EP-B2

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.
↑ 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.

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

Proteins: enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases(list) EC2 Transferases(list) EC3 Hydrolases(list) EC4 Lyases(list) EC5 Isomerases(list) EC6 Ligases(list)

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EP-B2

References

Further reading