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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
1992-1-24
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pubmed:abstractText |
Highly purified preparations of signal peptidase I (36 kDa) were found to undergo an apparent inter-autocatalytic degradation at 4 degrees C and 37 degrees C. The disappearance of the 36 kDa protein coincided with the stable appearance of a 31 kDa and a 5 kDa species. Amino-terminal sequencing of the 31 kDa product indicated a site specific cleavage following Ala38-Gln-Ala of signal peptidase I. The 31 kDa fragment was purified and shown to have 100-fold less activity than the native enzyme, with pre-maltose binding protein as a substrate.
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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/ATP-Binding Cassette Transporters,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Maltose-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Monosaccharide Transport Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Protease Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Precursors,
http://linkedlifedata.com/resource/pubmed/chemical/Serine Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/maltose transport system, E coli,
http://linkedlifedata.com/resource/pubmed/chemical/type I signal peptidase
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0006-291X
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
16
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pubmed:volume |
181
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
650-6
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:1755848-ATP-Binding Cassette Transporters,
pubmed-meshheading:1755848-Amino Acid Sequence,
pubmed-meshheading:1755848-Carrier Proteins,
pubmed-meshheading:1755848-Endopeptidases,
pubmed-meshheading:1755848-Escherichia coli,
pubmed-meshheading:1755848-Escherichia coli Proteins,
pubmed-meshheading:1755848-Kinetics,
pubmed-meshheading:1755848-Maltose-Binding Proteins,
pubmed-meshheading:1755848-Membrane Proteins,
pubmed-meshheading:1755848-Molecular Sequence Data,
pubmed-meshheading:1755848-Molecular Weight,
pubmed-meshheading:1755848-Monosaccharide Transport Proteins,
pubmed-meshheading:1755848-Peptide Fragments,
pubmed-meshheading:1755848-Protease Inhibitors,
pubmed-meshheading:1755848-Protein Precursors,
pubmed-meshheading:1755848-Serine Endopeptidases
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pubmed:year |
1991
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pubmed:articleTitle |
Inter-molecular degradation of signal peptidase I in vitro.
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pubmed:affiliation |
Wellcome Research Laboratories, Department of Molecular Genetics and Microbiology, Research Triangle Park, NC 27709.
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pubmed:publicationType |
Journal Article
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