Journal
NATURE CHEMICAL BIOLOGY
Volume 8, Issue 11, Pages 887-889Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/NCHEMBIO.1065
Keywords
-
Categories
Funding
- US National Institutes of Health [R01 CA1403160]
Ask authors/readers for more resources
Mutations in an enzyme can result in a neomorphic catalytic activity in cancers. We applied cancer-associated mutations from isocitrate dehydrogenases to homologous residues in the active sites of homoisocitrate dehydrogenases to derive enzymes that catalyze the conversion of 2-oxoadipate to (R)-2-hydroxyadipate, a critical step for adipic acid production. Thus, we provide a prototypic example of how insights from cancer genome sequencing and functional studies can aid in enzyme redesign.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available