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Structural insights into mutations of cystathionine beta-synthase

Meier, M. and Oliveriusova, J. and Kraus, J. P. and Burkhard, P.. (2003) Structural insights into mutations of cystathionine beta-synthase. Biochimica et biophysica acta, Vol. 1647, H. 1/2. pp. 206-213.

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Official URL: http://edoc.unibas.ch/dok/A5258513

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Abstract

Cystathionine beta-synthase (CBS) is a unique heme-containing enzyme that catalyses a pyridoxal 5'-phosphate (PLP)-dependent condensation of serine and homocysteine to give cystathionine. Deficiency of CBS leads to homocystinuria, an inherited disease of sulfur amino acid metabolism characterised by increased levels of homocysteine and methionine and decreased levels of cysteine. Presently, more than 100 CBS mutations have been described which lead to homocystinuria with different degrees of severity in the patients. We have recently solved the crystal structure of a truncated form of this enzyme, which enables us to correlate some of these mutations with the structure.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Former Organization Units Biozentrum > Structural Biology, associated group (Burkhard)
UniBasel Contributors:Burkhard, Peter
Item Type:Article, refereed
Article Subtype:Research Article
Bibsysno:Link to catalogue
Publisher:Elsevier
ISSN:0006-3002
Note:Publication type according to Uni Basel Research Database: Journal article
Last Modified:22 Mar 2012 14:20
Deposited On:22 Mar 2012 13:20

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