Phosphoserine phosphatase belongs to a new class of phosphotransferases forming an acylphosphate during catalysis and sharing three motifs with P-type ATPases and haloacid dehalogenases. The phosphorylated residue was identified as the first aspartate in the first motif (DXDXT) by mass spectrometry analysis of peptides derived from the phosphorylated enzyme treated with NaBH(4) or alkaline [(18)O]H(2)O. Incubation of native phosphoserine phosphatase with phosphoserine in [(18)O]H(2)O did not result in (18)O incorporation in residue Asp-20, indicating that the phosphoaspartate is hydrolyzed, as in P-type ATPases, by attack of the phosphorus atom. Mutagenesis studies bearing on conserved residues indicated that four conservative changes eithe...
AbstractThe machinery to catalyze elementary reactions is conserved, and the number of solved enzyme...
We report the identification of the mutations in the only known case of L-3-phosphoserine phosphatas...
Human prostatic acid phosphatase (E.C. 3.1.3.2) is a dimeric enzyme composed of two identical non-co...
AbstractBackground: D-Serine is a co-agonist of the N-methyl-D-aspartate subtype of glutamate recept...
When incubated with their substrates, human phosphomannomutase and L-3-phosphoserine phosphatase are...
The large HAD (haloacid dehalogenase) superfamily of hydrolases comprises P-type ATPases, phosphatas...
The low M$\sb{\rm r}$ PTPases are a family of 18 kDa proteins that are found in vertebrates, yeast a...
PHOSPHO1, a phosphoethanolamine/phosphocholine phosphatase, is upregulated in mineralising cells and...
PHOSPHO1 is a recently identified phosphatase whose expression is upregulated in mineralizing cells ...
Phosphoserine phosphatase (PSP), a member of the haloacid dehalogenase (HAD) superfamily that compri...
AbstractThe crystal structure of the bovine liver low Mr phosphotyrosine protein phosphatase suggest...
AbstractMutagenesis of Glu820, present in the catalytic subunit of gastric H+,K+-ATPase, into an Asp...
AbstractTo monitor structural changes during the binding of Pi to the active site of mammalian alkal...
Positive charge is uniformly present in the active sites of all known phosphatases. The postulate th...
The cooperative interplay between the functional devices of a preorganized active site is fundamenta...
AbstractThe machinery to catalyze elementary reactions is conserved, and the number of solved enzyme...
We report the identification of the mutations in the only known case of L-3-phosphoserine phosphatas...
Human prostatic acid phosphatase (E.C. 3.1.3.2) is a dimeric enzyme composed of two identical non-co...
AbstractBackground: D-Serine is a co-agonist of the N-methyl-D-aspartate subtype of glutamate recept...
When incubated with their substrates, human phosphomannomutase and L-3-phosphoserine phosphatase are...
The large HAD (haloacid dehalogenase) superfamily of hydrolases comprises P-type ATPases, phosphatas...
The low M$\sb{\rm r}$ PTPases are a family of 18 kDa proteins that are found in vertebrates, yeast a...
PHOSPHO1, a phosphoethanolamine/phosphocholine phosphatase, is upregulated in mineralising cells and...
PHOSPHO1 is a recently identified phosphatase whose expression is upregulated in mineralizing cells ...
Phosphoserine phosphatase (PSP), a member of the haloacid dehalogenase (HAD) superfamily that compri...
AbstractThe crystal structure of the bovine liver low Mr phosphotyrosine protein phosphatase suggest...
AbstractMutagenesis of Glu820, present in the catalytic subunit of gastric H+,K+-ATPase, into an Asp...
AbstractTo monitor structural changes during the binding of Pi to the active site of mammalian alkal...
Positive charge is uniformly present in the active sites of all known phosphatases. The postulate th...
The cooperative interplay between the functional devices of a preorganized active site is fundamenta...
AbstractThe machinery to catalyze elementary reactions is conserved, and the number of solved enzyme...
We report the identification of the mutations in the only known case of L-3-phosphoserine phosphatas...
Human prostatic acid phosphatase (E.C. 3.1.3.2) is a dimeric enzyme composed of two identical non-co...