Id |
Subject |
Object |
Predicate |
Lexical cue |
T1 |
0-89 |
Sentence |
denotes |
Biosynthesis in Escherichia coli of sn-glycerol 3-phosphate, a precursor of phospholipid. |
T2 |
90-215 |
Sentence |
denotes |
Kinetic characterization of wild type and feedback-resistant forms of the biosynthetic sn-glycerol-3-phosphate dehydrogenase. |
T3 |
216-419 |
Sentence |
denotes |
Homogeneous wild type and feedback-resistant forms of the biosynthetic sn-glycerol 3-phosphate (glycerol-P) dehydrogenase of Escherichia coli (EC1.1.1.8) were subjected to two-substrate kinetic analysis. |
T4 |
420-631 |
Sentence |
denotes |
The kinetics of the NADPH-dependent reduction of dihydroxyacetone phosphate (dihydroxyacetone-P) and of the NADP-dependent oxidation of glycerol-P indicate that these reactions proceed by a sequential mechanism. |
T5 |
632-723 |
Sentence |
denotes |
Glycerol-P was a competitive inhibitor with respect to dihydroxyacetone-P for both enzymes. |
T6 |
724-866 |
Sentence |
denotes |
The wild type and feedback-resistant glycerol-P dehydrogenases had Ki values for glycerol-P of 4.4 micrometer and 43 micrometer, respectively. |
T7 |
867-1061 |
Sentence |
denotes |
Therefore, the sensitivity of the wild type activity and reduced sensitivity of the feedback-resistant activity, both noted previously in crude extracts, were inherent properties of the enzymes. |
T8 |
1062-1273 |
Sentence |
denotes |
The patterns of product inhibition for both enzymes were identical, and the difference in the inhibition constants for glycerol-P occurred without significant alteration of any other kinetic constant determined. |
T9 |
1274-1407 |
Sentence |
denotes |
Kinetic mechanisms consistent with the patterns of product inhibition violated Haldane relationships and other kinetic relationships. |
T10 |
1408-1510 |
Sentence |
denotes |
These discrepancies suggest that glycerol-P inhibition occurs at a site distinct from the active site. |
T11 |
1511-1661 |
Sentence |
denotes |
The pH dependencies of the Km for dihydroxyacetone-P and the Ki for glycerol-P were markedly different suggesting the existence of an allosteric site. |
T12 |
1662-1767 |
Sentence |
denotes |
The addition of glycerol-P in the presence of NADPH stabilized both enzymes against thermal inactivation. |
T13 |
1768-1916 |
Sentence |
denotes |
Half-maximal stabilization was provided by 5 micrometer and 50 micrometer glycerol-P for the wild type and feedback-resistant enzymes, respectively. |
T14 |
1917-2127 |
Sentence |
denotes |
These kinetic data, considered in conjunction with previous physiologic and genetic data, indicate that the synthesis of glycerol-P is regulated in vivo by glycerol-P inhibition of the glycerol-P dehydrogenase. |
T15 |
2128-2213 |
Sentence |
denotes |
The data suggest that glycerol-P inhibition occurs at an allosteric, regulatory site. |
T1 |
0-89 |
Sentence |
denotes |
Biosynthesis in Escherichia coli of sn-glycerol 3-phosphate, a precursor of phospholipid. |
T2 |
90-215 |
Sentence |
denotes |
Kinetic characterization of wild type and feedback-resistant forms of the biosynthetic sn-glycerol-3-phosphate dehydrogenase. |
T3 |
216-419 |
Sentence |
denotes |
Homogeneous wild type and feedback-resistant forms of the biosynthetic sn-glycerol 3-phosphate (glycerol-P) dehydrogenase of Escherichia coli (EC1.1.1.8) were subjected to two-substrate kinetic analysis. |
T4 |
420-631 |
Sentence |
denotes |
The kinetics of the NADPH-dependent reduction of dihydroxyacetone phosphate (dihydroxyacetone-P) and of the NADP-dependent oxidation of glycerol-P indicate that these reactions proceed by a sequential mechanism. |
T5 |
632-723 |
Sentence |
denotes |
Glycerol-P was a competitive inhibitor with respect to dihydroxyacetone-P for both enzymes. |
T6 |
724-866 |
Sentence |
denotes |
The wild type and feedback-resistant glycerol-P dehydrogenases had Ki values for glycerol-P of 4.4 micrometer and 43 micrometer, respectively. |
T7 |
867-1061 |
Sentence |
denotes |
Therefore, the sensitivity of the wild type activity and reduced sensitivity of the feedback-resistant activity, both noted previously in crude extracts, were inherent properties of the enzymes. |
T8 |
1062-1273 |
Sentence |
denotes |
The patterns of product inhibition for both enzymes were identical, and the difference in the inhibition constants for glycerol-P occurred without significant alteration of any other kinetic constant determined. |
T9 |
1274-1407 |
Sentence |
denotes |
Kinetic mechanisms consistent with the patterns of product inhibition violated Haldane relationships and other kinetic relationships. |
T10 |
1408-1510 |
Sentence |
denotes |
These discrepancies suggest that glycerol-P inhibition occurs at a site distinct from the active site. |
T11 |
1511-1661 |
Sentence |
denotes |
The pH dependencies of the Km for dihydroxyacetone-P and the Ki for glycerol-P were markedly different suggesting the existence of an allosteric site. |
T12 |
1662-1767 |
Sentence |
denotes |
The addition of glycerol-P in the presence of NADPH stabilized both enzymes against thermal inactivation. |
T13 |
1768-1916 |
Sentence |
denotes |
Half-maximal stabilization was provided by 5 micrometer and 50 micrometer glycerol-P for the wild type and feedback-resistant enzymes, respectively. |
T14 |
1917-2127 |
Sentence |
denotes |
These kinetic data, considered in conjunction with previous physiologic and genetic data, indicate that the synthesis of glycerol-P is regulated in vivo by glycerol-P inhibition of the glycerol-P dehydrogenase. |
T15 |
2128-2213 |
Sentence |
denotes |
The data suggest that glycerol-P inhibition occurs at an allosteric, regulatory site. |