Z-Leu-Arg-7-amino-4-methylcoumarin

Product NameZ-Leu-Arg-7-amino-4-methylcoumarin
CAS156192-32-4
MFC30H38N6O6
MW578.66
EINECS
MOL File156192-32-4.mol

Chemical Properties

Density	1.31±0.1 g/cm3(Predicted)
storage temp.	Store at 0-5°C
solubility	Soluble in DMSO
form	solid
pka	11.13±0.46(Predicted)
color	White
Stability	Stable for 2 years from date of purchase as supplied. Solutions in DMSO may be stored at -20°C for up to 3 months. Protect from light!

Usage And Synthesis

Description

Z-Leu-Arg-AMC (156192-32-4) is a sensitive Cathepsin K fluorogenic substrate (Km=8μM, kcat/Km=4 x 105 M-1s-1)1-3. It is cleaved more slowly by the following cathepsins (kcat/Km: B (105)4, F (106)4, L (106)4,5, L2/V (104)5, S (105)2,4,5. Also cleaved by malaria parasite proteases berghepain6, vivapain-2 and -37, and falcipain-1, -2, and -36,8,9. Excitation: 365nm, Emission: 440nm.

Uses

A sensitive fluorogenic substrate for cathepsin K

IC 50

Trypanosoma

References

[1] M J BOSSARD. Proteolytic activity of human osteoclast cathepsin K. Expression, purification, activation, and substrate identification.[J]. The Journal of Biological Chemistry, 1996, 271 21: 12517-12524. DOI:10.1074/jbc.271.21.12517
[2] D BRÖMME. Human cathepsin O2, a matrix protein-degrading cysteine protease expressed in osteoclasts. Functional expression of human cathepsin O2 in Spodoptera frugiperda and characterization of the enzyme.[J]. The Journal of Biological Chemistry, 1996, 271 4: 2126-2132. DOI:10.1074/jbc.271.4.2126
[3] C J LINNEVERS. Expression of human cathepsin K in Pichia pastoris and preliminary crystallographic studies of an inhibitor complex.[J]. Protein Science, 1997, 6 4: 919-921. DOI:10.1002/pro.5560060421
[4] B WANG. Human cathepsin F. Molecular cloning, functional expression, tissue localization, and enzymatic characterization.[J]. The Journal of Biological Chemistry, 1998, 273 48: 32000-32008. DOI:10.1074/jbc.273.48.32000
[5] DIETER BRÖMME. Human Cathepsin V Functional Expression, Tissue Distribution, Electrostatic Surface Potential, Enzymatic Characterization, and Chromosomal Localization‡[J]. Biochemistry Biochemistry, 1999, 38 8: 2377-2385. DOI:10.1021/bi982175f
[6] AJAY SINGH. A chimeric cysteine protease of Plasmodium berghei engineered to resemble the Plasmodium falciparum protease falcipain-2.[J]. Protein Engineering Design & Selection, 2007, 20 4: 171-177. DOI:10.1093/protein/gzm009
[7] BYOUNG-KUK NA. Identification and biochemical characterization of vivapains, cysteine proteases of the malaria parasite Plasmodium vivax.[J]. Biochemical Journal, 2004, 378 Pt 2: 529-538. DOI:10.1042/bj20031487
[8] S L GOH T S S L L Goh. Cysteine protease falcipain 1 in Plasmodium falciparum is biochemically distinct from its isozymes.[J]. Parasitology Research, 2005, 97 4: 295-301. DOI:10.1007/s00436-005-1430-7
[9] KAILASH C PANDEY. Independent intramolecular mediators of folding, activity, and inhibition for the Plasmodium falciparum cysteine protease falcipain-2.[J]. The Journal of Biological Chemistry, 2004, 279 5: 3484-3491. DOI:10.1074/jbc.m310536200

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