The Enzymatic Synthesis of 5-Ribosyluridylic Acid
Year: 1963
Type: article
Abstract: Preliminary experiments have shown that picolinic carboxylase activity (3) appears to be inversely related to niacin ribonucleotide synthesis, as judged by the PP-ribose-P-dependent evolution of Cl402 in cat and rat liver.The activity leading to niacin ribonucleotide synthesis in cat liver was shown to be one-fifth of that in rat liver, but picolinic carboxylase was 20-to 50-fold greater in the former than in the latter.This evidence is consistent with the previous observation that niacin cannot be replaced by tryptophan in the cat ( 14), since picolinic carboxylase initiates the degradative reaction sequence from 2-acroleyl-3-aminofumarate to glutarate (4), and removes the former compound from consideration as the substrate for the niacin ribonucleotide synthesis.Further studies are now in progress in order to elucidate the detailed properties of the enzymes concerned as well as the regulatory mechanism of this vitamin synthesis.
Source: Journal of Biological Chemistry
Authors: Robert L. Heinrikson, Eugene Goldwasser
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: hybrid
Estimated APC paid: $3,430
OpenAlex ID: W45833831
