3.4.24.17	additional information	-	additional information	thermodynamic additivity analysis using stromelysin-1 and a series of biphenyl hydroxamate ligands identified through fragment additivity, thermodynamics determined by isothermal titration calorimetry, corrected for proton transfer events, overview. Additivity arises from enthalpic effects, while interaction entropies are unfavorable, the thermodynamic behavior is masked by proton transfer	733479	
3.4.24.17	0.025	-	(7-Methoxycoumarin-4-yl)acetyl-Arg-Pro-Lys-Pro-Val-Glu-norvaline-Trp-Arg-Lys(2,4-dinitrophenyl)-NH2	-	31015, 31017	
3.4.24.17	0.05	-	(7-Methoxycoumarin-4-yl)acetyl-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Lys-(2,4-dinitrophenyl)-Gly	-	31015	
3.4.24.17	0.066	-	(7-Methoxycoumarin-4-yl)acetyl-Arg-Pro-Lys-Pro-Tyr-Ala-norvaline-Trp-Met-Lys(2,4-dinitrophenyl)-NH2	-	31015	
3.4.24.17	0.1	-	2,4-Dinitrophenyl-Pro-Tyr-Ala-Tyr-Trp-Met-Arg-NH2	-	31015, 31017	
3.4.24.17	0.27	-	acetyl-Pro-Leu-Gly-thioester-Leu-Leu-Gly-ethylester	-	31012	
3.4.24.17	0.395	-	acetyl-Pro-Leu-Gly-[2-mercapto-4-methyl-pentanoyl]-Leu-Gly-OC2H5	pH 6.0, 25°C, catalytic domain (residues 83-247)	717280	
3.4.24.17	0.9	-	Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-norleucine-NH2	wild-type enzyme form	31010	
3.4.24.17	1.4	-	Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-norleucine-NH2	truncated enzyme form	31010