Author

Jennifer J. Schmidt

University of Michigan

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biochemistry· 1 Synthetic Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 1 Research Focus:protein folding & dynamics· 1 Approach:statistical model· 1 Assay:structural biology· 1

Frequent Co-Authors

David H. ShermaniD· 2 shared Aaron M. KeeleriD· 1 shared Andrew N. LowelliD· 1 shared David L. AkeyiD· 1 shared Edward KalkreuteriD· 1 shared Gavin J. WilliamsiD· 1 shared Janet Lynn SmithiD· 1 shared Jeffrey D. Kittendorf· 1 shared

Activity by Year

2021-2024 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 25 mutual co-author links

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2 shared papersBiochemistry

David H. ShermanORCID

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2 papers

Recent·Most cited

Substrate Trapping in Polyketide Synthase Thioesterase Domains: Structural Basis for Macrolactone Formation

Tyler M. McCullough, Vishakha Choudhary, David L. Akey, Meredith A. Skiba, Steffen M. Bernard, Jeffrey D. Kittendorf, Jennifer J. Schmidt, David H. Sherman, Janet Lynn Smith

This study investigates how polyketide synthase thioesterase domains direct substrate nucleophiles for macrolactone formation by analyzing structural and functional properties of modified TEs.

ACS Catalysis · Aug 6, 2024Peer-reviewedBiochemistry

Computationally-guided exchange of substrate selectivity motifs in a modular polyketide synthase acyltransferase

Edward Kalkreuter, Kyle S. Bingham, Aaron M. Keeler, Andrew N. Lowell, Jennifer J. Schmidt, David H. Sherman, Gavin J. Williams

The paper identifies key residues in an acyltransferase that influence substrate selectivity and demonstrates how swapping structural motifs can alter substrate specificity in polyketide synthases.

Nature Communications · Apr 13, 2021Peer-reviewedSynthetic Biology