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• W2030299248 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 . ► MMP-7 activity exhibits a broad bell-shaped pH-dependence with the p K e1 and p K e2 values of 4 and 10. ► The p K e2 value suggests Tyr or Lys, but no Lys is in the active site, and thus Tyr219 is the candidate. ► However, Tyr219 was declined to be the p K e2 residue by site-directed mutagenesis analysis of MMP-7. ► Thermodynamic analysis suggested that Glu198 is responsible for p K e1 . ► It also suggested that a protein-bound water molecule is responsible p K e2 ." @default.
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• W2030299248 date "2011-12-01" @default.
• W2030299248 modified "2023-10-08" @default.
• W2030299248 title "Thermodynamic analysis of ionizable groups involved in the catalytic mechanism of human matrix metalloproteinase 7 (MMP-7)" @default.
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• W2030299248 doi "https://doi.org/10.1016/j.bbapap.2011.07.008" @default.
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