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. Author manuscript; available in PMC: 2013 Feb 1.
Published in final edited form as: Biochim Biophys Acta. 2011 Oct 10;1823(2):406–419. doi: 10.1016/j.bbamcr.2011.09.012

Figure 3. Transamidase active site of TG2.

Figure 3

The catalytic site of transamidating activity is composed of the catalytic triad: Cys277, His335 and Asp358. A conserved tryptophan residue, Trp241 is also critical for the transamidating activity. A hydrogen bond forms between Cys277 and Tyr516 in the closed conformation of TG2, which is believed to further stabilize the closed conformation and keep the enzyme inactive.