Human L-3-phosphoserine phosphatase: sequence, expression and evidence for a phosphoenzyme intermediate
(1997) FEBS Letters — Vol. 408, n° 3, p. 281-284 (1997)
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- Authors
Rider, Mark H. 
- 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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Citations
Collet, J.-F., Gerin, I., Rider, M. H., Veiga da Cunha, M., & Van Schaftingen, E. (1997). Human L-3-phosphoserine phosphatase: sequence, expression and evidence for a phosphoenzyme intermediate. FEBS Letters, 408(3), 281-284. https://doi.org/10.1016/S0014-5793(97)00438-9 (Original work published 1997)