期刊论文详细信息
| FEBS Letters | |
| A consensus sequence for substrate hydrolysis by rhino virus 3C proteinase | |
| Dunn, Ben M.1  Orr, David C.3  Long, Audrey C.2  Kay, John2  Cameron, Janet M.3  | |
| [1] Dept. of Biochemistry & Mol. Biology, J. Hillis Miller Health Centre, University of Florida, Gainesville, FL 32610, USA;Dept. of Biochemistry, University of Wales College of Cardiff. PO Box 903, Cardiff CF1 1ST, WalesUK;Virology Division, Glaxo Group Research Ltd, Greenford, Middlesex UB6 OHE, England | |
| 关键词: Rhinovirus proteinase; Synthetic substrate; Specificity; Minimum requirement; | |
| DOI : 10.1016/0014-5793(89)81619-9 | |
| 学科分类:生物化学/生物物理 | |
| 来源: John Wiley & Sons Ltd. | |
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【 摘 要 】
Kinetic constants were determined for the hydrolysis of a series of synthetic peptide substrates by recombinant rhinovirus (HRV 14) 3C proteinase. Systematic removal or replacement of individual residues indicated that the minimum sequence required for effective cleavage by the viral cysteine proteinase was P5-Val/Thr-P3-P2-Gln-Gly-Pro.
【 授权许可】
Unknown
【 预 览 】
| Files | Size | Format | View |
|---|---|---|---|
| RO201912020292793ZK.pdf | 372KB |
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