Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1975-11-5
pubmed:abstractText
1. Beta-Phenylpropionylthiocholine and N-(5-aminopentyl)-5-dimethylaminonaphthalene-1-sulphonamide (dansylcadaverine) serve as a pair of water-soluble (pH7.5) model substrates for transamidating enzymes. Amide formation could be followed directly through fluorescence measurements by monitoring the continuous extraction of the water-soluble coupling product, N-(beta-phenylpropionyl)dansylcadaverine, into n-heptane. By this procedure, the steady-state kinetics of glutamine-lysine endo-gamma-glutamyltransferase from human plasma (fibrinoligase, thrombin- and Ca2+-activated blood coagulation Factor XII) and from guinea-pig liver (liver transglutaminase) were investigated at 25 degrees C. 2. With beta-phenylpropionylthiocholine as the varied substrate, Lineweaver-Burk plots with various concentrations of dansylcadaverine intercept on the horizontal axis, suggesting that formation of the acyl-enzyme is rate limiting. 3. On the basis of functional normality of active sites, kcat. values of 1.8 s(-1) and 0.9 s(-1) were obtained for the plasma and liver gamma-glutamyltransferase respectively. The two enzymes show identical affinities for the first substrate, beta-phenylpropionylthiocholine, with Ka 4 times 10(-4) M. 4. Utilization of the second substrate, dansylcadaverine, appears to be an order of magnitude more efficient with the liver enzyme. 5. N-(5-Amino-3-thiapentyl)-5-dimethylaminonaphthalene-1-sulphonamide (dansylthiacadaverine) could be used instead of dansylcadaverine in the fluorescent kinetic system. 6. Competitive inhibition by a non-fluorescent amine substrate histamine was also evaluated.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/239698-4133182, http://linkedlifedata.com/resource/pubmed/commentcorrection/239698-4149557, http://linkedlifedata.com/resource/pubmed/commentcorrection/239698-4405643, http://linkedlifedata.com/resource/pubmed/commentcorrection/239698-4506787, http://linkedlifedata.com/resource/pubmed/commentcorrection/239698-4508920, http://linkedlifedata.com/resource/pubmed/commentcorrection/239698-4508933, http://linkedlifedata.com/resource/pubmed/commentcorrection/239698-4565370, http://linkedlifedata.com/resource/pubmed/commentcorrection/239698-4623561, http://linkedlifedata.com/resource/pubmed/commentcorrection/239698-4629555, http://linkedlifedata.com/resource/pubmed/commentcorrection/239698-4674979, http://linkedlifedata.com/resource/pubmed/commentcorrection/239698-4736472, http://linkedlifedata.com/resource/pubmed/commentcorrection/239698-4778285, http://linkedlifedata.com/resource/pubmed/commentcorrection/239698-4829944, http://linkedlifedata.com/resource/pubmed/commentcorrection/239698-4841063, http://linkedlifedata.com/resource/pubmed/commentcorrection/239698-5096097, http://linkedlifedata.com/resource/pubmed/commentcorrection/239698-5159519, http://linkedlifedata.com/resource/pubmed/commentcorrection/239698-5413933, http://linkedlifedata.com/resource/pubmed/commentcorrection/239698-5488783, http://linkedlifedata.com/resource/pubmed/commentcorrection/239698-5690562, http://linkedlifedata.com/resource/pubmed/commentcorrection/239698-5928192, http://linkedlifedata.com/resource/pubmed/commentcorrection/239698-5958217, http://linkedlifedata.com/resource/pubmed/commentcorrection/239698-6065079
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Amides, http://linkedlifedata.com/resource/pubmed/chemical/Amidinotransferases, http://linkedlifedata.com/resource/pubmed/chemical/Amines, http://linkedlifedata.com/resource/pubmed/chemical/Cadaverine, http://linkedlifedata.com/resource/pubmed/chemical/Calcium, http://linkedlifedata.com/resource/pubmed/chemical/Carbon Radioisotopes, http://linkedlifedata.com/resource/pubmed/chemical/Dansyl Compounds, http://linkedlifedata.com/resource/pubmed/chemical/Factor XIII, http://linkedlifedata.com/resource/pubmed/chemical/Phenylpropionates, http://linkedlifedata.com/resource/pubmed/chemical/Sulfhydryl Compounds, http://linkedlifedata.com/resource/pubmed/chemical/Thrombin, http://linkedlifedata.com/resource/pubmed/chemical/gamma-Glutamyltransferase
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0264-6021
pubmed:author
pubmed:issnType
Print
pubmed:volume
147
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
155-63
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
1975
pubmed:articleTitle
Transamidase kinetics. Amide formation in the enzymic reactions of thiol esters with amines.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.