Linked Life Data

12670960

Source:http://linkedlifedata.com/resource/pubmed/id/12670960

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
23
pubmed:dateCreated
2003-6-2
pubmed:abstractText
Rhodobacter capsulatus xanthine dehydrogenase (XDH) forms an (alphabeta)2 heterotetramer and is highly homologous to homodimeric eukaryotic XDHs. The crystal structures of bovine XDH and R. capsulatus XDH showed that the two proteins have highly similar folds. We have developed an efficient system for the recombinant expression of R. capsulatus XDH in Escherichia coli. The recombinant protein shows spectral features and a range of substrate specificities similar to bovine milk xanthine oxidase. However, R. capsulatus XDH is at least 5 times more active than bovine XDH and, unlike mammalian XDH, does not undergo the conversion to the oxidase form. EPR spectra were obtained for the FeS centers of the enzyme showing an axial signal for FeSI, which is different from that reported for xanthine oxidase. X-ray absorption spectroscopy at the iron and molybdenum K-edge and the tungsten LIII-edge have been used to probe the different metal coordinations of variant forms of the enzyme. Based on a mutation identified in a patient suffering from xanthinuria I, the corresponding arginine 135 was substituted to a cysteine in R. capsulatus XDH, and the protein variant was purified and characterized. Two different forms of XDH-R135C were purified, an active (alphabeta)2 heterotetrameric form and an inactive (alphabeta) heterodimeric form. The active form contains a full complement of redox centers, whereas in the inactive form the FeSI center is likely to be missing.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
6
pubmed:volume
278
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
20802-11
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed-meshheading:12670960-Absorptiometry, Photon, pubmed-meshheading:12670960-Animals, pubmed-meshheading:12670960-Bacterial Proteins, pubmed-meshheading:12670960-Cattle, pubmed-meshheading:12670960-Dimerization, pubmed-meshheading:12670960-Electron Spin Resonance Spectroscopy, pubmed-meshheading:12670960-Escherichia coli, pubmed-meshheading:12670960-Gene Expression Regulation, Bacterial, pubmed-meshheading:12670960-Gene Expression Regulation, Enzymologic, pubmed-meshheading:12670960-Humans, pubmed-meshheading:12670960-Iron, pubmed-meshheading:12670960-Ligands, pubmed-meshheading:12670960-Milk, pubmed-meshheading:12670960-Molybdenum, pubmed-meshheading:12670960-Mutagenesis, Site-Directed, pubmed-meshheading:12670960-Purine-Pyrimidine Metabolism, Inborn Errors, pubmed-meshheading:12670960-Recombinant Proteins, pubmed-meshheading:12670960-Rhodobacter capsulatus, pubmed-meshheading:12670960-Substrate Specificity, pubmed-meshheading:12670960-Sulfur, pubmed-meshheading:12670960-Tungsten, pubmed-meshheading:12670960-Xanthine Dehydrogenase
pubmed:year
2003
pubmed:articleTitle
Recombinant Rhodobacter capsulatus xanthine dehydrogenase, a useful model system for the characterization of protein variants leading to xanthinuria I in humans.
pubmed:affiliation
Department of Plant Biology, Technical University Braunschweig, 38023 Braunschweig, Germany. S.Leimkuhler@tu-bs.de
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't