Document Detail


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.
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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


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