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J A Gerlt

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Biochemistry|December 19, 2001
Evolution of enzymatic activities in the enolase superfamily: crystal structures of the L-Ala-D/L-Glu epimerases from Escherichia coli and Bacillus subtilisA M Gulick, D M Schmidt, J A Gerlt, et al.
Biochemistry|August 22, 2001
Evolution of enzymatic activities in the enolase superfamily: identification of the general acid catalyst in the active site of D-glucarate dehydratase from Escherichia coliA M Gulick, B K Hubbard, J A Gerlt, et al.
Accounts of Chemical Research|March 27, 2001
The crotonase superfamily: divergently related enzymes that catalyze different reactions involving acyl coenzyme a thioestersH M Holden, M M Benning, T Haller, et al.
Biochemistry|January 26, 1988
Cloning, DNA sequence analysis, and expression in Escherichia coli of the gene for mandelate racemase from Pseudomonas putidaS C Ransom, J A Gerlt, V M Powers, et al.
Biochemistry|February 21, 1989
Kinetic and magnetic resonance studies of the glutamate-43 to serine mutant of staphylococcal nucleaseE H Serpersu, D W Hibler, J A Gerlt, et al.
Biochemistry|October 22, 1985
Thermal denaturation of staphylococcal nucleaseR O Calderon, N J Stolowich, J A Gerlt, et al.
Biochemistry|April 16, 1991
Deletion of the omega-loop in the active site of staphylococcal nuclease. 2. Effects on protein structure and dynamicsD M Baldisseri, D A Torchia, L B Poole, et al.
Nature|October 18, 1990
Mandelate racemase and muconate lactonizing enzyme are mechanistically distinct and structurally homologousD J Neidhart, G L Kenyon, J A Gerlt, et al.
The Journal of Biological Chemistry|December 10, 1973
The mechanism of action of 5'-adenylic acid-activated threonine dehydrase. IV. Characterization of kinetic effect of adenosine monophosphateC P Dunne, J A Gerlt, K W Rabinowitz, et al.
The Journal of Biological Chemistry|December 10, 1973
The mechanism of action of 5'-adenylic acid-activated threonine dehydrase. V. Relation between ligand-induced allosteric activation and the protomeroligomer interconversionJ A Gerlt, K W Rabinowitz, C P Dunne, et al.
Pageof 8

Showing results (31-40 of 72) with videos related to

Sort By:
Pageof 8
Biochemistry|December 19, 2001
Evolution of enzymatic activities in the enolase superfamily: crystal structures of the L-Ala-D/L-Glu epimerases from Escherichia coli and Bacillus subtilisA M Gulick, D M Schmidt, J A Gerlt, et al.
Biochemistry|August 22, 2001
Evolution of enzymatic activities in the enolase superfamily: identification of the general acid catalyst in the active site of D-glucarate dehydratase from Escherichia coliA M Gulick, B K Hubbard, J A Gerlt, et al.
Accounts of Chemical Research|March 27, 2001
The crotonase superfamily: divergently related enzymes that catalyze different reactions involving acyl coenzyme a thioestersH M Holden, M M Benning, T Haller, et al.
Biochemistry|January 26, 1988
Cloning, DNA sequence analysis, and expression in Escherichia coli of the gene for mandelate racemase from Pseudomonas putidaS C Ransom, J A Gerlt, V M Powers, et al.
Biochemistry|February 21, 1989
Kinetic and magnetic resonance studies of the glutamate-43 to serine mutant of staphylococcal nucleaseE H Serpersu, D W Hibler, J A Gerlt, et al.
Biochemistry|October 22, 1985
Thermal denaturation of staphylococcal nucleaseR O Calderon, N J Stolowich, J A Gerlt, et al.
Biochemistry|April 16, 1991
Deletion of the omega-loop in the active site of staphylococcal nuclease. 2. Effects on protein structure and dynamicsD M Baldisseri, D A Torchia, L B Poole, et al.
Nature|October 18, 1990
Mandelate racemase and muconate lactonizing enzyme are mechanistically distinct and structurally homologousD J Neidhart, G L Kenyon, J A Gerlt, et al.
The Journal of Biological Chemistry|December 10, 1973
The mechanism of action of 5'-adenylic acid-activated threonine dehydrase. IV. Characterization of kinetic effect of adenosine monophosphateC P Dunne, J A Gerlt, K W Rabinowitz, et al.
The Journal of Biological Chemistry|December 10, 1973
The mechanism of action of 5'-adenylic acid-activated threonine dehydrase. V. Relation between ligand-induced allosteric activation and the protomeroligomer interconversionJ A Gerlt, K W Rabinowitz, C P Dunne, et al.
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