Source:http://linkedlifedata.com/resource/pubmed/id/11574069
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
4
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| pubmed:dateCreated |
2001-9-27
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| pubmed:abstractText |
Mitochondrial processing peptidase (MPP) specifically cleaves off the N-terminal presequence of the mitochondrial protein precursor. Previous studies demonstrated that Arg at position -2 from the cleavage site, which is found among many precursors, plays a critical role in recognition by MPP. We analyzed the structural elements of bovine cytochrome P450 side-chain cleavage enzyme precursor [pre-P450(SCC)], which has Ala at position -2, for recognition by MPP. Replacement of Ala position -2 of pre-P450(SCC) with Arg resulted in an increase in the cleavage rate. Replacement with Gly caused a reduction in the cleavage rate and the appearance of an additional cleavage site downstream of the authentic site. A pre-P450(SCC) mutant with Met at position -2 retained cleavage efficiency equal to that of the wild type. These results indicate that -2 Ala of pre-P450(SCC) is recognized by MPP as a determinant for precise cleavage, and that the amino acid at -2 is required to have a straight methylene chain for interaction with the S(2) site. The preference for distal basic residues, a hydrophobic residue at +1, and hydroxyl residues at +2 and +3, was almost the same as those of the precursors with Arg at -2, indicating that the recognition mechanism of pre-P450(SCC) by MPP is essentially the same as that of the precursors with Arg at position -2.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Arginine,
http://linkedlifedata.com/resource/pubmed/chemical/Cholesterol Side-Chain Cleavage...,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Precursors,
http://linkedlifedata.com/resource/pubmed/chemical/Metalloendopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/mitochondrial processing peptidase
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| pubmed:status |
MEDLINE
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| pubmed:month |
Oct
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| pubmed:issn |
0021-924X
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| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
130
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| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
497-502
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| pubmed:dateRevised |
2007-12-19
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| pubmed:meshHeading |
pubmed-meshheading:11574069-Amino Acid Motifs,
pubmed-meshheading:11574069-Amino Acid Sequence,
pubmed-meshheading:11574069-Amino Acid Substitution,
pubmed-meshheading:11574069-Animals,
pubmed-meshheading:11574069-Arginine,
pubmed-meshheading:11574069-Binding Sites,
pubmed-meshheading:11574069-Catalytic Domain,
pubmed-meshheading:11574069-Cattle,
pubmed-meshheading:11574069-Cholesterol Side-Chain Cleavage Enzyme,
pubmed-meshheading:11574069-Enzyme Precursors,
pubmed-meshheading:11574069-Kinetics,
pubmed-meshheading:11574069-Metalloendopeptidases,
pubmed-meshheading:11574069-Mitochondria,
pubmed-meshheading:11574069-Molecular Sequence Data,
pubmed-meshheading:11574069-Mutation,
pubmed-meshheading:11574069-Protein Processing, Post-Translational,
pubmed-meshheading:11574069-Sequence Alignment,
pubmed-meshheading:11574069-Structure-Activity Relationship,
pubmed-meshheading:11574069-Substrate Specificity
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| pubmed:year |
2001
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| pubmed:articleTitle |
Recognition of mitochondrial protein precursor lacking arginine at position -2 by mitochondrial processing peptidase: processing of bovine cytochrome P450(SCC) precursor.
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| pubmed:affiliation |
Department of Chemistry, Faculty of Science, Kyushu University, Fukuoka 812-8581, Japan.
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|