Substrate specificity of glycinamide ribonucleotide transformylase from chicken liver

Vincent D. Antle, Dashan Liu, B. Robert McKellar, Carol A. Caperelli, Mei Hua, Robert Vince

Research output: Contribution to journalArticlepeer-review

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Several glycinamide ribonucleotide analogs have been prepared and evaluated as substrates and/or inhibitors of glycinamide ribonucleotide transformylase from chicken liver. The side chain modified analogs, in which the glycine side chain, R = CH2NH2, has been replaced by R = CH2NHCH3 and R = CH2CH2NH2, are substrates, with V/K (relative intensity) of 2.4% and 16.3%, respectively. Several carbocyclic analogs of glycinamide ribonucleotide, including the phosphonate derivative of carbocyclic glycinamide ribonucleotide, did not serve as substrates, but were inhibitors of the enzyme, competitive against glycinamide ribonucleotide, with K(i) values ranging from 7.4 to 23.6 times the K(m) for glycinamide ribonucleotide. However, the O-phosphonate analog of carbocyclic glycinamide ribonucleotide did support enzymatic activity, with V/K (relative intensity) of 0.8%. In addition, glycinamide ribonucleoside was neither a substrate for, nor an inhibitor of, glycinamide ribonucleotide transformylase. Furthermore, α-glycinamide ribonucleotide had no effect on enzyme activity. These studies have begun to define the structural features of the nucleotide substrate required to support enzymatic activity.

Original languageEnglish (US)
Pages (from-to)6045-6049
Number of pages5
JournalJournal of Biological Chemistry
Issue number11
StatePublished - Mar 15 1996

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