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The mode of condensation of aspartic acid and dihydroxyacetone phosphate in quinolinate synthesis in escherichia coli

1977; Elsevier BV; Volume: 500; Issue: 1 Linguagem: Inglês

10.1016/0304-4165(77)90061-7

1872-8006

Frank D. Wicks, Shigecki Sakakibara, R.K. Gholson, Thomas Allan Scott,

Enzyme Structure and Function

Dihydroxy[3-14C]acetone phosphate was prepared enzymatically from [1-14C]glucose and used as a substrate in a partially purified quinolinate synthetase system prepared from Escherichia coli mutants. Carbon-by-carbon degradation of the resulting [14C]quinolinate showed that 96% of the 14C was located in carbon-4, indicating that carbon-3 of dihydroxyacetone phosphate condenses with carbon-3 of aspartate in quinolinate synthesis in E. coli.