Evidence map›Paper›PMID 18230605›Full record

ArticleThe Journal of biological chemistry2008

Betaine-homocysteine S-methyltransferase-2 is an S-methylmethionine-homocysteine methyltransferase.

Sandra S Szegedi, Carmen C Castro, Markos Koutmos, Timothy A Garrow

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed, 1 pooled it
2.4field-weighted citation impact, top 13% 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

38 citing papers in PubMed, 1 synthesis or guideline pooled it, 83 citations in OpenAlex.

  1. Pooled it
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  15. Cross-comparison of systemic and tissue-specific metabolomes in a mouse model of Leigh syndrome.Metabolomics : Official journal of the Metabolomic Society · 2021
    Article
  16. A bicyclicRSC chemical biology · 2021
    Article
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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

4 authors at 3 institutions in 2 countries.

Sandra S SzegediDepartments of Animal Science and Food Science and Human Nutrition, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA.
Carmen C Castro
Markos Koutmos
Timothy A Garrow
Universidad de Cádiz · ESUniversity of Illinois Urbana-Champaign · USUniversity of Michigan–Ann Arbor · US

Funding

ROLE OF PROTEIN KINASE C IN YEAST GROWTH CONTROLR01GM048533 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI LEVIN, DAVID E. · 1992 to 2025
$7.8M
Nutrient Regulation of BHMT ExpressionR01DK052501 · NIDDK · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI GARROW, TIMOTHY A · 2003 to 2006
$1.3M
NUTRIENT REGULATION OF BHMT EXPRESSIONR29DK052501 · NIDDK · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI GARROW, TIMOTHY A · 1997 to 2003
$310k
NIDDK NIH HHS DK 52501NIGMS NIH HHS GM 48533
6 · The paper itself

Abstract

We demonstrate that purified recombinant human betainehomocysteine methyltransferase-2 (BHMT-2) is a zinc metalloenzyme that uses S-methylmethionine (SMM) as a methyl donor for the methylation of homocysteine. Unlike the highly homologous betaine-homocysteine methyltransferase (BHMT), BHMT-2 cannot use betaine. The K(m) of BHMT-2 for SMM was determined to be 0.94 mm, and it has a turnover number similar to BHMT. Several compounds were tested as inhibitors of recombinant human BHMT and BHMT-2. The SMM-specific methyltransferase activity of BHMT-2 is not inhibited by dimethylglycine and betaine, whereas the former is a potent inhibitor of BHMT. Methionine is a stronger inhibitor of BHMT-2 than BHMT, and S-adenosylmethionine does not inhibit BHMT but is a weak inhibitor of BHMT-2. BHMT can use SMM as a methyl donor with a k(cat)/K(m) that is 5-fold lower than the k(cat)/K(m) for betaine. However, SMM does not inhibit BHMT activity when it is presented to the enzyme at concentrations that are 10-fold greater than the subsaturating amounts of betaine used in the assay. Based on these data, it is our current hypothesis that in vivo most if not all of the SMM-dependent methylation of homocysteine occurs via BHMT-2.

Indexed as

BetaineBetaine-Homocysteine S-MethyltransferaseHomocysteineHomocysteine S-MethyltransferaseHumansMetalloproteinsMethylationRecombinant ProteinsS-AdenosylmethionineSarcosineSubstrate SpecificityVitamin UZincBetaineBetaine-Homocysteine S-MethyltransferaseBHMT2 protein, humanBHMT protein, humanHomocysteineHomocysteine S-MethyltransferaseMetalloproteinsRecombinant ProteinsS-AdenosylmethionineSarcosineVitamin UZinc

Identifiers

PMID18230605
PMCPMC2276374
OpenAlexW1969545266

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.