Linked Life Data

1527093

Source:http://linkedlifedata.com/resource/pubmed/id/1527093

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
27
pubmed:dateCreated
1992-10-22
pubmed:databankReference
pubmed:abstractText
Three overlapping cDNA clones encoding methylmalonate-semialdehyde dehydrogenase (MMSDH; 2-methyl-3-oxopropanoate:NAD+ oxidoreductase (CoA-propanoylating); EC 1.2.1.27) have been isolated by screening a rat liver lambda gt 11 library with nondegenerate oligonucleotide probes synthesized according to polymerase chain reaction-amplified portions coding for the N-terminal amino acid sequence of rat liver MMSDH. The three clones cover a total of 1942 base pairs of cDNA, with an open reading frame of 1569 base pairs. The authenticity of the composite cDNA was confirmed by a perfect match of 43 amino acids known from protein sequencing. The composite cDNA predicts a 503 amino acid mature protein with M(r) = 55,330, consistent with previous estimates. Polymerase chain reaction was used to obtain the sequence of the 32 amino acids corresponding to the mitochondrial entry peptide. Northern blot analysis of total RNA from several rat tissues showed a single mRNA band of 3.8 kilobases. Relative mRNA levels were: kidney greater than liver greater than heart greater than muscle greater than brain, which differed somewhat from relative MMSDH protein levels determined by Western blot analysis: liver = kidney greater than heart greater than muscle greater than brain. A 1423-base pair cDNA clone encoding human MMSDH was isolated from a human liver lambda gt 11 library. The human MMSDH cDNA contains an open reading frame of 1293 base pairs that encodes the protein from Leu-74 to the C terminus. Human and rat MMSDH share 89.6 and 97.7% identity in nucleotide and protein sequence, respectively. MMSDH clearly belongs to a superfamily of aldehyde dehydrogenases and is closely related to betaine aldehyde dehydrogenase, 2-hydroxymuconic semialdehyde dehydrogenase, and class 1 and 2 aldehyde dehydrogenases.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
267
pubmed:geneSymbol
MMSDH
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
19724-9
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:1527093-Aldehyde Oxidoreductases, pubmed-meshheading:1527093-Amino Acid Sequence, pubmed-meshheading:1527093-Animals, pubmed-meshheading:1527093-Base Sequence, pubmed-meshheading:1527093-Blotting, Western, pubmed-meshheading:1527093-Cloning, Molecular, pubmed-meshheading:1527093-DNA, pubmed-meshheading:1527093-Gene Expression, pubmed-meshheading:1527093-Humans, pubmed-meshheading:1527093-Liver, pubmed-meshheading:1527093-Methylmalonate-Semialdehyde Dehydrogenase (Acylating), pubmed-meshheading:1527093-Molecular Sequence Data, pubmed-meshheading:1527093-Oligodeoxyribonucleotides, pubmed-meshheading:1527093-Phylogeny, pubmed-meshheading:1527093-Polymerase Chain Reaction, pubmed-meshheading:1527093-RNA, Messenger, pubmed-meshheading:1527093-Rats, pubmed-meshheading:1527093-Sequence Alignment, pubmed-meshheading:1527093-Tissue Distribution
pubmed:year
1992
pubmed:articleTitle
CoA-dependent methylmalonate-semialdehyde dehydrogenase, a unique member of the aldehyde dehydrogenase superfamily. cDNA cloning, evolutionary relationships, and tissue distribution.
pubmed:affiliation
Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis 46202-5122.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't