PMID:324991
| Citation |
Yoshinaga, T (1977) Structural specificity of the allosteric inhibitor of phosphoenolpyruvate carboxylase of Escherichia coli. J. Biochem. 81:665-71 |
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| Abstract |
The structural specificity of the allosteric inhibitor of phosphoenolpyruvate carboxylas [EC 4.1.1.31] of Escherichia coli W was investigated using native enzyme and photooxidized enzyme which was desensitized to L-aspartate. Inhibitory activity was expressed in terms of the concentration of the compound required for 50% inhibition (I0.5). For the native enzyme, L-aspartate and L-malate were the strongest inhibitors with I0.5 values of about 0.10-0.15 mM among about 20 componds tested. For the photooxidized enzyme, oxaloacetate and L-malate were relatively strong inhibitors wiht I0.5 values of about 11-16 mM. The results obtained suggest that the inhibition of the native enzyme mainly reflects allosteric inhibition. |
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| Keywords |
Allosteric Regulation; Allosteric Site; Aspartic Acid/analogs & derivatives; Aspartic Acid/pharmacology; Carboxy-Lyases/antagonists & inhibitors; Escherichia coli/enzymology; Kinetics; Oxaloacetates/pharmacology; Phosphoenolpyruvate; Structure-Activity Relationship |
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