Source:http://linkedlifedata.com/resource/pubmed/id/12423352
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
22
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| pubmed:dateCreated |
2002-11-8
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| pubmed:databankReference | |
| pubmed:abstractText |
The gene encoding a subtilisin-like serine proteinase in the psychrotrophic Vibrio sp. PA44 has been successfully cloned, sequenced and expressed in Escherichia coli. The gene is 1593 basepairs and encodes a precursor protein of 530 amino acid residues with a calculated molecular mass of 55.7 kDa. The enzyme is isolated, however, as an active 40.6-kDa proteinase, without a 139 amino acid residue N-terminal prosequence. Under mild conditions the enzyme undergoes a further autocatalytic cleavage to give a 29.7-kDa proteinase that retains full enzymatic activity. The deduced amino acid sequence of the enzyme has high homology to proteinases of the proteinase K family of subtilisin-like proteinases. With respect to the enzyme characteristics compared in this study the properties of the wild-type and recombinant proteinases are the same. Sequence analysis revealed that especially with respect to the thermophilic homologues, aqualysin I from Thermus aquaticus and a proteinase from Thermus strain Rt41A, the cold-adapted Vibrio-proteinase has a higher content of polar/uncharged amino acids, as well as aspartate residues. The thermophilic enzymes had a higher content of arginines, and relatively higher number of hydrophobic amino acids and a higher aliphatic index. These factors may contribute to the adaptation of these proteinases to different temperature conditions.
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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/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/Endopeptidase K,
http://linkedlifedata.com/resource/pubmed/chemical/Guanidine,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/Phenylmethylsulfonyl Fluoride,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Serine Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Subtilisin
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| pubmed:status |
MEDLINE
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| pubmed:month |
Nov
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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 |
5536-46
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| pubmed:dateRevised |
2008-11-21
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| pubmed:meshHeading |
pubmed-meshheading:12423352-Amino Acid Sequence,
pubmed-meshheading:12423352-Base Sequence,
pubmed-meshheading:12423352-Binding Sites,
pubmed-meshheading:12423352-Cold Temperature,
pubmed-meshheading:12423352-DNA,
pubmed-meshheading:12423352-Dose-Response Relationship, Drug,
pubmed-meshheading:12423352-Endopeptidase K,
pubmed-meshheading:12423352-Escherichia coli,
pubmed-meshheading:12423352-Guanidine,
pubmed-meshheading:12423352-Kinetics,
pubmed-meshheading:12423352-Ligands,
pubmed-meshheading:12423352-Molecular Sequence Data,
pubmed-meshheading:12423352-Phenylmethylsulfonyl Fluoride,
pubmed-meshheading:12423352-Protein Denaturation,
pubmed-meshheading:12423352-Protein Structure, Tertiary,
pubmed-meshheading:12423352-Recombinant Proteins,
pubmed-meshheading:12423352-Sequence Homology, Amino Acid,
pubmed-meshheading:12423352-Serine Endopeptidases,
pubmed-meshheading:12423352-Subtilisin,
pubmed-meshheading:12423352-Vibrio
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| pubmed:year |
2002
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| pubmed:articleTitle |
Characterization of a cloned subtilisin-like serine proteinase from a psychrotrophic Vibrio species.
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| pubmed:affiliation |
Institute of Biology, University of Iceland; and Department of Biochemistry, Science Institute, University of Iceland, Reykjavik, Iceland.
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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