Jf. Collet et al., HUMAN L-3-PHOSPHOSERINE PHOSPHATASE - SEQUENCE, EXPRESSION AND EVIDENCE FOR A PHOSPHOENZYME INTERMEDIATE, FEBS letters, 408(3), 1997, pp. 281-284
We report the sequence of the cDNA encoding human L-3-phosphoserine ph
osphatase, The encoded polypeptide contains 225 residues and shows 30%
sequence identity with the Escherichia coli enzyme, The human protein
was expressed in a bacterial expression system and purified, Similar
to known L-3-phosphoserine phosphatases, it catalyzed the Mg2+-depende
nt hydrolysis of L-phosphoserine and an exchange reaction between L-se
rine and L-phosphoserine. In addition we found that the enzyme was pho
sphorylated upon incubation with L-[P-32]phosphoserine, which indicate
s that the reaction mechanism proceeds via the formation of a phosphor
yl-enzyme intermediate, The sensitivity of the phosphoryl-enzyme to al
kali and to hydroxylamine suggests that an aspartyl- or a glutamyl-pho
sphate was formed, The nucleotide sequence of the cDNA described in th
is article has been deposited in the EMBL data base under accession nu
mber Y10275. (C) 1997 Federation of European Biochemical Societies.