benzyl N-[(2S)-1-[[(2S)-5-(diaminomethylideneamino)-1-[(4-methyl-2-oxochromen-7-yl)amino]-1-oxopentan-2-yl]amino]-1-oxo-3-phenylpropan-2-yl]carbamate:hydrochloride

Description

Z-Phe-Arg-AMC (70382-26-2) is a fluorogenic substrate1 for the following cathepsins (kcat/Km 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 (kcat/Km=105 M-1s-1).3?Excitation: 365nm, Emission: 440nm.5

Uses

Z-Phe-Arg 7-amido-4-methylcoumarin hydrochloride has been used:

• as a fluorogenic substrate in actinidin inhibition assay
• as a kallikrein substrate
• as a trypsin substrate for fluorometric assay
• as a cathepsin-L substrate

General Description

Substrate for fluorogenic assay of plasma and glandular kallikreins. Also serves as a substrate for cathepsin B, cathepsin L, and papain.

Biochem/physiol Actions

Z-Phe-Arg 7-amido-4-methylcoumarin (Z-FR-AMC) proteolytic lysis by proteases leads to the liberation of AMC resulting in increased fluorescence in the enzymatic reaction.

References

Tavares et al. (2004), Design of potent, selective, and orally bioavailable inhibitors of cysteine protease cathepsin k; J. Med. Chem., 47 588 Therrien et al. (2001), Cathepsins X and B can be differentiated through their respective mono- and dipeptidyl carboxypeptidase activities; Biochemistry, 40 2702 N?gler et al. (1999), Interdependency of sequence and positional specificities for cysteine proteases of the papain family; Biochemistry, 38 4868 Wang et al. (1998), Human cathepsin F. Molecular cloning, functional expression, tissue localization, and enzymatic characterization; J. Biol. Chem., 273 32000 Br?mme et al. (1999), Human cathepsin V functional expression, tissue distribution, electrostatic surface potential, enzymatic characterization and chromosomal localization; Biochemistry, 38 2377 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 Kopitar et al. (1996), Folding and activation of human procathepsin S from inclusion bodies produced in Escherichia coli; Eur. J. Biochem., 236 558 Klemen?i? 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 Kishi et al. (2006), Activation and enzymatic characterization of recombinant human kallikrein 8; Biol. Chem., 387 723