NDLI: Expression, purification, and characterization of thymidylate synthase from Lactococcus lactis.

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

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

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Yu, P. L. Schiffer, C. A. Zhao, J. Santi, D. Greene, P. J.
Description	Author Affiliation: Greene PJ ( Department of Biochemistry, University of California, San Francisco 94143.)
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.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	7
Volume Number	3
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	1994-07-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Gene Expression Lactococcus Lactis Enzymology Thymidylate Synthase Genetics Amino Acid Sequence Binding Sites Crystallization Escherichia Coli Hydrogen-ion Concentration Models, Molecular Molecular Sequence Data Molecular Structure Osmolar Concentration Recombinant Proteins Structure-activity Relationship Chemistry Isolation & Purification Research Support, U.s. Gov't, P.h.s. Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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