be converted to xanthosine 5’-phosphate. The nucleotide has been characterized by means of paper chromatography, paper electrophoresis, and its ultraviolet absorption spect,rum. Also, xanthosine 5’-phosphate trapped the product formed enzymatically from 2.r4C-xanthine-8carboxylic acid and 5-phosphoribosyl 1-pyrophosphate. The decarboxylase which catalyzes the conversion of xanthine8-carboxylic acid to xanthine is an inducible enzyme, whereas the nucleotide pyrophosphorylase which catalyzes the formation of xanthosine 5’-phosphate from xanthine and 5-phosphoribosyl 1-pyrophosphate is constitutive. A pathway thus exists in A. jaecalis for the conversion of pteridines to conventional purine intermediates. Further work is still required to elucidate the mechanism by which the nitrogen atoms of the ring are utilized by this organism.
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عنوان ژورنال:
- The Journal of biological chemistry
دوره 239 شماره
صفحات -
تاریخ انتشار 1964