PTP NE‐6: A Brain‐Enriched Receptor‐Type Protein Tyrosine Phosphatase with a Divergent Catalytic Domain

: A receptor‐type protein tyrosine phosphatase, PTP NE‐6, was identified from rat olfactory epithelial cDNA and cloned from a rat brain cDNA library. PTP NE‐6 mRNA is abundant in brain and expressed at lower levels in olfactory tissue and adrenal gland. In situ hybridization demonstrates that PTP NE...

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Bibliographic Details
Published in:Journal of neurochemistry 1997-05, Vol.68 (5), p.1820-1829
Main Authors: Fitzgerald, Laura Rydelek, Walton, Kevin M., Dixon, Jack E., Largent, Brian L.
Format: Article
Language:English
Subjects:
Adrenal
Amino Acid Sequence
Animals
Base Sequence
Biological and medical sciences
Brain - metabolism
Catalysis
Cloning, Molecular
Fundamental and applied biological sciences. Psychology
Genes. Genome
Molecular and cellular biology
Molecular genetics
Molecular Sequence Data
Olfactory
Protein tyrosine phosphatase
Protein Tyrosine Phosphatases - genetics
Protein Tyrosine Phosphatases - metabolism
Rat
Rats
Receptor-Like Protein Tyrosine Phosphatases, Class 8
Tissue Distribution
Citations: Items that cite this one
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Summary:: A receptor‐type protein tyrosine phosphatase, PTP NE‐6, was identified from rat olfactory epithelial cDNA and cloned from a rat brain cDNA library. PTP NE‐6 mRNA is abundant in brain and expressed at lower levels in olfactory tissue and adrenal gland. In situ hybridization demonstrates that PTP NE‐6 mRNA is expressed throughout the brain, with highest levels in the medial habenula and at intermediate levels in layer IV of cortex, medial geniculate nucleus, inferior colliculus, hypothalamus, and thalamus. The predicted amino acid sequence demonstrates that PTP NE‐6 contains a single catalytic domain that diverges from the consensus protein tyrosine phosphatase catalytic domain by expressing an aspartate instead of the conserved alanine residue in the catalytic site. Recombinantly expressed PTP NE‐6 does not exhibit detectable phosphatase activity. Upon mutation of the aspartate to the consensus alanine, phosphatase activity toward p‐nitrophenyl phosphate is observable with a kcat value of 3.7 s−1 and a Km of 980 µM. These data demonstrate that the inactivity of native PTP NE‐6 toward p‐nitrophenyl phosphate is due to the divergent aspartate in the catalytic site and not to variant amino acids within the phosphatase domain.
ISSN:0022-3042
1471-4159
DOI:10.1046/j.1471-4159.1997.68051820.x