Structure at 2.9-A resolution of aspartate carbamoyltransferase complexed with the bisubstrate analogue N-(phosphonacetyl)-L-aspartate.
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چکیده
منابع مشابه
Long-term association of N-(phosphonacetyl)-L-aspartate with bone.
By means of enzymatic and autoradiographic techniques, it has been demonstrated that, 24 hr after a single dose of the antitumor amino acid N-phosphonacetyl-L-aspartic acid (PALA), (400 mg/kg i.p.; 1.15 mmol/kg) to C57BL x DBA/2 F1 mice, the agent accumulates in bone to a concentration of approximately 400 microM; this is 3000 times greater than the Ki of PALA for its target enzyme, aspartate c...
متن کاملSerum uridine levels in patients receiving N-(phosphonacetyl)-L-aspartate.
Serum uridine levels of N-(phosphonacetyl)-L-aspartate-treated patients from Phase 1 and continuing trials receiving 1000 to 2000 mg/sq m/day were measured by reverse-phase high-pressure liquid chromatography. For the five patients studied, the predose serum levels ranged from 2.6 to 64. microM, well within the normal range of 1.9 to 8.9 microM. All serum uridine levels decreased in the first 2...
متن کاملCooperative binding of the bisubstrate analog N-(phosphonacetyl)-L-aspartate to aspartate transcarbamoylase and the heterotropic effects of ATP and CTP.
Most investigations of the allosteric properties of the regulatory enzyme aspartate transcarbamoylase (ATCase) from Escherichia coli are based on the sigmoidal dependence of enzyme activity on substrate concentration and the effects of the inhibitor, CTP, and the activator, ATP, on the saturation curves. Interpretations of these effects in terms of molecular models are complicated by the inabil...
متن کاملAspartate carbamoyltransferase from rat liver.
1. Aspartate-carbamoyltransferase activity was concentrated from rat-liver preparations. Only l-aspartate, beta-benzyl-l-aspartate and beta-erythro-hydroxy-dl-aspartate were carbamoylated enzymically. The K(m) for l-aspartate and carbamoyl phosphate have been determined by three methods: colorimetric procedure, radioactive assay with [(14)C]aspartate and an assay with [(14)C]carbamoyl phosphate...
متن کاملSelective inhibition of pyrimidine synthesis and depletion of nucleotide pools by N-(phosphonacetyl)-L-aspartate.
poration of these compounds into pyrimidines is inefficient (27). Evidence concerning the degree of inhibition of aspartate transcarbamylase produced in animals by PALA treatment was obtained by Yoshida et ai. (27), who found that the specific activity of aspartate transcarbamylase in extracts of spleens from animals treated with PALA was only 20% of that found in control mouse spleen. The resi...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 1985
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.82.6.1643