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, 408 (3), 281-4

Human L-3-phosphoserine Phosphatase: Sequence, Expression and Evidence for a Phosphoenzyme Intermediate

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Human L-3-phosphoserine Phosphatase: Sequence, Expression and Evidence for a Phosphoenzyme Intermediate

J F Collet et al. FEBS Lett.

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.

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