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Inhibition of dihydrofolate synthetase by folate, homofolate, pteroate and homopteroate and their reduced forms.

Authors
  • Webb, S R
  • Ferone, R
Type
Published Article
Journal
Biochimica et Biophysica Acta
Publisher
Elsevier
Publication Date
Feb 13, 1976
Volume
422
Issue
2
Pages
419–426
Identifiers
PMID: 764876
Source
Medline
License
Unknown

Abstract

Dihydrofolate (H2-folate) synthetase (EC 6.3.2.12) was isolated from Escherichia coli B. A radiochemical assay was developed to determine the activity of H2-folate synthetase in order to study the effects of folate metabolites and antimetabolites which would interfere with the microbiological assay method previously used. The effects of folate and pteroate derivatives on the activity of this enzyme were investigated to determine if inhibition of this enzyme could constitute a site of action for these compounds as chemotherapeutic agents or a site of metabolic regulation. H2-folate synthetase was inhibited by its product, H2-folate, and by the antimetabolite dihydrohomopteroate, with apparent Ki values of 23.4 and 9.2 muM, respectively.

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