Kinetic studies of the transphosphorylation reactions catalyzed by alkaline phosphatase from E. coli: Hydrolysis of p-nitrophenyl phosphate and o-carboxyphenyl phosphate in presence of tris

4-Nitrophenyl phosphoric acid and its four different potassium salts: a solid state structure and kinetic study

“…The H 2 NPP molecule contains a protonated phosphate group, which is singly and doubly ionized in the (HNPP) 2 anion and the (NPP) 22 dianion, respectively. The aromatic rings exhibit distortions from the ideal hexagonal form expected for an unsubstituted benzene.…”

“…18). Heptacoordinated K1 is coordinated by one bidentate and two monodentate (NPP) 22 The salt of 5 forms a polymeric structure with a double corrugated layer of hepta-and octacoordinated potassium cations chelated by dianions and bridged by water molecules and dianions. Such layers are extended along the a axis and are connected by hydrogen bonds.…”

“…16 The 4-nitrophenyl phosphate has a high energy P-O ester bond and is a substrate for the phosphatase assay; many phosphotransferases utilise it as a phosphoryl donor. [17][18][19][20][21][22][23][24] There are only a few references concerning solid state studies of 4-nitrophenyl phosphate acting as a ligand. [25][26][27][28][29][30] So far, the structure and reactivity of homo-and heteronuclear metal (Zn, Cu, Co, Fe, and Mn) complexes with the bridging 4-nitrophenyl phosphate dianion have been reported.…”

Phosphatase Active Cross-Flow Microfiltration Poly(vinylidene Difluoride) Bioreactor

“…From the graphical and numerical-statistical analysis carried out it seems that the global or effective kinetic behaviour of the immobilized enzyme at high and low flow rates can be expressed as a polynomial quotient rate equation In free solution alkaline phosphatase from human placenta catalyses the hydrolysis of p-nitro-and ucarboxyphenyl phosphates according to a rate equation of at least grade 3 : 3, which means that the enzyme behaves in solution in a non-Michaelian way. 5 Since alkaline phosphatase from human placenta is a dimer, it could be proposed that the cause of the nonMichaelian kinetics is the cooperativity between the two active sites of the enzyme molecules, either of binding and catalysis of the substrate, or only the former.…”

Bioremediation of uranium-bearing wastewater: Biochemical and chemical factors influencing bioprocess application

“…Note that these preliminary tests were done in Tris buffer (pH 7), which is known to stimulate the activity of some phosphatases (Roig et al, 1982). In some subsequent tests the buffer was changed to 20 mM MOPS-NaOH (3-N-Morpholino)propanesulfonic acid)/2 mM citrate (pH 7).…”