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Endoprotease B, isoform 2 (EP-B2) is a cysteine protease found in barley. In studies, it has shown promise as a possible therapeutic for coeliac disease.^[1] Aspergillopepsin from Aspergillus niger has been shown to enhance the effects of EP-B2.^[2]

References

^ Vora, H.; McIntire, J.; Kumar, P.; Deshpande, M.; Khosla, C. (2007). "A scaleable manufacturing process for pro-EP-B2, a cysteine protease from barley indicated for celiac sprue". Biotechnology and Bioengineering. 98 (1): 177–185. doi:10.1002/bit.21423. PMID 17385743. S2CID 19581223.
^ Ehren, J.; Morón, B.; Martin, E.; Bethune, M.; Gray, G.; Khosla, C.; El-Shemy, H. A. (2009). "A food-grade enzyme preparation with modest gluten detoxification properties". PLOS ONE. 4 (7): e6313. Bibcode:2009PLoSO...4.6313E. doi:10.1371/journal.pone.0006313. PMC 2708912. PMID 19621078.

Bethune, M.; Ribka, E.; Khosla, C.; Sestak, K.; Bozza, P. (2008). "Transepithelial transport and enzymatic detoxification of gluten in gluten-sensitive rhesus macaques". PLOS ONE. 3 (3): e1857. Bibcode:2008PLoSO...3.1857B. doi:10.1371/journal.pone.0001857. PMC 2267209. PMID 18365012.
Gass, J.; Bethune, M.; Siegel, M.; Spencer, A.; Khosla, C. (2007). "Combination enzyme therapy for gastric digestion of dietary gluten in patients with celiac sprue". Gastroenterology. 133 (2): 472–480. doi:10.1053/j.gastro.2007.05.028. PMID 17681168.
Siegel, M.; Bethune, M.; Gass, J.; Ehren, J.; Xia, J.; Johannsen, A.; Stuge, T.; Gray, G.; Lee, P.; Khosla, C. (2006). "Rational design of combination enzyme therapy for celiac sprue". Chemistry & Biology. 13 (6): 649–658. doi:10.1016/j.chembiol.2006.04.009. PMID 16793522.
Bethune, M.; Strop, P.; Tang, Y.; Sollid, L.; Khosla, C. (2006). "Heterologous expression, purification, refolding, and structural-functional characterization of EP-B2, a self-activating barley cysteine endoprotease". Chemistry & Biology. 13 (6): 637–647. doi:10.1016/j.chembiol.2006.04.008. PMID 16793521.
Gass, J.; Vora, H.; Bethune, M.; Gray, G.; Khosla, C. (2006). "Effect of barley endoprotease EP-B2 on gluten digestion in the intact rat". The Journal of Pharmacology and Experimental Therapeutics. 318 (3): 1178–1186. doi:10.1124/jpet.106.104315. PMID 16757540. S2CID 33662709.

v t e Proteases: cysteine proteases (EC 3.4.22)
Caspase	Caspase 1 Caspase 2 Caspase 3 Caspase 4 Caspase 5 Caspase 6 Caspase 7 Caspase 8 Caspase 9 Caspase 10 Caspase 12 Caspase 13 Caspase 14
Fruit-derived	Papain Ficain Bromelain Actinidain
Calpain	CAPN1 CAPN2 CAPN3 CAPN5 CAPN6 CAPN7 CAPN8 CAPN9 CAPN10 CAPN11 CAPN12 CAPN13 CAPN14 CAPNS1 CAPNS2
Cathepsin	B C F H K L1/L2 O S W Z
Other	Clostripain Cancer procoagulant Separase Autophagin Cruzipain 3C-like protease Gingipain R Gingipain K

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

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