Human L-3-phosphoserine phosphatase: sequence, expression and evidence for a phosphoenzyme intermediate.
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Collet JF, Gerin I, Rider MH, Veiga-da-Cunha M, Van Schaftingen E
Human L-3-phosphoserine phosphatase: sequence, expression and evidence for a phosphoenzyme intermediate.
FEBS Lett. 1997 May 26;408(3):281-4.
- PubMed ID
- 9188776 [ View in PubMed]
- Abstract
We report the sequence of the cDNA encoding human L-3-phosphoserine phosphatase. 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(+)-dependent hydrolysis of L-phosphoserine and an exchange reaction between L-serine and L-phosphoserine. In addition we found that the enzyme was phosphorylated upon incubation with L-[32P]phosphoserine, which indicates that the reaction mechanism proceeds via the formation of a phosphoryl-enzyme intermediate. The sensitivity of the phosphoryl-enzyme to alkali and to hydroxylamine suggests that an aspartyl- or a glutamyl-phosphate was formed. The nucleotide sequence of the cDNA described in this article has been deposited in the EMBL data base under accession number Y10275.