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rdf:type |
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lifeskim:mentions |
umls-concept:C0001383,
umls-concept:C0026845,
umls-concept:C0030016,
umls-concept:C0030685,
umls-concept:C0033727,
umls-concept:C0039005,
umls-concept:C0061539,
umls-concept:C0243144,
umls-concept:C0391871,
umls-concept:C0596524,
umls-concept:C0680255,
umls-concept:C1283071,
umls-concept:C1963578,
umls-concept:C2603343
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pubmed:issue |
4
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pubmed:dateCreated |
1974-4-11
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pubmed:abstractText |
In the presence of NAD(+) the acylation by 1,3-diphosphoglycerate of the four active sites of pig muscle d-glyceraldehyde 3-phosphate dehydrogenase can be monitored at 365nm by the disappearance of the absorption band present in the binary complex of NAD(+) and the enzyme. A non-specific salt effect decreased the acylation rate 25-fold when the ionic strength was increased from 0.10 to 1.0. This caused acylation to be the rate-limiting process in the enzyme-catalysed reductive dephosphorylation of 1,3-diphosphoglycerate at high ionic strength at pH8. The salt effect permitted investigation of the acylation over a wide range of conditions. Variation of pH from 5.4 to 8.6 produced at most a two-fold change in the acylation rate. One proton was taken up per site acylated at pH8.0. By using a chromophoric H(+) indicator the rate of proton uptake could be monitored during the acylation and was also almost invariant in the pH range 5.5-8.5. Transient kinetic studies of the overall enzyme-catalysed reaction indicated that acylation was the process involving proton uptake at pH8.0. The enzyme mechanism is discussed in the light of these results.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/4360248-13246635,
http://linkedlifedata.com/resource/pubmed/commentcorrection/4360248-13544942,
http://linkedlifedata.com/resource/pubmed/commentcorrection/4360248-14209940,
http://linkedlifedata.com/resource/pubmed/commentcorrection/4360248-14275144,
http://linkedlifedata.com/resource/pubmed/commentcorrection/4360248-4238423,
http://linkedlifedata.com/resource/pubmed/commentcorrection/4360248-4300829,
http://linkedlifedata.com/resource/pubmed/commentcorrection/4360248-4326012,
http://linkedlifedata.com/resource/pubmed/commentcorrection/4360248-4326767,
http://linkedlifedata.com/resource/pubmed/commentcorrection/4360248-4330968,
http://linkedlifedata.com/resource/pubmed/commentcorrection/4360248-4332544,
http://linkedlifedata.com/resource/pubmed/commentcorrection/4360248-4332597,
http://linkedlifedata.com/resource/pubmed/commentcorrection/4360248-4333192,
http://linkedlifedata.com/resource/pubmed/commentcorrection/4360248-4345585,
http://linkedlifedata.com/resource/pubmed/commentcorrection/4360248-4352913,
http://linkedlifedata.com/resource/pubmed/commentcorrection/4360248-4399048,
http://linkedlifedata.com/resource/pubmed/commentcorrection/4360248-4509026,
http://linkedlifedata.com/resource/pubmed/commentcorrection/4360248-4643321,
http://linkedlifedata.com/resource/pubmed/commentcorrection/4360248-5880873
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0264-6021
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
135
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
695-703
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pubmed:dateRevised |
2010-9-13
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pubmed:meshHeading |
pubmed-meshheading:4360248-Acylation,
pubmed-meshheading:4360248-Animals,
pubmed-meshheading:4360248-Binding Sites,
pubmed-meshheading:4360248-Diphosphoglyceric Acids,
pubmed-meshheading:4360248-Glyceraldehyde-3-Phosphate Dehydrogenases,
pubmed-meshheading:4360248-Hydrogen-Ion Concentration,
pubmed-meshheading:4360248-Kinetics,
pubmed-meshheading:4360248-Models, Theoretical,
pubmed-meshheading:4360248-Muscles,
pubmed-meshheading:4360248-NAD,
pubmed-meshheading:4360248-Osmolar Concentration,
pubmed-meshheading:4360248-Protons,
pubmed-meshheading:4360248-Spectrophotometry,
pubmed-meshheading:4360248-Swine
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pubmed:year |
1973
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pubmed:articleTitle |
Kinetic studies of the acylation of pig muscle D-glyceraldehyde 3-phosphate dehydrogenase by 1,3-diphosphoglycerate and of proton uptake and release in the overall enzyme mechanism.
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pubmed:publicationType |
Journal Article
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