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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
1995-3-9
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pubmed:databankReference |
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pubmed:abstractText |
Holocarboxylase synthetase (HCS) plays an essential role in biotin utilization in eukaryotic cells and its deficiency causes biotin-responsive multiple carboxylase deficiency in humans. We have cloned the human HCS cDNA and show that antiserum against the recombinant protein immunoprecipitates human HCS. A one base deletion resulting in a premature termination and a missense mutation (Leu to Pro) were found in cells from siblings with HCS deficiency. Human HCS shows homology to BirA, which acts as both a biotin-[acetyl-CoA-carboxylase] ligase and a biotin repressor in E. coli, suggesting a functional relationship between the two proteins. The human HCS gene maps to chromosome 21q22.1.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Biotin,
http://linkedlifedata.com/resource/pubmed/chemical/Carbon-Nitrogen Ligases,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ligases,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/birA protein, E coli,
http://linkedlifedata.com/resource/pubmed/chemical/holocarboxylase synthetases
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
1061-4036
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
8
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pubmed:geneSymbol |
birA
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
122-8
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:7842009-Amino Acid Sequence,
pubmed-meshheading:7842009-Animals,
pubmed-meshheading:7842009-Bacterial Proteins,
pubmed-meshheading:7842009-Base Sequence,
pubmed-meshheading:7842009-Biotin,
pubmed-meshheading:7842009-Carbon-Nitrogen Ligases,
pubmed-meshheading:7842009-Cattle,
pubmed-meshheading:7842009-Chromosome Mapping,
pubmed-meshheading:7842009-Chromosomes, Human, Pair 21,
pubmed-meshheading:7842009-Cloning, Molecular,
pubmed-meshheading:7842009-DNA, Complementary,
pubmed-meshheading:7842009-DNA Mutational Analysis,
pubmed-meshheading:7842009-Escherichia coli,
pubmed-meshheading:7842009-Escherichia coli Proteins,
pubmed-meshheading:7842009-Female,
pubmed-meshheading:7842009-Genes,
pubmed-meshheading:7842009-Humans,
pubmed-meshheading:7842009-Ligases,
pubmed-meshheading:7842009-Molecular Sequence Data,
pubmed-meshheading:7842009-Point Mutation,
pubmed-meshheading:7842009-Recombinant Fusion Proteins,
pubmed-meshheading:7842009-Repressor Proteins,
pubmed-meshheading:7842009-Sequence Alignment,
pubmed-meshheading:7842009-Sequence Deletion,
pubmed-meshheading:7842009-Sequence Homology, Amino Acid,
pubmed-meshheading:7842009-Transcription Factors
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pubmed:year |
1994
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pubmed:articleTitle |
Isolation and characterization of mutations in the human holocarboxylase synthetase cDNA.
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pubmed:affiliation |
Department of Biomedical Genetics, Tohoku University School of Medicine, Sendai, Japan.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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