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 - 1975

Fingerprint

Aminobenzoates
multienzyme complexes
Multienzyme Complexes
Biosynthesis
Folic Acid
folic acid
Enzymes
biosynthesis
enzyme
enzymes
Molecular weight
varespladib methyl
molecular weight
substrate
Pathway
Molecular Weight
Substrate
Enzyme activity
Substrates
Integrated Process

ASJC Scopus subject areas

  • Ecology, Evolution, Behavior and Systematics
  • Biotechnology
  • Drug Discovery

Cite this

New vistas for P-aminobenzoate participation in the biosynthesis of dihydro folate : A tentative model of the tetrahydro folate multienzyme complex. / Tóth-Martinez, B. L.; Papp, S.; Dinya, Z.; Hernádi, F. J.

In: BioSystems, Vol. 7, No. 1, 1975, p. 172-182.

Research output: Contribution to journalArticle

@article{4188c8152f95408192906b22c7835f51,
title = "New vistas for P-aminobenzoate participation in the biosynthesis of dihydro folate: A tentative model of the tetrahydro folate multienzyme complex",
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{\%} (T{\'o}th-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.",
author = "T{\'o}th-Martinez, {B. L.} and S. Papp and Z. Dinya and Hern{\'a}di, {F. J.}",
year = "1975",
doi = "10.1016/0303-2647(75)90055-6",
language = "English",
volume = "7",
pages = "172--182",
journal = "BioSystems",
issn = "0303-2647",
publisher = "Elsevier Ireland Ltd",
number = "1",

}

TY - JOUR

T1 - New vistas for P-aminobenzoate participation in the biosynthesis of dihydro folate

T2 - A tentative model of the tetrahydro folate multienzyme complex

AU - Tóth-Martinez, B. L.

AU - Papp, S.

AU - Dinya, Z.

AU - Hernádi, F. J.

PY - 1975

Y1 - 1975

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=0016527373&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0016527373&partnerID=8YFLogxK

U2 - 10.1016/0303-2647(75)90055-6

DO - 10.1016/0303-2647(75)90055-6

M3 - Article

C2 - 168934

AN - SCOPUS:0016527373

VL - 7

SP - 172

EP - 182

JO - BioSystems

JF - BioSystems

SN - 0303-2647

IS - 1

ER -