Biochemical and Structural Analysis of 14 Mutant ADSL Enzyme Complexes and Correlation to Phenotypic Heterogeneity of Adenylosuccinate Lyase Deficiency

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11110%2F10%3A7879" target="_blank" >RIV/00216208:11110/10:7879 - isvavai.cz</a>

Alternative codes found

RIV/00064165:_____/10:7879

Result on the web

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DOI - Digital Object Identifier

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Result language

angličtina

Original language name

Biochemical and Structural Analysis of 14 Mutant ADSL Enzyme Complexes and Correlation to Phenotypic Heterogeneity of Adenylosuccinate Lyase Deficiency

Original language description

Adenylosuccinate lyase (ADSL) deficiency, an inborn error of purine metabolism, leads to accumulation of dephosphorylated ADSL substrates SAICA-riboside (SAICAr) and succinyladenosine (S-Ado) in body fluids and affects the patients´ nervous system. Severity of symptoms differs and correlates with diverse S-Ado/SAICAr concentrations´ ratio in cerebrospinal fluid. To identify biochemical and structural basis of the S-Ado/SAICAr ratio and phenotypic heterogeneity we expressed and characterized 19 ADSL mutant proteins corresponding to 16 clinically well characterized genotypes. We found that phenotypic severity correlates with residual enzymatic activities and structural stability of the corresponding mutant ADSL complex and does not result from genotype-specific disproportional catalytic activities toward one of the enzyme substrates. It suggests that S-Ado/SAICAr ratio value is probably not predictive of phenotype severity but rather it may be secondary to degree of patient?s development

Czech name

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Czech description

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Type

J_x - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

CEP classification

EB - Genetics and molecular biology

OECD FORD branch

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Project

Result was created during the realization of more than one project. More information in the Projects tab.

Continuities

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>Z - Vyzkumny zamer (s odkazem do CEZ)

Publication year

2010

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Human Mutation

ISSN

1059-7794

e-ISSN

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Volume of the periodical

31

Issue of the periodical within the volume

4

Country of publishing house

US - UNITED STATES

Number of pages

11

Pages from-to

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UT code for WoS article

000276810600009

EID of the result in the Scopus database

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