Linked Life Data

11087663

Source:http://linkedlifedata.com/resource/pubmed/id/11087663

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2001-1-4
pubmed:databankReference
pubmed:abstractText
Anomalies in folate and homocysteine metabolism can result in homocysteinemia and are implicated in disorders ranging from vascular disease to neural tube defects. Two enzymes are known to methylate homocysteine, vitamin B(12)-dependent methionine synthase (MTR) and betaine-homocysteine methyltransferase (BHMT). BHMT uses betaine, an intermediate of choline oxidation, as a methyl donor and is expressed primarily in the liver and kidney. We report the discovery of a novel betaine-homocysteine methyltransferase gene in humans and mice. The human BHMT2 gene is predicted to encode a 363-amino-acid protein (40.3 kDa) that shows 73% amino acid identity to BHMT. The BHMT2 transcript in humans is most abundant in adult liver and kidney and is found at reduced levels in the brain, heart, and skeletal muscle. The mouse Bhmt2 gene shows 69% amino acid identity and 79% similarity to the mouse Bhmt gene and 82% amino acid identity and 87% similarity to the human BHMT2 gene. Bhmt2 is expressed in fetal heart, lung, liver, kidney and eye. The discovery of a third gene with putative homocysteine methyltransferase activity is important for understanding the biochemical balance in using methyltetrahydrofolate and betaine as methyl donors as well as the metabolic flux between folate and choline metabolism in health and disease.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0888-7543
pubmed:author
pubmed:copyrightInfo
Copyright 2000 Academic Press.
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
70
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
66-73
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:11087663-Amino Acid Sequence, pubmed-meshheading:11087663-Amyloid, pubmed-meshheading:11087663-Animals, pubmed-meshheading:11087663-Betaine, pubmed-meshheading:11087663-Betaine-Homocysteine S-Methyltransferase, pubmed-meshheading:11087663-Chromosome Mapping, pubmed-meshheading:11087663-Chromosomes, Human, Pair 5, pubmed-meshheading:11087663-Homocysteine, pubmed-meshheading:11087663-Humans, pubmed-meshheading:11087663-In Situ Hybridization, Fluorescence, pubmed-meshheading:11087663-Methyltransferases, pubmed-meshheading:11087663-Mice, pubmed-meshheading:11087663-Molecular Sequence Data, pubmed-meshheading:11087663-Prions, pubmed-meshheading:11087663-Protein Precursors, pubmed-meshheading:11087663-Sequence Analysis, DNA, pubmed-meshheading:11087663-Sequence Homology, Amino Acid, pubmed-meshheading:11087663-Two-Hybrid System Techniques
pubmed:year
2000
pubmed:articleTitle
Betaine-homocysteine methyltransferase-2: cDNA cloning, gene sequence, physical mapping, and expression of the human and mouse genes.
pubmed:affiliation
Department of Genetics, Case Western Reserve University School of Medicine, Cleveland, Ohio 44106, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't