Linked Life Data

20374941

Source:http://linkedlifedata.com/resource/pubmed/id/20374941

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2010-4-8
pubmed:abstractText
BLAT (BLAST-Like Alignment Tool) analyses of the opossum (Monodelphis domestica) and zebrafish (Danio rerio) genomes were undertaken using amino acid sequences of the acylglycerol acyltransferase (AGAT) superfamily. Evidence is reported for 8 opossum monoacylglycerol acyltransferase-like (MGAT) (E.C. 2.3.1.22) and diacylglycerol acyltransferase-like (DGAT) (E.C. 2.3.1.20) genes and proteins, including DGAT1, DGAT2, DGAT2L6 (DGAT2-like protein 6), AWAT1 (acyl CoA wax alcohol acyltransferase 1), AWAT2, MGAT1, MGAT2 and MGAT3. Three of these genes (AWAT1, AWAT2 and DGAT2L6) are closely localized on the opossum X chromosome. Evidence is also reported for six zebrafish MGAT- and DGAT-like genes, including two DGAT1-like genes, as well as DGAT2-, MGAT1-, MGAT2- and MGAT3-like genes and proteins. Predicted primary, secondary and transmembrane structures for the opossum and zebrafish MGAT-, AWAT- and DGAT-like subunits and the intron-exon boundaries for genes encoding these enzymes showed a high degree of similarity with other members of the AGAT superfamily, which play major roles in triacylglyceride (DGAT), diacylglyceride (MGAT) and wax ester (AWAT) biosynthesis. Alignments of predicted opossum, zebrafish and other vertebrate DGAT1, DGAT2, other DGAT2-like and MGAT-like amino acid sequences with known human and mouse enzymes demonstrated conservation of residues which are likely to play key roles in catalysis, lipid binding or in maintaining structure. Phylogeny studies of the human, mouse, opossum, zebrafish and pufferfish MGAT- and DGAT-like enzymes indicated that the common ancestors for these genes predated the appearance of bony fish during vertebrate evolution whereas the AWAT- and DGAT2L6-like genes may have appeared more recently prior to the appearance of marsupial and eutherian mammals.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
1878-0407
pubmed:author
pubmed:copyrightInfo
Copyright 2009 Elsevier Inc. All rights reserved.
pubmed:issnType
Electronic
pubmed:volume
5
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
45-54
pubmed:meshHeading
pubmed-meshheading:20374941-Acyltransferases, pubmed-meshheading:20374941-Amino Acid Sequence, pubmed-meshheading:20374941-Animals, pubmed-meshheading:20374941-Diacylglycerol O-Acyltransferase, pubmed-meshheading:20374941-Exons, pubmed-meshheading:20374941-Genetic Variation, pubmed-meshheading:20374941-Humans, pubmed-meshheading:20374941-Isoenzymes, pubmed-meshheading:20374941-Mice, pubmed-meshheading:20374941-Molecular Sequence Data, pubmed-meshheading:20374941-Opossums, pubmed-meshheading:20374941-Phylogeny, pubmed-meshheading:20374941-Protein Structure, Secondary, pubmed-meshheading:20374941-Protein Subunits, pubmed-meshheading:20374941-Proteomics, pubmed-meshheading:20374941-RNA, Messenger, pubmed-meshheading:20374941-Sequence Alignment, pubmed-meshheading:20374941-Vertebrates, pubmed-meshheading:20374941-Zebrafish
pubmed:year
2010
pubmed:articleTitle
Comparative genomics and proteomics of vertebrate diacylglycerol acyltransferase (DGAT), acyl CoA wax alcohol acyltransferase (AWAT) and monoacylglycerol acyltransferase (MGAT).
pubmed:affiliation
School of Biomolecular and Physical Sciences, Griffith University, Nathan 4111 Brisbane, Queensland, Australia. r.holmes@griffith.edu.au
pubmed:publicationType
Journal Article, Comparative Study