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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Takeharu, Hitoshi Inouye, Kuniyo Yasukawa, Kiyoshi |
| Description | Author Affiliation: Takeharu H ( Kyoto University, Kyoto, Japan.) |
| Abstract | Human matrix metalloproteinase 7 (MMP-7) exhibits a broad bell-shaped pH-dependence with the acidic and alkaline p $K_{e}$ (p $K_{e1}$ and p $K_{e2}$ ) values of about 4 and 10. In this study, we estimated the ionizable groups involved in its catalytic mechanism by thermodynamic analysis. p $K_{a}$ of side chains of L -Asp, L -Glu, L-His, L -Cys, L -Tyr, L -Lys, and L -Arg at 25–45 °C were determined by the pH titration of amino-acid solutions, from which their enthalpy changes, ∆H °, of deprotonation were calculated. p $K_{e1}$ and p $K_{e2}$ of MMP-7 at 15–45 °C were determined in the hydrolysis of (7-methoxycoumarin-4-yl)acetyl- L -Pro- L -Leu-Gly- L -Leu-[ $N^{3}$ -(2,4-dinitrophenyl)- L -2,3-diaminopropionyl]- L -Ala- L -Arg-NH $_{2}$ , from which $∆H^{o}$ for p $K_{e1}$ and p $K_{e2}$ was calculated. The $∆H^{o}$ for p $K_{e1}$ (− 20.6 ± 6.1 kJ mol $^{−$ 1 ) was similar to that for L -Glu (− 23.6 ± 5.8 kJ mol $^{−$ 1 ), and the $∆H^{o}$ for p $K_{e2}$ (89.9 ± 4.0 kJ mol $^{−$ 1 ) was similar to those for L -Arg (87.6 ± 5.5 kJ mol $^{−$ 1 ) and L -Lys (70.4 ± 4.4 kJ mol $^{−$ 1 ). The mutation of the active-site residue Glu198 into Ala completely abolished the activity, suggesting that Glu198 is the ionizable group for p $K_{e1}$ . On the other hand, no arginine or lysine residues are found in the active site of MMP-7. We proposed a possibility that a protein-bound water is the ionizable group for p $K_{e2}$ . |
| 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 | Ions Chemistry Matrix Metalloproteinase 7 Metabolism Catalysis Catalytic Domain Kinetics Genetics Models, Biological Mutant Proteins Protein Interaction Domains And Motifs Physiology Protein Structure, Secondary Thermodynamics Research Support, Non-U.S. Gov't Biochemistry |
| Content Type | Text |
| Resource Type | Article |
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