Exploring the selenium-over-sulfur substrate specificity and kinetics of a bacterial selenocysteine lyase.

ABSTRACT: Selenium is a vital micronutrient in many organisms. While traces are required for microbial utilization, excess amounts are toxic; thus, selenium can be regarded as a biological double-edged sword. Selenium is chemically similar to the essential element sulfur, but curiously, evolution has selected the former over the latter for a subset of oxidoreductases. Enzymes involved in sulfur metabolism are less discriminate in terms of preventing selenium incorporation; however, its specific incorporation into selenoproteins reveals a highly discriminate process that is not completely understood. We have identified SclA, a NifS-like protein in the nosocomial pathogen, Enterococcus faecalis, and characterized its enzymatic activity and specificity for l-selenocysteine over l-cysteine. It is known

SUBMITTER: Johnstone MA 

PROVIDER: S-EPMC8833086 | biostudies-literature | 2021 Mar

REPOSITORIES: biostudies-literature