WebMay 1, 2002 · Acid phosphatases (APs) are a family of enzymes that are widespread in nature, and can be found in many animal and plant species. Mystery surrounds the precise functional role of these molecular... WebMyosin light-chain phosphatase, also called myosin phosphatase (EC 3.1.3.53; systematic name [myosin-light-chain]-phosphate phosphohydrolase ), is an enzyme (specifically a serine/threonine-specific protein phosphatase) that dephosphorylates the regulatory light chain of myosin II :
Acid phosphatases Molecular Pathology
WebJun 9, 1995 · Kidney bean purple acid phosphatase (KBPAP) is an Fe (III)-Zn (II) metalloenzyme resembling the mammalian Fe (III)-Fe (II) purple acid phosphatases. The structure of the homodimeric 111-kilodalton KBPAP was determined at a resolution of 2.9 angstroms. The enzyme contains two domains in each subunit. Purple acid phosphatases (PAPs) (EC 3.1.3.2) are metalloenzymes that hydrolyse phosphate esters and anhydrides under acidic condition. In their oxidised form, PAPs in solution are purple in colour. This is due to the presence of a dinuclear iron centre, to which a tyrosine residue is connected via a charge transfer. This metallic centre is composed of Fe and M, where M is Fe , Zn , Mg or Mn . The conserved Fe is stabilised in the ferric form, whereas M may undergo reduction. Upon treatment … novant and mychart login
LOC108461286 probable inactive purple acid phosphatase 1 []
WebJul 7, 1992 · The rate-determining step in the binding of phosphate to the pink active form (FeIIFeIII) of purple acid phosphatase monitored at 620 nm is independent of phosphate, indicating rapid binding... WebFeb 15, 2014 · Induction and secretion of acid phosphatases (APases) is thought to be an adaptive mechanism that helps plants survive and grow under phosphate (Pi) … WebJan 1, 2013 · Metallo-dependent acid phosphatases (a.k.a. purple acid phosphatases) contain a binuclear ion center [ 18, 19] in the active site which confers a characteristic purple color in solution. The color is produced by a charge transfer mechanism between a conserved tyrosine residue and a Fe +3 ion in the active site [ 20 ]. novant anesthesia associates