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A new class of phosphotransferases phosphorylated on an aspartate residue in an amino-terminal DXDX(T/V) motif.

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Collet, Jean-François [UCL] Stroobant, Vincent Pirard, M. Delpierre, Ghislain [UCL] Van Schaftingen, Emile [UCL]

When incubated with their substrates, human phosphomannomutase and L-3-phosphoserine phosphatase are known to form phosphoenzymes with chemical characteristics of an acyl-phosphate. The phosphorylated residue in phosphomannomutase has now been identified by mass spectrometry after reduction of the phosphoenzyme with tritiated borohydride and trypsin digestion. It is the first aspartate in a conserved DVDGT motif. Replacement of either aspartate of this motif by asparagine or glutamate resulted in complete inactivation of the enzyme. The same mutations performed in the DXDST motif of L-3-phosphoserine phosphatase also resulted in complete inactivation of the enzyme, except for the replacement of the second aspartate by glutamate, which reduced the activity by only about 40%. This suggests that the first aspartate of the motif is also the phosphorylated residue in L-3-phosphoserine phosphatase. Data banks contained seven other phosphomutases or phosphatases sharing a similar, totally conserved DXDX(T/V) motif at their amino terminus. One of these (beta-phosphoglucomutase) is shown to form a phosphoenzyme with the characteristics of an acyl-phosphate. In conclusion, phosphomannomutase and L-3-phosphoserine phosphatase belong to a new phosphotransferase family with an amino-terminal DXDX(T/V) motif that serves as an intermediate phosphoryl acceptor.

Document type Article de périodique (Journal article) – Journal Article, Research Support, Non-U.S. Gov't
Access type Accès restreint
Publication date 1998
Journal information "The Journal of biological chemistry" - Vol. 273, no. 23, p. 14107-12 (1998)
Peer reviewed yes
issn 0021-9258
Publication status Publié
Affiliation UCL - MD/BICL - Département de biochimie et de biologie cellulaire
MESH Subject Amino Acid Sequence ; Aspartic Acid - chemistry ; Bacterial Proteins - chemistry ; Borohydrides - metabolism ; Conserved Sequence ; Databases, Factual ; Humans ; Hydrolases - chemistry ; Lactobacillus - enzymology ; Mass Spectrometry ; Molecular Sequence Data ; Mutagenesis, Site-Directed - genetics ; Peptide Fragments - chemistry ; Phosphoric Monoester Hydrolases - chemistry - genetics ; Phosphorylation ; Phosphotransferases - chemistry - genetics ; Phosphotransferases (Phosphomutases) - chemistry - genetics ; Recombinant Proteins - chemistry ; Sequence Alignment ; Trypsin - metabolism
Links
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Bibliographic reference Collet, Jean-François ; Stroobant, Vincent ; Pirard, M. ; Delpierre, Ghislain ; Van Schaftingen, Emile. A new class of phosphotransferases phosphorylated on an aspartate residue in an amino-terminal DXDX(T/V) motif.. In: The Journal of biological chemistry, Vol. 273, no. 23, p. 14107-12 (1998)
Permanent URL http://hdl.handle.net/2078.1/21992