Ontology highlight
ABSTRACT:
SUBMITTER: Pei XY
PROVIDER: S-EPMC2855724 | biostudies-literature | 2010 Mar
REPOSITORIES: biostudies-literature
Pei Xue-Yuan XY Erixon Karl M KM Luisi Ben F BF Leeper Finian J FJ
Biochemistry 20100301 8
Pyruvate decarboxylase (PDC) uses thiamine diphosphate as an essential cofactor to catalyze the formation of acetaldehyde on the pathway of ethanol synthesis. Here we report the crystallographic image of a prereaction intermediate of a bacterial pyruvate decarboxylase prepared by cocrystallizing the enzyme with pyruvate and a stable analogue of the cofactor's activated ylid form. A second crystal structure of PDC in complex with fluoride shows that the ion organizes a water molecule that occlude ...[more]