Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
39
pubmed:dateCreated
2000-10-27
pubmed:databankReference
pubmed:abstractText
The cDNAs coding for two novel mouse molybdo-flavoproteins, AOH1 and AOH2 (aldehyde oxidase homolog 1 and 2), were isolated. The AOH1 and AOH2 cDNAs code for polypeptides of 1336 amino acids. The two proteins have similar primary structure and show striking amino acid identity with aldehyde oxidase and xanthine oxidoreductase, two other molybdo-flavoenzymes. AOH1 and AOH2 contain consensus sequences for a molybdopterin-binding site and two distinct 2Fe-2S redox centers. In its native conformation, AOH1 has a molecular weight consistent with a homotetrameric structure. Transfection of the AOH1 and AOH2 cDNAs results in the production of proteins with phenanthridine but not hypoxanthine oxidizing activity. Furthermore, the AOH1 protein has benzaldehyde oxidizing activity with electrophoretic characteristics identical to those of a previously identified aldehyde oxidase isoenzyme (Holmes, R. S. (1979) Biochem. Genet. 17, 517-528). The AOH1 transcript is expressed in the hepatocytes of the adult and fetal liver and in spermatogonia. In liver, the AOH1 protein is synthesized in a gender-specific fashion. The expression of AOH2 is limited to keratinized epithelia and the basal layer of the epidermis and hair folliculi. The selective cell and tissue distribution of AOH1 and AOH2 mRNAs is consistent with the localization of the respective protein products.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Aldehyde Oxidase, http://linkedlifedata.com/resource/pubmed/chemical/Aldehyde Oxidoreductases, http://linkedlifedata.com/resource/pubmed/chemical/Coenzymes, http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary, http://linkedlifedata.com/resource/pubmed/chemical/Metalloproteins, http://linkedlifedata.com/resource/pubmed/chemical/Mitochondrial Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Molybdenum, http://linkedlifedata.com/resource/pubmed/chemical/Oxidoreductases, http://linkedlifedata.com/resource/pubmed/chemical/Plant Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Pteridines, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Xanthine Oxidase, http://linkedlifedata.com/resource/pubmed/chemical/alternative oxidase, http://linkedlifedata.com/resource/pubmed/chemical/molybdenum cofactor
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
29
pubmed:volume
275
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
30690-700
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed-meshheading:10893244-Aldehyde Oxidase, pubmed-meshheading:10893244-Aldehyde Oxidoreductases, pubmed-meshheading:10893244-Amino Acid Sequence, pubmed-meshheading:10893244-Animals, pubmed-meshheading:10893244-Base Sequence, pubmed-meshheading:10893244-Binding Sites, pubmed-meshheading:10893244-Cloning, Molecular, pubmed-meshheading:10893244-Coenzymes, pubmed-meshheading:10893244-Consensus Sequence, pubmed-meshheading:10893244-DNA, Complementary, pubmed-meshheading:10893244-Desulfovibrio, pubmed-meshheading:10893244-Evolution, Molecular, pubmed-meshheading:10893244-Female, pubmed-meshheading:10893244-Humans, pubmed-meshheading:10893244-Male, pubmed-meshheading:10893244-Metalloproteins, pubmed-meshheading:10893244-Mice, pubmed-meshheading:10893244-Mitochondrial Proteins, pubmed-meshheading:10893244-Molecular Sequence Data, pubmed-meshheading:10893244-Molybdenum, pubmed-meshheading:10893244-Oxidoreductases, pubmed-meshheading:10893244-Phylogeny, pubmed-meshheading:10893244-Plant Proteins, pubmed-meshheading:10893244-Pteridines, pubmed-meshheading:10893244-Recombinant Proteins, pubmed-meshheading:10893244-Sequence Homology, Amino Acid, pubmed-meshheading:10893244-Sex Characteristics, pubmed-meshheading:10893244-Tissue Distribution, pubmed-meshheading:10893244-Xanthine Oxidase
pubmed:year
2000
pubmed:articleTitle
Cloning of the cDNAs coding for two novel molybdo-flavoproteins showing high similarity with aldehyde oxidase and xanthine oxidoreductase.
pubmed:affiliation
Laboratory of Molecular Biology, Centro Catullo e Daniela Borgomainerio, Istituto di Ricerche Farmacologiche "Mario Negri," via Eritrea, 62, 20157 Milano, Italy.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't