Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1976-4-2
pubmed:abstractText
The presence of activators(AMP and sulphate) or inhibitors(acetyl-CoA) has no influence on the Hill coefficient of the S-shaped [pyruvate]--velocity curve of either the pyruvate-NAD+ overall reaction(h equals 2.5) or that of the pyruvate-K3Fe(CN)6 ACTIVITY OF THE FIRST ENZYME (H EQUALs 1.3). pH STUDIES INDICATED THAT THE Hill coefficient is dependent on subunit ionization within the pyruvate-containing complex and not on those in the free complex. It is concluded that pyruvate conversion rather that pyruvate binding is responsible for the allosteric pattern. The activity is due to absence of a protein kinase, mainly regulated at the acetyl-CoA/CoA, and NADH/NAD+ levels and by the value of the energy charge.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
59
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
347-53
pubmed:dateRevised
2007-7-23
pubmed:meshHeading
pubmed:year
1975
pubmed:articleTitle
The pyruvate-dehydrogenase complex from Azotobacter vinelandii. 2. Regulation of the activity.
pubmed:publicationType
Journal Article