Cloning, overproduction, and purification of native and mutant recombinant yeast orotate phosphoribosyltransferase and the demonstration from magnetization inversion transfer that a proposed oxocarbocation intermediate does not have a kinetic lifetime.

doi:10.1006/abbi.1998.0971

Article

Cloning, overproduction, and purification of native and mutant recombinant yeast orotate phosphoribosyltransferase and the demonstration from magnetization inversion transfer that a proposed oxocarbocation intermediate does not have a kinetic lifetime.

Archives of biochemistry and biophysics - 1 Jan 1999

Witte J F, Tsou R, McClard R W

Abstract excerpt

The gene for orotate phosphoribosyltransferase from Saccharomyces cerevisiae has been subcloned into an Escherichia coli overexpression vector and the enzyme has been produced in large quantities, thus simplifying the purification to one step. We were able to repeat the published (J. Victor, L. B. Greenberg, and D. L. Sloan J. Biol. Chem. 254, 2647-2655, 1979). 32PPi/5-phosphorylribose 1-alpha-diphosphate...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Cloning, overproduction, and purification of native and mutant recombinant yeast orotate phosphoribosyltransferase and the demonstration from magnetization inversion transfer that a proposed oxocarbocation intermediate does not have a kinetic lifetime.

Abstract excerpt

Topics

Related research