Ontology highlight
ABSTRACT:
SUBMITTER: Chauliac D
PROVIDER: S-EPMC7679959 | biostudies-literature | 2020 Dec
REPOSITORIES: biostudies-literature
Chauliac Diane D Wang Qingzhao Q St John Franz J FJ Jones Grace G Hurlbert Jason C JC Ingram Lonnie O LO Shanmugam Keelnatham T KT
Protein science : a publication of the Protein Society 20201024 12
During adaptive metabolic evolution a native glycerol dehydrogenase (GDH) acquired a d-lactate dehydrogenase (LDH) activity. Two active-site amino acid changes were detected in the altered protein. Biochemical studies along with comparative structure analysis using an X-ray crystallographic structure model of the protein with the two different amino acids allowed prediction of pyruvate binding into the active site. We propose that the F245S alteration increased the capacity of the glycerol bindi ...[more]