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D J Kuo

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Biochemistry|August 2, 1983
Active site directed irreversible inactivation of brewers' yeast pyruvate decarboxylase by the conjugated substrate analogue (E)-4-(4-chlorophenyl)-2-oxo-3-butenoic acid: development of a suicide substrateD J Kuo, F Jordan
The Journal of Biological Chemistry|November 25, 1983
Direct spectroscopic observation of a brewer's yeast pyruvate decarboxylase-bound enamine intermediate produced from a suicide substrate. Evidence for nonconcerted decarboxylationD J Kuo, F Jordan
Biochemistry|December 1, 1987
Aconitase: its source of catalytic protonsD J Kuo, I A Rose
Biochemistry|June 30, 1992
Role of CO2 in proton activation by histidine decarboxylase (pyruvoyl)I A Rose, D J Kuo
Biochemistry|July 16, 1985
Chemical trapping of complexes of dihydroxyacetone phosphate with muscle fructose-1,6-bisphosphate aldolaseD J Kuo, I A Rose
Biochemistry|December 12, 1989
The substrate proton of the pyruvate kinase reactionI A Rose, D J Kuo
The Journal of Biological Chemistry|March 5, 1986
Resolution of brewers' yeast pyruvate decarboxylase into two isozymesD J Kuo, G Dikdan, F Jordan
Analytical Biochemistry|May 1, 1978
A pH-rate determination of the activity-pH profile of enzymes. application to yeast pyruvate decarboxylase demonstrating the existence of multiple ionizable groupsF Jordan, D J Kuo, E U Monse
Biochemistry|January 22, 1991
A rate-determining proton relay in the pyruvate kinase reactionI A Rose, D J Kuo, J V Warms
The Journal of Biological Chemistry|January 15, 1987
Concentration and partitioning of intermediates in the fructose bisphosphate aldolase reaction. Comparison of the muscle and liver enzymesI A Rose, J V Warms, D J Kuo
Pageof 2

Showing results (1-10 of 11) with videos related to

Sort By:
Pageof 2
Biochemistry|August 2, 1983
Active site directed irreversible inactivation of brewers' yeast pyruvate decarboxylase by the conjugated substrate analogue (E)-4-(4-chlorophenyl)-2-oxo-3-butenoic acid: development of a suicide substrateD J Kuo, F Jordan
The Journal of Biological Chemistry|November 25, 1983
Direct spectroscopic observation of a brewer's yeast pyruvate decarboxylase-bound enamine intermediate produced from a suicide substrate. Evidence for nonconcerted decarboxylationD J Kuo, F Jordan
Biochemistry|December 1, 1987
Aconitase: its source of catalytic protonsD J Kuo, I A Rose
Biochemistry|June 30, 1992
Role of CO2 in proton activation by histidine decarboxylase (pyruvoyl)I A Rose, D J Kuo
Biochemistry|July 16, 1985
Chemical trapping of complexes of dihydroxyacetone phosphate with muscle fructose-1,6-bisphosphate aldolaseD J Kuo, I A Rose
Biochemistry|December 12, 1989
The substrate proton of the pyruvate kinase reactionI A Rose, D J Kuo
The Journal of Biological Chemistry|March 5, 1986
Resolution of brewers' yeast pyruvate decarboxylase into two isozymesD J Kuo, G Dikdan, F Jordan
Analytical Biochemistry|May 1, 1978
A pH-rate determination of the activity-pH profile of enzymes. application to yeast pyruvate decarboxylase demonstrating the existence of multiple ionizable groupsF Jordan, D J Kuo, E U Monse
Biochemistry|January 22, 1991
A rate-determining proton relay in the pyruvate kinase reactionI A Rose, D J Kuo, J V Warms
The Journal of Biological Chemistry|January 15, 1987
Concentration and partitioning of intermediates in the fructose bisphosphate aldolase reaction. Comparison of the muscle and liver enzymesI A Rose, J V Warms, D J Kuo
Pageof 2