Regulation of intracellular concentrations of flavoenzymes and flavin coenzymes is essential for proper cell homeostasis. Red cell acid phosphatase, known as ACP1, catalyzes the transfer of phosphate from phosphate ester substrates to suitable acceptor alcohols such as methanol and glycerol. ACP is a genetically polymorphic, cytoplasmic low-molecular-weight flavin mononucleotide phosphatase that regulates the intracellular concentrations of flavin coenzymes. The human ACP1 gene maps to chromosome 2p25 and encodes a pair of isozymes, Bf (alpha) and Bs (beta). The ACP1 alpha and beta isozymes are not glycosylated. Both ACP1-alpha and ACP1-beta isozymes are 157 amino acids in length; however the two forms differ in sequence over an internal 34 residue segment. The two isoforms are believed to differ in substrate specificity.
