<unk>  <unk>  or<unk> ase), also called acid phosphatase 5,<unk><unk>  (ACP5), is a glycosylated monomeric metalloprotein enzyme expressed in mammals. It has a molecular weight of approximately 35kDa, a basic isoelectric point (7.6–9.5), and optimal activity in acidic conditions.<unk>  is synthesized as latent proenzyme and activated by proteolytic cleavage and reduction. It is differentiated from other mammalian acid phosphatases by its<unk> e to inhibition by<unk>  and by its molecular weight. The mechanism of phosphate ester hydrolysis by<unk>  is through a nucleophilic attack mechanism, whereby, catalysis occurs with the binding of a phosphate-substrate to the Fe2+ in the active site of<unk> . This is then followed by a nucleophilic attack by a hydroxide ligand on the bound phosphorus atom, resulting in cleavage of the phosphate ester bond and production of an alcohol. The exact identity and mechanism of the hydroxide ligand is unclear, but it is thought to be either a hydroxide that bridges the metal ions within the active site or a terminal hydroxide bound to Fe3+, with conflicting reports for both mechanisms.
Tartrate-resistant acid phosphatase
Acid phosphatase
Alanine transaminase
Alpha-amylase
Mammaglobin
Hepcidin
Alpha-fetoprotein
Leukocyte esterase