New vistas for P-aminobenzoate participation in the biosynthesis of dihydro folate: A tentative model of the tetrahydro folate multienzyme complex

B. L. Tóth-Martinez, S. Papp, Z. Dinya, F. J. Hernádi

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

Figures 6a and 6b and Table 2 show the united pattern of possible pathways of THFA biosynthesis with the substrates and the enzymes involved. With substrate selection ten different individual enzyme activities can be distinguished, but A2′ is identical with A2, and their apparent molecular weight is 28,000 daltons ±7%, and similarly c1-4 are the same enzymes with an apparent molecular weight of 40,000 daltons ±5% (Tóth-Martinez et al., 1974a). The identity of these enzymes has preliminary been shown, and construction of the THFA-MEC model was partly based on these findings. So, no distinction can be made among functioning MEC-es. The different pathways, mentioned in the introductory part of this paper, can be a product of the separated study of the individual enzymic steps of DHFA (THFA) biosynthesis. By all means it is an important approach to understand the dynamics of the integrated process what we tentatively suggest in this paper for further elucidation.

Original languageEnglish
Pages (from-to)172-182
Number of pages11
JournalBioSystems
Volume7
Issue number1
DOIs
Publication statusPublished - Jul 1975

ASJC Scopus subject areas

  • Statistics and Probability
  • Modelling and Simulation
  • Biochemistry, Genetics and Molecular Biology(all)
  • Applied Mathematics

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