Ontology highlight
ABSTRACT:
SUBMITTER: Buddrus L
PROVIDER: S-EPMC5012210 | biostudies-literature | 2016 Sep
REPOSITORIES: biostudies-literature
Buddrus Lisa L Andrews Emma S V ES Leak David J DJ Danson Michael J MJ Arcus Vickery L VL Crennell Susan J SJ
Acta crystallographica. Section F, Structural biology communications 20160826 Pt 9
Pyruvate decarboxylase (PDC; EC 4.1.1.1) is a thiamine pyrophosphate- and Mg(2+) ion-dependent enzyme that catalyses the non-oxidative decarboxylation of pyruvate to acetaldehyde and carbon dioxide. It is rare in bacteria, but is a key enzyme in homofermentative metabolism, where ethanol is the major product. Here, the previously unreported crystal structure of the bacterial pyruvate decarboxylase from Zymobacter palmae is presented. The crystals were shown to diffract to 2.15 Å resolution. They ...[more]