| Biochemical and molecular genetic correlation in adenylosuccinate lyase deficiency. | |
| | |
MedLine Citation:
|
PMID: 15571240 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
|
An homology model of human adenylosuccinate lyase structure shows that P100A substitution distorts the amino acid chain of domain I in the proximity of His-86, which behaves as general acid in the catalysis, and may expose Cys-98 and Cys-99 to oxidising agents. This model is in line with the observation that the defective protein is strongly inhibited by 4-hydroxy-2-nonenal, an hydroxyalkenal that is known to form thio-ether linkage with proteins. |
| | |
Authors:
|
C Salerno; C Crifò |
Publication Detail:
|
Type: Journal Article; Review |
Journal Detail:
|
Title: Nucleosides, nucleotides & nucleic acids Volume: 23 ISSN: 1525-7770 ISO Abbreviation: Nucleosides Nucleotides Nucleic Acids Publication Date: 2004 Oct |
Date Detail:
|
Created Date: 2004-12-01 Completed Date: 2005-02-03 Revised Date: 2005-11-16 |
Medline Journal Info:
|
Nlm Unique ID: 100892832 Medline TA: Nucleosides Nucleotides Nucleic Acids Country: United States |
Other Details:
|
Languages: eng Pagination: 1253-5 Citation Subset: IM |
Affiliation:
|
Department of Gynecology, Perinatology and Child Health, University of Roma La Sapienza, Roma, Italy. |
Export Citation:
|
APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
|
Adenylosuccinate Lyase
/
deficiency*,
genetics* Aldehydes / pharmacology Binding Sites Catalysis Crystallography, X-Ray Cysteine / chemistry Disulfides / chemistry Humans Kinetics Oxidative Stress Protein Structure, Tertiary |
| Chemical | |
Reg. No./Substance:
|
0/Aldehydes; 0/Disulfides; 29343-52-0/4-hydroxy-2-nonenal; 52-90-4/Cysteine; EC 4.3.2.2/Adenylosuccinate Lyase |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
Previous Document: Urinary methylxanthine and autistic disorder: absence of previously reported correlation.
Next Document: Identification of the 5'-nucleotidase activity altered in neurological syndromes.