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    Expression, purification, and characterization of thymidylate synthase from Lactococcus lactis

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    Authors
    Greene, Patricia J.
    Yu, Pak-Lam
    Zhao, Jia
    Schiffer, Celia A.
    Santi, Daniel V.
    UMass Chan Affiliations
    Department of Biochemistry and Molecular Pharmacology
    Document Type
    Journal Article
    Publication Date
    1994-07-01
    Keywords
    Amino Acid Sequence
    Binding Sites
    Crystallization
    Escherichia coli
    *Gene Expression
    Hydrogen-Ion Concentration
    Lactococcus lactis
    Models, Molecular
    Molecular Sequence Data
    Molecular Structure
    Osmolar Concentration
    Recombinant Proteins
    Structure-Activity Relationship
    Thymidylate Synthase
    Biochemistry, Biophysics, and Structural Biology
    Pharmacology, Toxicology and Environmental Health
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    Link to Full Text
    http://dx.doi.org/10.1002/pro.5560030715
    Abstract
    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.
    Source
    Protein Sci. 1994 Jul;3(7):1114-6. Link to article on publisher's site
    DOI
    10.1002/pro.5560030715
    Permanent Link to this Item
    http://hdl.handle.net/20.500.14038/25974
    PubMed ID
    7920258
    Related Resources
    Link to Article in PubMed
    ae974a485f413a2113503eed53cd6c53
    10.1002/pro.5560030715
    Scopus Count
    Collections
    UMass Chan Faculty and Researcher Publications
    Schiffer Lab Publications

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