Angiotension Converting Enzyme 2 is a metallopeptidase of the MA(E) subclan of peptidases, also know as the “Glu-zincins” which use the motif HExxH as a catalytic triad. ACE-2 shares the HHEMGH catalytic domain with ACE-1, but otherwise homology is low between ACE-1 and ACE-2 (40% identity). ACE-2 is a type-II transmembrane protein, like ACE-1, and contains one catalytic domain, making it more similar to the germinal form of ACE-1 than the somatic, long form. The stalk region that separates the transmembrane region from the catalytic domain(s) is the cleavage site of a sheddase that releases the catalytic domains of full-length ACE-2 from the cell surface. ACE-2 differs from ACE-1 in enzymatic activity. Whereas ACE-1 is a carboxy dipeptidase that cleaves Angiotension I to form Angiotension II, ACE-2 cleaves Angiotension II to form Angiotension (1-7), an action that would downregulate the Angiotension II activity. ACE-1 inhibitors such as catopril and lisinopril do not block ACE-2 activity. ACE-1 is found in the lung, kidney, heart, pancreas, prostate, testis, small intestine and colon, and is found in cell lysates and as shed or processed forms in cell culture media and in biological fluids, but ACE-2 is more restricted to the testis, heart, kidney and colon. The full-length sequence for ACE-2 encodes an 805 amino acid protein with predicted mass of 92.46 kDa and a pI of 5.22. Glycosylation and other post-translational modifications make the apparent molecular weight on SDS PAGE gels larger, about 120 kDa by Western blot. Many smaller forms may be seen on Western blot of culture media and biological fluid. A recommended starting concentration for Western blots is 1:1000 when using colorimetric substrates such as BCIP/NBT, and 1:5000 for chemiluminescent substrates. Higher concentrations of antibody may be needed for samples from more distantly related species.

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