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dc.contributor.authorGreene, Patricia J.
dc.contributor.authorYu, Pak-Lam
dc.contributor.authorZhao, Jia
dc.contributor.authorSchiffer, Celia A.
dc.contributor.authorSanti, Daniel V.
dc.date2022-08-11T08:08:00.000
dc.date.accessioned2022-08-23T15:38:38Z
dc.date.available2022-08-23T15:38:38Z
dc.date.issued1994-07-01
dc.date.submitted2010-02-05
dc.identifier.citationProtein Sci. 1994 Jul;3(7):1114-6. <a href="http://dx.doi.org/10.1002/pro.5560030715">Link to article on publisher's site</a>
dc.identifier.issn0961-8368 (Print)
dc.identifier.doi10.1002/pro.5560030715
dc.identifier.pmid7920258
dc.identifier.urihttp://hdl.handle.net/20.500.14038/25974
dc.description.abstractThe thymidylate synthase (TS) gene from Lactococcus lactis has been highly expressed in Escherichia coli. The TS protein was purified by sequential chromatography on Q-Sepharose and phenyl-Sepharose. Six grams of cell pellet yielded 140 mg of homogeneous TS. TS is a highly conserved enzyme, and several of the conserved amino acid residues that have been implicated in catalytic function are altered in L. lactis TS. By use of a 3-dimensional homology model, we have predicted covariant changes that might compensate for these differences. With the large amounts of L. lactis TS now available, studies can be pursued to understand the structure-function relationships of this enzyme compared to other TSs and to confirm the presumed roles of the compensatory changes predicted in the homology model.
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=7920258&dopt=Abstract">Link to Article in PubMed</a>
dc.relation.urlhttp://dx.doi.org/10.1002/pro.5560030715
dc.subjectAmino Acid Sequence
dc.subjectBinding Sites
dc.subjectCrystallization
dc.subjectEscherichia coli
dc.subject*Gene Expression
dc.subjectHydrogen-Ion Concentration
dc.subjectLactococcus lactis
dc.subjectModels, Molecular
dc.subjectMolecular Sequence Data
dc.subjectMolecular Structure
dc.subjectOsmolar Concentration
dc.subjectRecombinant Proteins
dc.subjectStructure-Activity Relationship
dc.subjectThymidylate Synthase
dc.subjectBiochemistry, Biophysics, and Structural Biology
dc.subjectPharmacology, Toxicology and Environmental Health
dc.titleExpression, purification, and characterization of thymidylate synthase from Lactococcus lactis
dc.typeJournal Article
dc.source.journaltitleProtein science : a publication of the Protein Society
dc.source.volume3
dc.source.issue7
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/bmp_pp/102
dc.identifier.contextkey1134075
html.description.abstract<p>The thymidylate synthase (TS) gene from Lactococcus lactis has been highly expressed in Escherichia coli. The TS protein was purified by sequential chromatography on Q-Sepharose and phenyl-Sepharose. Six grams of cell pellet yielded 140 mg of homogeneous TS. TS is a highly conserved enzyme, and several of the conserved amino acid residues that have been implicated in catalytic function are altered in L. lactis TS. By use of a 3-dimensional homology model, we have predicted covariant changes that might compensate for these differences. With the large amounts of L. lactis TS now available, studies can be pursued to understand the structure-function relationships of this enzyme compared to other TSs and to confirm the presumed roles of the compensatory changes predicted in the homology model.</p>
dc.identifier.submissionpathbmp_pp/102
dc.contributor.departmentDepartment of Biochemistry and Molecular Pharmacology
dc.source.pages1114-6


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