Protein engineering of penicillinase as affinity ligands for bioprocessing
dc.contributor.author | Imanaka, Tadayuki | en_US |
dc.contributor.author | Kuroda, Akio | en_US |
dc.contributor.author | Wang, Henry Y. | en_US |
dc.date.accessioned | 2006-04-07T20:58:13Z | |
dc.date.available | 2006-04-07T20:58:13Z | |
dc.date.issued | 1989 | en_US |
dc.identifier.citation | Imanaka, Tadayuki, Kuroda, Akio, Wang, Henry Y. (1989)."Protein engineering of penicillinase as affinity ligands for bioprocessing." Journal of Fermentation and Bioengineering 67(5): 315-320. <http://hdl.handle.net/2027.42/28176> | en_US |
dc.identifier.uri | http://www.sciencedirect.com/science/article/B6T8G-47FX6JN-36/2/2cf9fb248adef235cd4c387f58900c70 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/28176 | |
dc.description.abstract | The active site and the substrate binding site of penicillinase ([beta]-lactamase) from Bacillus licheniformis were altered in this study so that the enzyme retains the specific binding capability to the [beta]-lactam antibiotics, but fails to hydrolyze them. When Lys47 in the enzyme molecule was replaced by Ala47, the mutant protein PenP(KA) lost not only its catalytic activity but also the substrate binding ability. In contrast, when Ser44 was replaced by Ala, the mutant protein PenP(SA) lost its catalytic activity but still kept the substrate binding ability. It was found that PenP(SA) exhibited the characteristic association and dissociation with penicillin G, but the dissociation constant was much larger than expected. Possible use of this mutant protein as an affinity ligand is also discussed. | en_US |
dc.format.extent | 494047 bytes | |
dc.format.extent | 3118 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.language.iso | en_US | |
dc.publisher | Elsevier | en_US |
dc.title | Protein engineering of penicillinase as affinity ligands for bioprocessing | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Natural Resources and Environment | en_US |
dc.subject.hlbsecondlevel | Molecular, Cellular and Developmental Biology | en_US |
dc.subject.hlbsecondlevel | Ecology and Evolutionary Biology | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Department of Chemical Engineering, The University of Michigan, Ann Arbor, Michigan 48109, U.S.A. | en_US |
dc.contributor.affiliationother | Department of Fermentation Technology, Faculty of Engineering, Osaka University, Yamadaoka, Suita-shi, Osaka 565, Japan | en_US |
dc.contributor.affiliationother | Department of Fermentation Technology, Faculty of Engineering, Osaka University, Yamadaoka, Suita-shi, Osaka 565, Japan | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/28176/1/0000628.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1016/0922-338X(89)90247-X | en_US |
dc.identifier.source | Journal of Fermentation and Bioengineering | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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