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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Chen, Jian An Tanaka, Takuji |
| Description | Author Affiliation: Chen JA ( Department of Food and Bioproduct Sciences, University of Saskatchewan, Saskatoon, Canada.) |
| Abstract | Allosteric behavior and substrate inhibition are unique characteristics of Lactococcus lactis prolidase. We hypothesized that charged residues (Asp36, His38, Glu39, and Arg40), present on one loop essential for catalysis, interact with residues in or near the active site to impart these unique characteristics. Asp36 has a predominant role in the allosteric behavior, as demonstrated through the non-allosteric behavior of the D36S mutant enzyme. In contrast, a double mutant (D36E/R293K) maintained the allostery, indicating that this aspartic acid residue interacts with Arg293, previously shown to be critical in the allostery. Substitution of His38 drastically reduced the substrate inhibition, and substrate specificity of the mutant at Asp36 or His38 showed the influence of these residues to the substrate specificity. These findings confirm the importance of the loop in the enzymatic reaction mechanism and suggest the existence of conformational changes of the loop structure between open and closed states. A variety of mutations at Glu39 and Arg40 showed that these residues influence roles of the loop in the enzyme reaction. On the basis of these results and combined with observations of molecular models of this prolidase, we concluded that Asp36 and His38 interact with the residues in the active site to generate an allosteric subsite and a pseudo- $S_{1}$ ′ site, which are responsible for the allosteric behavior and substrate inhibition. |
| ISSN | 00063002 |
| Journal | Biochimica et Biophysica Acta (BBA) - Reviews on Cancer |
| Issue Number | 12 |
| Volume Number | 1814 |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2011-12-01 |
| Publisher Place | Netherlands |
| Access Restriction | Open |
| Subject Keyword | Allosteric Regulation Dipeptidases Antagonists & Inhibitors Chemistry Lactococcus Lactis Enzymology Protein Interaction Domains And Motifs Physiology Genetics Allosteric Site Amino Acid Substitution Catalytic Domain Metabolism Enzyme Inhibitors Hydrogen-Ion Concentration Models, Biological Models, Molecular Mutant Proteins Protein Structure, Secondary Substrate Specificity Research Support, Non-U.S. Gov't Biochemistry |
| Content Type | Text |
| Resource Type | Article |
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