Substrate specificity of human glycinamide ribonucleotide transformylase

Vincent D. Antle, Nathaniel Donat, Mei Hua, Pei Ling Liao, Robert Vince, Carol A. Caperelli

Research output: Contribution to journalArticlepeer-review

3 Scopus citations


The nucleotide substrate specificity of human glycinamide ribonucleotide transformylase, a chemotherapeutic target, has been examined. The enzyme accepts the sarcosyl analog of glycinamide ribonucleotide, carbocyclic glycinamide ribonucleotide, and two phosphonate derivatives of carbocyclic glycinamide ribonucleotide with V/K values, relative to that obtained for β- glycinamide ribonucleotide, of 1, 27, 1.4, and 2.9%, respectively. Several other analogs of carbocyclic glycinamide ribonucleotide, namely a truncated phosphonate and 2',3'-dideoxy- and 2',3'-dideoxy-2',3'-didehydro-carbocyclic glycinamide ribonucleotide, were inhibitors of the enzyme, competitive against glycinamide ribonucleotide, with K(i) values approximately 100 times higher than the K(m) for β-glycinamide ribonucleotide. Although the results of the present study parallel those obtained previously with the avian enzyme (V. D. Antle, D. Liu, B. R. McKellar, C. A. Caperelli, M. Hua, and R. Vince (1996) J. Biol. Chem. 271, 6045-6049), quantitative differences between the two enzyme species have been uncovered.

Original languageEnglish (US)
Pages (from-to)231-235
Number of pages5
JournalArchives of Biochemistry and Biophysics
Issue number2
StatePublished - Oct 15 1999

Bibliographical note

Funding Information:
1 This research was supported by NIH Grants GM42663 to C.A.C. and CA23263 to R.V. 2Current address: MDS Panlabs, Bothell, WA. 3Current address: Procter & Gamble Co., Cincinnati, OH. 4Current address: M. D. Anderson, Houston, TX. 5To whom correspondence should be addressed. Fax (513) 558-0978. E-mail:


  • Human folate enzyme
  • Purine biosynthesis


Dive into the research topics of 'Substrate specificity of human glycinamide ribonucleotide transformylase'. Together they form a unique fingerprint.

Cite this