Linked Life Data

1101964

Source:http://linkedlifedata.com/resource/pubmed/id/1101964

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1976-1-8
pubmed:abstractText
Pyruvate decarboxylase dissociates into sub-units of one half the molecular weight at alkaline pH. At the same conditions the cofactors thiamine pyrophosphate and Mg2+ are released and can be separated from the protein. Thiamine pyrophosphate is an obligatory cofactor for reconstitution to the oligomer [1]. In this study the effect of thiamine pyrophosphate derivatives (thiamine monophosphate, thiamine, and thiazole pyrophosphate) upon the reconstitution procedure was evaluated. The complete association of sub-units to form active oligomer was attained only when thiamine pyrophosphate was present. It is concluded that both the pyrimidine ring and the pyrophosphate group are required for productive co-enzyme binding and it is proposed that this interaction effects a conformational change which promotes protomer aggregation to form the enzymatically active holoenzyme. In addition data are presented which indicate that the monomer unit is 60 000 +/- 3000 daltons and that the N-terminal amino acid is histidine. Since the molecular weight of the active oligomer is 230 000 it is proposed that pyruvate decarboxylase is a tetramer comprised of four identical or nearly identical monomer units.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
20
pubmed:volume
405
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
492-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1975
pubmed:articleTitle
Pyruvate decarboxylase III. Specificity restrictions for thiamine pyrophosphate in the protein association step, sub-unit structure.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.