pubmed-article:10550686 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:10550686 | lifeskim:mentions | umls-concept:C0032105 | lld:lifeskim |
pubmed-article:10550686 | lifeskim:mentions | umls-concept:C0205145 | lld:lifeskim |
pubmed-article:10550686 | lifeskim:mentions | umls-concept:C0004492 | lld:lifeskim |
pubmed-article:10550686 | lifeskim:mentions | umls-concept:C0007841 | lld:lifeskim |
pubmed-article:10550686 | lifeskim:mentions | umls-concept:C0005456 | lld:lifeskim |
pubmed-article:10550686 | lifeskim:mentions | umls-concept:C1999216 | lld:lifeskim |
pubmed-article:10550686 | lifeskim:mentions | umls-concept:C0043309 | lld:lifeskim |
pubmed-article:10550686 | lifeskim:mentions | umls-concept:C0242417 | lld:lifeskim |
pubmed-article:10550686 | lifeskim:mentions | umls-concept:C0747055 | lld:lifeskim |
pubmed-article:10550686 | lifeskim:mentions | umls-concept:C2603343 | lld:lifeskim |
pubmed-article:10550686 | lifeskim:mentions | umls-concept:C1710236 | lld:lifeskim |
pubmed-article:10550686 | pubmed:issue | 5 | lld:pubmed |
pubmed-article:10550686 | pubmed:dateCreated | 1999-11-30 | lld:pubmed |
pubmed-article:10550686 | pubmed:abstractText | Ceruloplasmin is a multi-copper oxidase, which contains most of the copper present in the plasma. It is an acute-phase reactant that exhibits a two- to three-fold increase over the normal concentration of 300 microg/ml in adult plasma. However, the precise physiological role(s) of ceruloplasmin has been the subject of intensive debate and it is likely that the enzyme has a multi-functional role, including iron oxidase activity and the oxidation of biogenic amines. The three-dimensional X-ray structure of the human enzyme was elucidated in 1996 and showed that the molecule was composed of six cupredoxin-type domains arranged in a triangular array. There are six integral copper atoms per molecule (mononuclear sites in domains 2, 4 and 6 and a trinuclear site between domains 1 and 6) and two labile sites with roughly 50% occupancy. Further structural studies on the binding of metal cations by the enzyme indicated a putative mechanism for ferroxidase activity. In this paper we report medium-resolution X-ray studies (3.0-3.5 A) which locate the binding sites for an inhibitor (azide) and various substrates [aromatic diamines, biogenic amines and (+)-lysergic acid diethylamide, LSD]. The binding site of the azide moiety is topologically equivalent to one of the sites reported for ascorbate oxidase. However, there are two distinct binding sites for amine substrates: aromatic diamines bind on the bottom of domain 4 remote from the mononuclear copper site, whereas the biogenic amine series typified by serotonin, epinephrine and dopa bind in close vicinity to that utilised by cations in domain 6 and close to the mononuclear copper. These binding sites are discussed in terms of possible oxidative mechanisms. The binding site for LSD is also reported. | lld:pubmed |
pubmed-article:10550686 | pubmed:language | eng | lld:pubmed |
pubmed-article:10550686 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10550686 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:10550686 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10550686 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10550686 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10550686 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10550686 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10550686 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10550686 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10550686 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10550686 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10550686 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10550686 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10550686 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10550686 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:10550686 | pubmed:month | Oct | lld:pubmed |
pubmed-article:10550686 | pubmed:issn | 0949-8257 | lld:pubmed |
pubmed-article:10550686 | pubmed:author | pubmed-author:LindleyP FPF | lld:pubmed |
pubmed-article:10550686 | pubmed:author | pubmed-author:ZaitsevV NVN | lld:pubmed |
pubmed-article:10550686 | pubmed:author | pubmed-author:ZaitsevaII | lld:pubmed |
pubmed-article:10550686 | pubmed:author | pubmed-author:PapizMM | lld:pubmed |
pubmed-article:10550686 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:10550686 | pubmed:volume | 4 | lld:pubmed |
pubmed-article:10550686 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:10550686 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:10550686 | pubmed:pagination | 579-87 | lld:pubmed |
pubmed-article:10550686 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
pubmed-article:10550686 | pubmed:meshHeading | pubmed-meshheading:10550686... | lld:pubmed |
pubmed-article:10550686 | pubmed:meshHeading | pubmed-meshheading:10550686... | lld:pubmed |
pubmed-article:10550686 | pubmed:meshHeading | pubmed-meshheading:10550686... | lld:pubmed |
pubmed-article:10550686 | pubmed:meshHeading | pubmed-meshheading:10550686... | lld:pubmed |
pubmed-article:10550686 | pubmed:meshHeading | pubmed-meshheading:10550686... | lld:pubmed |
pubmed-article:10550686 | pubmed:meshHeading | pubmed-meshheading:10550686... | lld:pubmed |
pubmed-article:10550686 | pubmed:meshHeading | pubmed-meshheading:10550686... | lld:pubmed |
pubmed-article:10550686 | pubmed:meshHeading | pubmed-meshheading:10550686... | lld:pubmed |
pubmed-article:10550686 | pubmed:meshHeading | pubmed-meshheading:10550686... | lld:pubmed |
pubmed-article:10550686 | pubmed:meshHeading | pubmed-meshheading:10550686... | lld:pubmed |
pubmed-article:10550686 | pubmed:meshHeading | pubmed-meshheading:10550686... | lld:pubmed |
pubmed-article:10550686 | pubmed:meshHeading | pubmed-meshheading:10550686... | lld:pubmed |
pubmed-article:10550686 | pubmed:meshHeading | pubmed-meshheading:10550686... | lld:pubmed |
pubmed-article:10550686 | pubmed:meshHeading | pubmed-meshheading:10550686... | lld:pubmed |
pubmed-article:10550686 | pubmed:meshHeading | pubmed-meshheading:10550686... | lld:pubmed |
pubmed-article:10550686 | pubmed:meshHeading | pubmed-meshheading:10550686... | lld:pubmed |
pubmed-article:10550686 | pubmed:year | 1999 | lld:pubmed |
pubmed-article:10550686 | pubmed:articleTitle | An X-ray crystallographic study of the binding sites of the azide inhibitor and organic substrates to ceruloplasmin, a multi-copper oxidase in the plasma. | lld:pubmed |
pubmed-article:10550686 | pubmed:affiliation | CCLRC Daresbury Laboratory, Warrington, Cheshire WA4 4AD, UK. | lld:pubmed |
pubmed-article:10550686 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:10550686 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10550686 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10550686 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10550686 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10550686 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10550686 | lld:pubmed |