Evidence map›Paper›PMID 9118956›Full record

ArticleThe EMBO journal1997

Folate biosynthesis in higher plants: purification and molecular cloning of a bifunctional 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase/7,8-dihydropteroate synthase localized in mitochondria.

F Rébeillé, D Macherel, J M Mouillon, J Garin, R Douce

Abstract read
In one paragraph

Article in The EMBO journal, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

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Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

41 citing papers in PubMed.

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4 · The record

Corrections and comments

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5 · Who and what money

Authors and funding

5 authors.

F RébeilléLaboratoire de Physiologie Cellulaire Végétale, CNRS URA no. 576, Département de Biologie Moléculaire et Structurale, CEA-Grenoble, France.
D Macherel
J M Mouillon
J Garin
R Douce

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In pea leaves, the synthesis of 7,8-dihydropteroate, a primary step in folate synthesis, was only detected in mitochondria. This reaction is catalyzed by a bifunctional 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase/7,8-dihydropteroate synthase enzyme, which represented 0.04-0.06% of the matrix proteins. The enzyme had a native mol. wt of 280-300 kDa and was made up of identical subunits of 53 kDa. The reaction catalyzed by the 7,8-dihydropteroate synthase domain of the protein was Mg2+-dependent and behaved like a random bireactant system. The related cDNA contained an open reading frame of 1545 bp and the deduced amino acid sequence corresponded to a polypeptide of 515 residues with a calculated M(r) of 56,454 Da. Comparison of the deduced amino acid sequence with the N-terminal sequence of the purified protein indicated that the plant enzyme is synthesized with a putative mitochondrial transit peptide of 28 amino acids. The calculated M(r) of the mature protein was 53,450 Da. Southern blot experiments suggested that a single-copy gene codes for the enzyme. This result, together with the facts that the protein is synthesized with a mitochondrial transit peptide and that the activity was only detected in mitochondria, strongly supports the view that mitochondria is the major (unique?) site of 7,8-dihydropteroate synthesis in higher plant cells.

Indexed as

Amino Acid SequenceBase SequenceBlotting, NorthernChromatography, GelCloning, MolecularDihydropteroate SynthaseDiphosphotransferasesDNA PrimersElectrophoresis, Agar GelElectrophoresis, Polyacrylamide GelEnzyme InhibitorsKineticsMitochondriaMolecular Sequence DataMolecular WeightMultienzyme Complexes2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase-7,8-dihydropteroate synthasedihydropteroateDihydropteroate SynthaseDiphosphotransferasesDNA PrimersEnzyme InhibitorsMultienzyme ComplexesPterins

Identifiers

PMID9118956
PMCPMC1169695

What OpenQuestion holds

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.