Cobalt chelatase are homologous to Mg-chelatase subunits BchH and BchI, respectively. CobT, too, has been found to be remotely related to the third subunit of Mg-chelatase, BchD (involved in bacteriochlorophyll synthesis, e.g., in Rhodobacter capsulatus). This enzyme belongs to the family of ligases, specifically those forming nitrogen-D-metal bonds in coordination complexes. The systematic name of this enzyme class is hydrogenobyrinic-acid-a,c-diamide:cobalt cobalt-ligase (ADP-forming). Other names in common use include hydrogenobyrinic acid a,c-diamide cobaltochelatase, CobNST, and CobNCobST. This enzyme participates in porphyrin and chlorophyll metabolism. Cobalt chelatase Cobalt chelatase () is an enzyme that catalyzes the chemical reaction The 4 substrates of this enzyme
Cobalt aminopeptidase 2, an enzyme that occurs in humans and other mammals that does not use the corrin ring of B, but binds cobalt directly. Another non-corrin cobalt enzyme is nitrile hydratase, an enzyme in bacteria that metabolizes nitriles. Cobalt is an essential element for life in minute amounts. The LD value for soluble cobalt salts has been estimated to be between 150 and 500 mg/kg. In the US, the Occupational Safety and Health Administration (OSHA) has designated a permissible exposure limit (PEL) in the workplace as a time-weighted average (TWA) of 0.1 mg/m. The National Institute for Occupational Safety and