Source:http://linkedlifedata.com/resource/pubmed/id/12383260
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
20
|
| pubmed:dateCreated |
2002-10-17
|
| pubmed:databankReference | |
| pubmed:abstractText |
Protein histidine phosphorylation in eukaryotes has been sparsely studied compared to protein serine/threonine and tyrosine phosphorylation. In an attempt to rectify this by probing porcine liver cytosol with the phosphohistidine-containing peptide succinyl-Ala-His(P)-Pro-Phe-p-nitroanilide (phosphopeptide I), we observed a phosphatase activity that was insensitive towards okadaic acid and EDTA. This suggested the existence of a phosphohistidine phosphatase different from protein phosphatase 1, 2A and 2C. A 1000-fold purification to apparent homogeneity gave a 14-kDa phosphatase with a specific activity of 3 micro mol.min-1.mg-1 at pH 7.5 with 7 micro m phosphopeptide I as substrate. Partial amino-acid sequence determination of the purified porcine enzyme by MS revealed similarity with a human sequence representing a human chromosome 9 gene of hitherto unknown function. Molecular cloning from a human embryonic kidney cell cDNA-library followed by expression and purification, yielded a protein with a molecular mass of 13 700 Da, and an EDTA-insensitive phosphohistidine phosphatase activity of 9 micro mol.min-1.mg-1 towards phosphopeptide I. No detectable activity was obtained towards a set of phosphoserine-, phosphothreonine-, and phosphotyrosine peptides. Northern blot analysis indicated that the human phosphohistidine phosphatase mRNA was present preferentially in heart and skeletal muscle. These results provide a new tool for studying eukaryotic histidine phosphorylation/dephosphorylation.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical | |
| pubmed:status |
MEDLINE
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| pubmed:month |
Oct
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| pubmed:issn |
0014-2956
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:volume |
269
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
5016-23
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| pubmed:dateRevised |
2007-11-15
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| pubmed:meshHeading |
pubmed-meshheading:12383260-Amino Acid Sequence,
pubmed-meshheading:12383260-Animals,
pubmed-meshheading:12383260-Base Sequence,
pubmed-meshheading:12383260-Biochemistry,
pubmed-meshheading:12383260-Chromosomes, Human, Pair 9,
pubmed-meshheading:12383260-Cloning, Molecular,
pubmed-meshheading:12383260-Cytosol,
pubmed-meshheading:12383260-Humans,
pubmed-meshheading:12383260-Liver,
pubmed-meshheading:12383260-Mammals,
pubmed-meshheading:12383260-Molecular Sequence Data,
pubmed-meshheading:12383260-Muscle, Skeletal,
pubmed-meshheading:12383260-Myocardium,
pubmed-meshheading:12383260-Phosphopeptides,
pubmed-meshheading:12383260-Phosphoprotein Phosphatases,
pubmed-meshheading:12383260-Phosphorylation,
pubmed-meshheading:12383260-Protein Phosphatase 1,
pubmed-meshheading:12383260-RNA, Messenger,
pubmed-meshheading:12383260-Sequence Analysis, Protein,
pubmed-meshheading:12383260-Sequence Homology, Amino Acid
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| pubmed:year |
2002
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| pubmed:articleTitle |
Identification and characterization of a mammalian 14-kDa phosphohistidine phosphatase.
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| pubmed:affiliation |
Department of Medical Biochemistry and Microbiology, Uppsala University, Uppsala, Sweden.
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|