Z-Phe-Arg-AMC | Fluorogenic cathepsin substrate

Z-Phe-Arg-AMC (70382-26-2) is a fluorogenic substrate¹ for the following cathepsins (k_cat/K_m in M^-1s^-1): B (10⁵)², C/DPP-I (10⁴)³, F (10⁶)⁴, K/O2 (10⁵)³, L (10⁶)³, L2/V (10⁵)⁵, O⁶, S (10⁴)⁷, X/Z (10⁴)⁸. The peptide is also cleaved by plasma kallikrein and kallikrein 8⁹, and papain (k_cat/K_m=10⁵ M^-1s^-1).³ Excitation: 365nm, Emission: 440nm.⁵

References/Citations:

1. Tavares et al. (2004), Design of potent, selective, and orally bioavailable inhibitors of cysteine protease cathepsin k; J. Med. Chem., 47 588
2. Therrien et al. (2001), Cathepsins X and B can be differentiated through their respective mono- and dipeptidyl carboxypeptidase activities; Biochemistry, 40 2702
3. Nägler et al. (1999), Interdependency of sequence and positional specificities for cysteine proteases of the papain family; Biochemistry, 38 4868
4. Wang et al. (1998), Human cathepsin F. Molecular cloning, functional expression, tissue localization, and enzymatic characterization; J. Biol. Chem., 273 32000
5. Brömme et al. (1999), Human cathepsin V functional expression, tissue distribution, electrostatic surface potential, enzymatic characterization and chromosomal localization; Biochemistry, 38 2377
6. Velasco et al. (1994), Human cathepsin O. Molecular cloning from a breast carcinoma, production of the active enzyme in Escherichia coli, and expression analysis in in human tissues; J. Biol. Chem., 269 27136
7. Kopitar et al. (1996), Folding and activation of human procathepsin S from inclusion bodies produced in Escherichia coli; Eur. J. Biochem., 236 558
8. Klemenčič et al. (2000), Biochemical characterization of human cathepsin X revealed that the enzyme is an exopeptidase, acting as carboxymonopeptidase or carboxydipeptidase; Eur. J. Biochem., 267 5404
9. Kishi et al. (2006), Activation and enzymatic characterization of recombinant human kallikrein 8; Biol. Chem., 387 723