Linked Life Data

8530107

Source:http://linkedlifedata.com/resource/pubmed/id/8530107

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1996-2-1
pubmed:databankReference
pubmed:abstractText
Histidase (EC 4.3.1.3) is a cytosolic enzyme that catalyzes the nonoxidative deamination of histidine to urocanic acid. Histidinemia, resulting from reduced histidase activity as reported in Cambridge stock his/his mice and in humans, is the most frequent inborn metabolic error in Japan. The histidase chromosomal gene (HAL) was isolated from a lambda EMBL-3 human genomic library using the human histidase cDNA as a probe. Restriction mapping and Southern blot analysis of the isolated clones reveal a single-copy gene spanning approximately 25 kb and consisting of 21 exons. Exon 1 encodes only 5' untranslated sequence of liver histidase mRNA, with protein coding beginning in exon 2. A rarely observed 5' GC, similar to that reported in the human P-450 (SCC) gene, is present in intron 20. All other splicing junctions adhere to the canonical GT/AG rule. A TATA box sequence is located 25 bp upstream of the liver histidase transcription initiation site determined by S1 nuclease protection analysis. Several liver- and epidermis-specific transcription factor binding sites, including C/EBP, NFIL6, HNF5, AP2/KER1, MNF, and others, are also identified in the 5' flanking region. Consistent with the hepatic and epidermal expression of histidase, this finding suggests that histidase transcription may be regulated by these factors. We further identify a polymorphism (A to G transition) in the histidase coding region of exon 16. The human histidase genomic structure presented here should facilitate the molecular investigation of symptomatic and asymptomatic forms of histidinemia.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0888-7543
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
29
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
98-104
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:8530107-Alternative Splicing, pubmed-meshheading:8530107-Amino Acid Metabolism, Inborn Errors, pubmed-meshheading:8530107-Animals, pubmed-meshheading:8530107-Base Sequence, pubmed-meshheading:8530107-Binding Sites, pubmed-meshheading:8530107-Cholesterol Side-Chain Cleavage Enzyme, pubmed-meshheading:8530107-Cloning, Molecular, pubmed-meshheading:8530107-DNA, pubmed-meshheading:8530107-DNA Primers, pubmed-meshheading:8530107-Exons, pubmed-meshheading:8530107-Genomic Library, pubmed-meshheading:8530107-Histidine, pubmed-meshheading:8530107-Histidine Ammonia-Lyase, pubmed-meshheading:8530107-Hominidae, pubmed-meshheading:8530107-Humans, pubmed-meshheading:8530107-Introns, pubmed-meshheading:8530107-Liver, pubmed-meshheading:8530107-Mice, pubmed-meshheading:8530107-Molecular Sequence Data, pubmed-meshheading:8530107-Polymerase Chain Reaction, pubmed-meshheading:8530107-Polymorphism, Genetic, pubmed-meshheading:8530107-RNA, Messenger, pubmed-meshheading:8530107-Restriction Mapping, pubmed-meshheading:8530107-Skin, pubmed-meshheading:8530107-TATA Box, pubmed-meshheading:8530107-Transcription Factors
pubmed:year
1995
pubmed:articleTitle
Molecular cloning and structural characterization of the human histidase gene (HAL).
pubmed:affiliation
Department of Pediatrics, Nagoya City University Medical School, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't