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Catalysis of serine oligopeptidases is controlled by a gating filter mechanism
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UNSPECIFIED (2000) Catalysis of serine oligopeptidases is controlled by a gating filter mechanism. EMBO REPORTS, 1 (3). pp. 277-281. doi:10.1093/embo-reports/kvd048 ISSN 1469-221X.
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Official URL: http://dx.doi.org/10.1093/embo-reports/kvd048
Abstract
Proteases have a variety of strategies for selecting substrates in order to prevent uncontrolled protein degradation. A recent crystal structure determination of prolyl oligopeptidase has suggested a way for substrate selection involving an unclosed seven-bladed beta -propeller domain. We have engineered a disulfide bond between the first and seventh blades of the propeller, which resulted in the loss of enzymatic activity. These results provided direct evidence for a novel strategy of regulation in which oscillating propeller blades act as a gating filter during catalysis, letting small peptide substrates into the active site while excluding large proteins to prevent accidental proteolysis.
Item Type: | Journal Article | ||||
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Subjects: | Q Science > QD Chemistry Q Science > QH Natural history > QH301 Biology |
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Journal or Publication Title: | EMBO REPORTS | ||||
Publisher: | OXFORD UNIV PRESS | ||||
ISSN: | 1469-221X | ||||
Official Date: | September 2000 | ||||
Dates: |
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Volume: | 1 | ||||
Number: | 3 | ||||
Number of Pages: | 5 | ||||
Page Range: | pp. 277-281 | ||||
DOI: | 10.1093/embo-reports/kvd048 | ||||
Publication Status: | Published |
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