Enzyme redesign guided by cancer-derived IDH1 mutations.

Published

Journal Article

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.

Full Text

Duke Authors

Cited Authors

  • Reitman, ZJ; Choi, BD; Spasojevic, I; Bigner, DD; Sampson, JH; Yan, H

Published Date

  • November 2012

Published In

Volume / Issue

  • 8 / 11

Start / End Page

  • 887 - 889

PubMed ID

  • 23001033

Pubmed Central ID

  • 23001033

Electronic International Standard Serial Number (EISSN)

  • 1552-4469

International Standard Serial Number (ISSN)

  • 1552-4450

Digital Object Identifier (DOI)

  • 10.1038/nchembio.1065

Language

  • eng