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- W2047346815 abstract "Using spectrophotometry, it was found that histidine enhances weakly but specifically various metabolic reaction rates such as pyruvate carboxylase, oxalacetate decarboxylase and glucose-6-phosphate isomerase (indicating that only one of the twenty amino acids is catalytic). Oligo-ribonucleotides having flexible dihedral angles could also be expected to be rate enhancers in these metabolic reactions. The survey by spectrophotometry showed that GpUpG, an anticodon of histidine, is also a similar rate enhancer. The formation of the reaction products in the cases of pyruvate carboxylase and oxalacetate decarboxylase was furthermore confirmed by thin-layer chromatography using 14 C-labeled pyruvate and by high-performance liquid chromatography. The origin of the genetic code may thus be based on direct molecular relationships between amino acids and anticodons." @default.
- W2047346815 created "2016-06-24" @default.
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- W2047346815 date "2004-02-15" @default.
- W2047346815 modified "2023-10-14" @default.
- W2047346815 title "Histidine and Its Anticodon GpUpG are Similar Metabolic Reaction Rate Enhancers: Molecular Origin of the Genetic Code" @default.
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- W2047346815 doi "https://doi.org/10.1143/jpsj.73.323" @default.
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