Source:http://linkedlifedata.com/resource/pubmed/id/11173483
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
Pt 2
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pubmed:dateCreated |
2001-2-22
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pubmed:abstractText |
Cystathionine beta-synthase (CBS) is a unique heme enzyme that catalyzes a PLP-dependent condensation of serine and homocysteine to give cystathionine. Deficiency of CBS leads to homocystinuria, an autosomal recessively inherited disease of sulfur metabolism. A truncated form of CBS in which the C-terminal amino-acid residues have been deleted has been prepared. The truncated CBS subunits form a dimer, in contrast to the full-length subunits which form tetramers and higher oligomers. The truncated CBS yielded crystals diffracting to 2.6 A which belong to space group P3(1) or P3(2). This is the first comprehensive structural investigation of a PLP and heme-containing enzyme.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0907-4449
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
57
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
289-91
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pubmed:dateRevised |
2007-7-24
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pubmed:meshHeading |
pubmed-meshheading:11173483-Binding Sites,
pubmed-meshheading:11173483-Cloning, Molecular,
pubmed-meshheading:11173483-Crystallization,
pubmed-meshheading:11173483-Cystathionine beta-Synthase,
pubmed-meshheading:11173483-Escherichia coli,
pubmed-meshheading:11173483-Humans,
pubmed-meshheading:11173483-Recombinant Proteins,
pubmed-meshheading:11173483-Sequence Deletion,
pubmed-meshheading:11173483-Vascular Diseases,
pubmed-meshheading:11173483-X-Ray Diffraction
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pubmed:year |
2001
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pubmed:articleTitle |
Crystallization and preliminary X-ray diffraction analysis of the active core of human recombinant cystathionine beta-synthase: an enzyme involved in vascular disease.
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pubmed:affiliation |
Department of Pediatrics, University of Colorado School of Medicine, Denver, CO 80262, USA.
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pubmed:publicationType |
Journal Article
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