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Aminohydrolases acting on adenine, adenosine and their derivatives
H. Pospisilova, I. Frebort
Jazyk angličtina Země Česko
Typ dokumentu časopisecké články, práce podpořená grantem, přehledy
NLK
Directory of Open Access Journals
od 2001
Free Medical Journals
od 1998
Medline Complete (EBSCOhost)
od 2007-06-01
ROAD: Directory of Open Access Scholarly Resources
od 2001
PubMed
17690732
DOI
10.5507/bp.2007.001
Knihovny.cz E-zdroje
- MeSH
- adenosindeaminasa chemie genetika MeSH
- aminohydrolasy chemie genetika MeSH
- aminokyseliny analýza MeSH
- Bacteria enzymologie MeSH
- lidé MeSH
- zvířata MeSH
- Check Tag
- lidé MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- přehledy MeSH
BACKGROUND: Adenine and adenosine-acting aminohydrolases are important groups of enzymes responsible for the metabolic salvage of purine compounds. Several subclasses of these enzymes have been described and given current knowledge of the full genome sequences of many organisms, it is possible to identify genes encoding these enzymes and group them according to their primary structure. METHODS AND RESULTS: This article is a short overview of the enzymes classified as adenine and adenosine deaminase. It summarises knowledge of their occurrence, genetic basis and their catalytic and structural properties. CONCLUSIONS: These enzymes are constitutive components of purine metabolism and their impairment may cause serious medical disorders. In humans, adenosine deaminase deficiency is linked to severe combined immunodeficiency and as such the enzyme has been approved for the first gene therapy trial. The role of these enzymes in plants is unclear, since the activity was has not been detected in extracts and putative genes have not been yet cloned and analyzed. A literature search and amino acid identity comparison show that Ascomycetes contain only adenine deaminase, but not adenosine deaminase, despite the fact that corresponding genes are annotated in databases as the adenosine cleaving enzymes because they share the same conserved domain.
Citace poskytuje Crossref.org
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