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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
2005-2-17
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pubmed:abstractText |
Myo-inositol monophosphate phosphatase (IMPP) is a key enzyme in the phosphoinositide cell-signaling system. This study found that incubating the IMPP from a porcine brain with pyridoxal-5'-phosphate (PLP) resulted in a time-dependent enzymatic inactivation. Spectral evidence showed that the inactivation proceeds via the formation of a Schiff's base with the amino groups of the enzyme. After the sodium borohydride reduction of the inactivated enzyme, it was observed that 1.8 mol phosphopyridoxyl residues per mole of the enzyme dimer were incorporated. The substrate, myo-inositol-1-phosphate, protected the enzyme against inactivation by PLP. After tryptic digestion of the enzyme modified with PLP, a radioactive peptide absorbing at 210 nm was isolated by reverse-phase HPLC. Amino acid sequencing of the peptide identified a portion of the PLP-binding site as being the region containing the sequence L-Q-V-S-Q-Q-E-D-I-T-X, where X indicates that phenylthiohydantoin amino acid could not be assigned. However, the result of amino acid composition of the peptide indicated that the missing residue could be designated as a phosphopyridoxyl lysine. This suggests that the catalytic function of IMPP is modulated by the binding of PLP to a specific lysyl residue at or near its substrate-binding site of the protein.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Amino Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Borohydrides,
http://linkedlifedata.com/resource/pubmed/chemical/Inositol Phosphates,
http://linkedlifedata.com/resource/pubmed/chemical/Lysine,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Phenylthiohydantoin,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoric Monoester Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Pyridoxal Phosphate,
http://linkedlifedata.com/resource/pubmed/chemical/inositol 1-phosphate,
http://linkedlifedata.com/resource/pubmed/chemical/myo-inositol-1 (or...,
http://linkedlifedata.com/resource/pubmed/chemical/sodium borohydride
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
1225-8687
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pubmed:author |
pubmed-author:AnJae JinJJ,
pubmed-author:ChoSung-WooSW,
pubmed-author:ChoiHee SoonHS,
pubmed-author:ChoiSoo HyunSH,
pubmed-author:ChoiSoo YoungSY,
pubmed-author:EumWon SikWS,
pubmed-author:HongJoung WooJW,
pubmed-author:KimDae WonDW,
pubmed-author:KimSo YoungSY,
pubmed-author:KwonHyeok YilHY,
pubmed-author:KwonOh-ShinOS,
pubmed-author:LeeByung RyongBR,
pubmed-author:LeeKil SooKS,
pubmed-author:LeeSeung ReeSR,
pubmed-author:LeeSun HwaSH,
pubmed-author:ParkJinseuJ
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pubmed:issnType |
Print
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pubmed:day |
31
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pubmed:volume |
38
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
58-64
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:15715947-Amino Acids,
pubmed-meshheading:15715947-Animals,
pubmed-meshheading:15715947-Binding Sites,
pubmed-meshheading:15715947-Borohydrides,
pubmed-meshheading:15715947-Brain,
pubmed-meshheading:15715947-Catalysis,
pubmed-meshheading:15715947-Chromatography, High Pressure Liquid,
pubmed-meshheading:15715947-Enzyme Activation,
pubmed-meshheading:15715947-Inositol Phosphates,
pubmed-meshheading:15715947-Lysine,
pubmed-meshheading:15715947-Oxidation-Reduction,
pubmed-meshheading:15715947-Peptide Fragments,
pubmed-meshheading:15715947-Phenylthiohydantoin,
pubmed-meshheading:15715947-Phosphoric Monoester Hydrolases,
pubmed-meshheading:15715947-Protein Binding,
pubmed-meshheading:15715947-Pyridoxal Phosphate,
pubmed-meshheading:15715947-Swine,
pubmed-meshheading:15715947-Time Factors
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pubmed:year |
2005
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pubmed:articleTitle |
Inactivation of brain myo-inositol monophosphate phosphatase by pyridoxal-5'-phosphate.
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pubmed:affiliation |
Department of Genetic Engineering and Research Institute for Bioscience and Biotechnology, Hallym University, Chunchon 200-702, Korea.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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