Ontology highlight
ABSTRACT:
SUBMITTER: Kim S
PROVIDER: S-EPMC4595758 | biostudies-literature | 2015 Sep
REPOSITORIES: biostudies-literature
Kim Sangwoo S Jang Yu-Sin YS Ha Sung-Chul SC Ahn Jae-Woo JW Kim Eun-Jung EJ Lim Jae Hong JH Cho Changhee C Ryu Yong Shin YS Lee Sung Kuk SK Lee Sang Yup SY Kim Kyung-Jin KJ
Nature communications 20150922
Thiolase is the first enzyme catalysing the condensation of two acetyl-coenzyme A (CoA) molecules to form acetoacetyl-CoA in a dedicated pathway towards the biosynthesis of n-butanol, an important solvent and biofuel. Here we elucidate the crystal structure of Clostridium acetobutylicum thiolase (CaTHL) in its reduced/oxidized states. CaTHL, unlike those from other aerobic bacteria such as Escherichia coli and Zoogloea ramegera, is regulated by the redox-switch modulation through reversible disu ...[more]