Ontology highlight
ABSTRACT:
SUBMITTER: Dym O
PROVIDER: S-EPMC16878 | biostudies-literature | 2000 Aug
REPOSITORIES: biostudies-literature
Dym O O Pratt E A EA Ho C C Eisenberg D D
Proceedings of the National Academy of Sciences of the United States of America 20000801 17
d-Lactate dehydrogenase (d-LDH) of Escherichia coli is a peripheral membrane respiratory enzyme involved in electron transfer, located on the cytoplasmic side of the inner membrane. d-LDH catalyzes the oxidation of d-lactate to pyruvate, which is coupled to transmembrane transport of amino acids and sugars. Here we describe the crystal structure at 1.9 A resolution of the three domains of d-LDH: the flavin adenine dinucleotide (FAD)-binding domain, the cap domain, and the membrane-binding domain ...[more]