Reinvestigation of the roles of the carboxyl groups of glutathione with yeast glyoxalase I : Implications as to the mechanism and coenzymic role of glutathione
dc.contributor.author | D'Silva, Claudius | en_US |
dc.date.accessioned | 2006-04-07T19:28:40Z | |
dc.date.available | 2006-04-07T19:28:40Z | |
dc.date.issued | 1986-07-07 | en_US |
dc.identifier.citation | D'Silva, Claudius (1986/07/07)."Reinvestigation of the roles of the carboxyl groups of glutathione with yeast glyoxalase I : Implications as to the mechanism and coenzymic role of glutathione." FEBS Letters 202(2): 240-244. <http://hdl.handle.net/2027.42/26104> | en_US |
dc.identifier.uri | http://www.sciencedirect.com/science/article/B6T36-44PFRHG-1T/2/68e26344704fd525b3f5be2eacaadfcf | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/26104 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=3522272&dopt=citation | en_US |
dc.description.abstract | A number of carboxyl-substituted s-blocked glutathiones have been shown to be competitive inhibitors of yeast glyoxalase I at 25[deg]C, pH 6.6. Amidation of the glycyl carboxyl group of S-(p-bromobenzyl)glutathione has no appreciable effect on binding whilst methylation reduces binding by 8.9-fold, indicating a steric constraint and the possible presence of a hydrogen bond in this region of the enzyme. Amidation of both carboxyl groups of S-(p-bromobenzyl)glutathione reduces binding significantly by 237-fold; this result agrees with electrostatic interaction of the Glu COO- group with a group located within the enzyme surface as opposed to the Gly COO- group, previously proposed. | en_US |
dc.format.extent | 379120 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 | Reinvestigation of the roles of the carboxyl groups of glutathione with yeast glyoxalase I : Implications as to the mechanism and coenzymic role of glutathione | 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 Biological Chemistry, The University of Michigan, Ann Arbor, MI 48109, USA | en_US |
dc.identifier.pmid | 3522272 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/26104/1/0000180.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1016/0014-5793(86)80694-9 | en_US |
dc.identifier.source | FEBS Letters | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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