Linked Life Data

12889960

Source:http://linkedlifedata.com/resource/pubmed/id/12889960

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
31
pubmed:dateCreated
2003-7-31
pubmed:abstractText
Two recent crystal structures of acetyl-CoA synthase (ACS) from Moorella thermoacetica exhibited different metal contents and geometries at their active site, called the A-cluster. This led to the proposal of two catalytic mechanisms, one Ni-based, the other Cu-based. ACS was studied with respect to synthase activity, methyl group transfer activity, metal content, and EPR spectroscopy. Our results indicate that Cu is not required for catalysis and that it inactivates ACS by binding to the proximal site of the A-cluster. With Cu in this site, the A-cluster cannot accept a methyl group from the corrinoid-iron-sulfur protein, nor can it exhibit the NiFeC EPR signal after treatment with CO.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0002-7863
pubmed:author
pubmed:issnType
Print
pubmed:day
6
pubmed:volume
125
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
9316-7
pubmed:dateRevised
2008-1-17
pubmed:meshHeading
pubmed:year
2003
pubmed:articleTitle
Inactivation of acetyl-CoA synthase/carbon monoxide dehydrogenase by copper.
pubmed:affiliation
Department of Biochemistry and Biophysics, Texas A&M University, College Station, Texas 77843, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.