Evidence map›Paper›PMID 12487625›Full record

ArticleThe Biochemical journal2003

Active-site-mutagenesis study of rat liver betaine-homocysteine S-methyltransferase.

Beatriz González, Nuria Campillo, Francisco Garrido, María Gasset, Juliana Sanz-Aparicio, María A Pajares

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.8field-weighted citation impact, top 17% 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

10 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
  2. Article
  3. Betaine-homocysteineFASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019
    Article
  4. Article
  5. Article
  6. Folic acid deficiency induces premature hearing loss through mechanisms involving cochlear oxidative stress and impairment of homocysteine metabolism.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2015
    Article
  7. Article
  8. Article
  9. Article
  10. Article
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

6 authors at 3 institutions in 1 country.

Beatriz GonzálezInstituto de Química-Física Rocasolano (CSIC), Serrano 119, 28006 Madrid, Spain.
Nuria Campillo
Francisco Garrido
María Gasset
Juliana Sanz-Aparicio
María A Pajares
Instituto de Química Física Blas Cabrera · ESInstituto de Investigaciones Biomédicas Sols-Morreale · ESInstituto de Química Médica · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A site-directed-mutagenesis study of putative active-site residues in rat liver betaine-homocysteine S-methyltransferase has been carried out. Identification of these amino acids was based on data derived from a structural model of the enzyme. No alterations in the CD spectra or the gel-filtration chromatography elution pattern were observed with the mutants, thus suggesting no modification in the secondary structure content or in the association state of the proteins. All the mutants obtained showed a reduction of the enzyme activity, the most dramatic effect being that of Glu(159), followed by Tyr(77) and Asp(26). Changes in affinity for either of the substrates, homocysteine or betaine, were detected when substitutions were performed of Glu(21), Asp(26), Phe(74) and Cys(186). Interestingly, Asp(26), postulated to be involved in homocysteine binding, has a strong effect on affinity for betaine. The relevance of these results is discussed in the light of very recent structural data obtained for the human enzyme.

Indexed as

Adenosine DeaminaseAmino Acid SequenceAnimalsBetaineBetaine-Homocysteine S-MethyltransferaseBinding SitesCircular DichroismHomocysteineHumansLiverMethyltransferasesMiceModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedProtein Structure, TertiaryAdenosine DeaminaseBetaineBetaine-Homocysteine S-MethyltransferaseBHMT protein, humanBhmt protein, mouseBhmt protein, ratHomocysteineMethyltransferasesRecombinant Fusion Proteins

Identifiers

PMID12487625
PMCPMC1223237
OpenAlexW2021055104

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.