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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
|
pubmed:dateCreated |
1990-6-11
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pubmed:abstractText |
The amino acid sequences of mammalian purple acid phosphatases and phosphoprotein phosphatases are shown to possess regions of significant homology. The conserved residues contain a high percentage of possible metal-binding residues. The phosphoprotein phosphatases 1, 2A and 2B are proposed to be iron-zinc metalloenzymes with active sites isostructural (or nearly so) with those of the purple phosphatases.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Apr
|
pubmed:issn |
0014-5793
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pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
24
|
pubmed:volume |
263
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pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
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pubmed:pagination |
265-8
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:2159423-Acid Phosphatase,
pubmed-meshheading:2159423-Amino Acid Sequence,
pubmed-meshheading:2159423-Animals,
pubmed-meshheading:2159423-Humans,
pubmed-meshheading:2159423-Metalloproteins,
pubmed-meshheading:2159423-Molecular Sequence Data,
pubmed-meshheading:2159423-Phosphoprotein Phosphatases,
pubmed-meshheading:2159423-Protein Conformation,
pubmed-meshheading:2159423-Sequence Homology, Nucleic Acid
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pubmed:year |
1990
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pubmed:articleTitle |
Sequence homology between purple acid phosphatases and phosphoprotein phosphatases. Are phosphoprotein phosphatases metalloproteins containing oxide-bridged dinuclear metal centers?
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pubmed:affiliation |
University of Virginia, Department of Chemistry, Charlottesville 22901.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.
|