Evidence map›Paper›PMID 17696876›Full record

ArticleThe Biochemical journal2007

Molecular characterization of the thi3 gene involved in thiamine biosynthesis in Zea mays: cDNA sequence and enzymatic and structural properties of the recombinant bifunctional protein with 4-amino-5-hydroxymethyl-2-methylpyrimidine (phosphate) kinase and thiamine monophosphate synthase activities.

Maria Rapala-Kozik, Mariusz Olczak, Katarzyna Ostrowska, Agata Starosta, Andrzej Kozik

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Article in The Biochemical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
0.9field-weighted citation impact, top 25% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

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

14 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
  2. The importance of thiamine (vitamin BThe Journal of biological chemistry · 2020
    Review
  3. Review
  4. Frontiers in plant science · 2019
    Article
  5. Article
  6. Article
  7. Article
  8. Article
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  14. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 1 country.

Maria Rapala-KozikFaculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Gronostajowa 7, 30-387 Kraków, Poland. rapala@mol.uj.edu.pl
Mariusz Olczak
Katarzyna Ostrowska
Agata Starosta
Andrzej Kozik
Jagiellonian University · PLUniversity of Wrocław · PL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A thiamine biosynthesis gene, thi3, from maize Zea mays has been identified through cloning and sequencing of cDNA and heterologous overexpression of the encoded protein, THI3, in Escherichia coli. The recombinant THI3 protein was purified to homogeneity and shown to possess two essentially different enzymatic activities of HMP(-P) [4-amino-5-hydroxymethyl-2-methylpyrimidine (phosphate)] kinase and TMP (thiamine monophosphate) synthase. Both activities were characterized in terms of basic kinetic constants, with interesting findings that TMP synthase is uncompetitively inhibited by excess of one of the substrates [HMP-PP (HMP diphosphate)] and ATP. A bioinformatic analysis of the THI3 sequence suggested that these activities were located in two distinct, N-terminal kinase and C-terminal synthase, domains. Models of the overall folds of THI3 domains and the arrangements of active centre residues were obtained with the SWISS-MODEL protein modelling server, on the basis of the known three-dimensional structures of Salmonella enterica serotype Typhimurium HMP(-P) kinase and Bacillus subtilis TMP synthase. The essential roles of Gln98 and Met134 residues for HMP kinase activity and of Ser444 for TMP synthase activity were experimentally confirmed by site-directed mutagenesis.

Indexed as

Alkyl and Aryl TransferasesAmino Acid SequenceDNA, ComplementaryEscherichia coliMolecular Sequence DataMultienzyme ComplexesPhosphotransferases (Phosphate Group Acceptor)Plant ProteinsPyrimidinesRecombinant ProteinsThiamineZea mays4-amino-5-hydroxymethyl-2-methylpyrimidine4-amino-5-(hydroxymethyl)-2-methylpyrimidine phosphate kinaseAlkyl and Aryl TransferasesDNA, ComplementaryMultienzyme ComplexesPhosphotransferases (Phosphate Group Acceptor)Plant ProteinsPyrimidinesRecombinant ProteinsThiaminethiamin phosphate synthase

Identifiers

PMID17696876
PMCPMC2267346
OpenAlexW2025701228

What OpenQuestion holds

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Registered trials

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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.