Article
Structural basis for the activity of two muconate cycloisomerase variants toward substituted muconates.
Proteins - 1 Jan 1999
Schell U, Helin S, Kajander T, Schlömann M, Goldman A
Abstract excerpt
We have refined to 2.3 A resolution two muconate cycloisomerase (MCIase) variant structures, F329I and I54V, that differ from each other and from wild-type in their activity toward cis,cis-muconate (CCM) and substituted CCMs. The working and free R-factors for F329I are 17.4/21.6% and for I54V, 17.6/22.3% with good stereochemistry. Except for the mutated residue, there are no significant changes in structure. To...
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