I have heard some rumors that the HRV-3C protease can recognize and cleave ENLYFQG peptide, which is a consensus sequence cleaved by the TEV protease. Can anyone confirm or suggest some literature where I can find this information?
Tobacco Etch Virus (TEV) is a cysteine protease known for its high activity and very specific cleaving. while HRV 3C is human rhinovirus protease and similar to TEV it is also a cysteine protease. TEV cleaves between Gln and Gln/Ser residues in the recognition sequence Glu-Asn-Leu-Tyr-Phe-Gln ↓Gly/Ser while HRV-3C cleaves between Gln and Gly at the recognition site Leu-Glu-Val-Phe Gln ↓ Gly-Pro Although their cleavage site amino acids are identical as shown by the row between Gln -Gly but the presence of the Gly-Pro peptide is very important for substrate recognition of the HRV 3C enzyme but not TEV enzyme and only in this case the two enzymes might work on the same substrate of course with different rates and conditions of pH ,temp etc. Good luck
Did anyone have any evidence showing that TEV cannot cleave a HRV3C site? Trying to design a construct with both a TEV and HRV3C site but I'm now hesitant.