[5] Members of the ADAM family are cell surface proteins with a unique structure, possessing both potential adhesion and protease domains.

[11] ADAM10, along with ADAM17, cleaves the ectodomain of the triggering receptor expressed on myeloid cells 2 (TREM2), to produce soluble TREM2 (sTREM2), which has been proposed as a CSF and sera biomarker of neurodegeneration.

Recent experimental evidence suggests that this region, which is distinct from the active site, may be responsible for substrate specificity of the enzyme.

[14] The proposed active site of ADAM10 has been identified by sequence analysis, and is identical to enzymes in the Snake Venom metalloprotein domain family.

The resultant hydroxide initiates a nucleophilic attack on a carbonyl carbon on the peptide backbone, producing a tetrahedral intermediate.

As electrons move down from the oxygen atom to re-form the double bond, the tetrahedral intermediate collapses to products with protonation of -NH by the glutamate residue.

[17] A number of different proteins on the surface of Plasmodium falciparum malaria parasites help the invaders bind to red blood cells.

The entire invasion lasts about 30 seconds and without this ADAM metallopeptidase, malaria would be ineffective at invading the red blood cells.