Assembly of 7,8-dihydrofolic acid in de novo folate biosynthesizing microorganisms. Intermediary enzymes as partial heterologous protein associates of the 5,6,7,8-tetrahydrofolate multienzyme complex

B. L. Toth-Martinez, F. J. Hernádi, Z. Dinya

Research output: Contribution to journalArticle

Abstract

7,8-dihydro-6-hydroxymethyl pteridine:ATP pyrophosphokinase, 7,8-dihydropteroate synthetase, 7,8-dihydrofolate synthetase have been isolated from E. coli B by mild conditioms. Presence of functionally different variants of each enzyme was observed. A protein fraction exhibiting p-aminobenzoylglutamate synthetase activity was also purified. The use of guanidine. HCl and EDTA in the final step of isolation allowed separation of specific and stoichiometric substrate-binding proteins of the above enzymes from contaminations of protein nature. From their respective subunits the individual enzymes were reconstituted and partially characterized. Although the origine of subunit structuralization is not known exactly it is assumed to be a native property of theses enzymes which are considered as dynamically regulable structures in microorganisms capable of biosynthesizing 5,6,7,8-tetrahydro folate de novo.

Original languageEnglish
Pages (from-to)391-430
Number of pages40
JournalPharmacological Research Communications
Volume10
Issue number5
DOIs
Publication statusPublished - 1978

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Multienzyme Complexes
Folic Acid
dihydrofolate synthetase
Enzymes
Diphosphotransferases
Proteins
Dihydropteroate Synthase
Pteridines
Guanidine
Ligases
Edetic Acid
Carrier Proteins
Adenosine Triphosphate
Escherichia coli
dihydrofolate
5,6,7,8-tetrahydrofolic acid

ASJC Scopus subject areas

  • Pharmacology

Cite this

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title = "Assembly of 7,8-dihydrofolic acid in de novo folate biosynthesizing microorganisms. Intermediary enzymes as partial heterologous protein associates of the 5,6,7,8-tetrahydrofolate multienzyme complex",
abstract = "7,8-dihydro-6-hydroxymethyl pteridine:ATP pyrophosphokinase, 7,8-dihydropteroate synthetase, 7,8-dihydrofolate synthetase have been isolated from E. coli B by mild conditioms. Presence of functionally different variants of each enzyme was observed. A protein fraction exhibiting p-aminobenzoylglutamate synthetase activity was also purified. The use of guanidine. HCl and EDTA in the final step of isolation allowed separation of specific and stoichiometric substrate-binding proteins of the above enzymes from contaminations of protein nature. From their respective subunits the individual enzymes were reconstituted and partially characterized. Although the origine of subunit structuralization is not known exactly it is assumed to be a native property of theses enzymes which are considered as dynamically regulable structures in microorganisms capable of biosynthesizing 5,6,7,8-tetrahydro folate de novo.",
author = "Toth-Martinez, {B. L.} and Hern{\'a}di, {F. J.} and Z. Dinya",
year = "1978",
doi = "10.1016/S0031-6989(78)80033-2",
language = "English",
volume = "10",
pages = "391--430",
journal = "Pharmacological Research",
issn = "1043-6618",
publisher = "Academic Press Inc.",
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AU - Toth-Martinez, B. L.

AU - Hernádi, F. J.

AU - Dinya, Z.

PY - 1978

Y1 - 1978

N2 - 7,8-dihydro-6-hydroxymethyl pteridine:ATP pyrophosphokinase, 7,8-dihydropteroate synthetase, 7,8-dihydrofolate synthetase have been isolated from E. coli B by mild conditioms. Presence of functionally different variants of each enzyme was observed. A protein fraction exhibiting p-aminobenzoylglutamate synthetase activity was also purified. The use of guanidine. HCl and EDTA in the final step of isolation allowed separation of specific and stoichiometric substrate-binding proteins of the above enzymes from contaminations of protein nature. From their respective subunits the individual enzymes were reconstituted and partially characterized. Although the origine of subunit structuralization is not known exactly it is assumed to be a native property of theses enzymes which are considered as dynamically regulable structures in microorganisms capable of biosynthesizing 5,6,7,8-tetrahydro folate de novo.

AB - 7,8-dihydro-6-hydroxymethyl pteridine:ATP pyrophosphokinase, 7,8-dihydropteroate synthetase, 7,8-dihydrofolate synthetase have been isolated from E. coli B by mild conditioms. Presence of functionally different variants of each enzyme was observed. A protein fraction exhibiting p-aminobenzoylglutamate synthetase activity was also purified. The use of guanidine. HCl and EDTA in the final step of isolation allowed separation of specific and stoichiometric substrate-binding proteins of the above enzymes from contaminations of protein nature. From their respective subunits the individual enzymes were reconstituted and partially characterized. Although the origine of subunit structuralization is not known exactly it is assumed to be a native property of theses enzymes which are considered as dynamically regulable structures in microorganisms capable of biosynthesizing 5,6,7,8-tetrahydro folate de novo.

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