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Cobalt chelatase
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Cobalt chelatase () is an that the chemical reaction

ATP + hydrogenobyrinic acid a,c-diamide + Co2+ + H2O \rightleftharpoons ADP + phosphate + cob(II)yrinic acid a,c-diamide + H+

The four substrates of this enzyme are ATP, hydrogenobyrinic acid a,c-diamide, 2+, and ; its four products are ADP, , cob(II)yrinic acid a,c-diamide, and .

The aerobic cobalt chelatase (aerobic cobalamin biosynthesis pathway) consists of three subunits, CobT, CobN () and CobS ().

The of vitamin B12 can be complexed with metal via the ATP-dependent reactions in the aerobic pathway (e.g., in Pseudomonas denitrificans) or via ATP-independent reactions of in the anaerobic pathway (e.g., in Salmonella typhimurium). The corresponding cobalt chelatases are not homologous. However, aerobic cobalt chelatase subunits CobN and CobS 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 , 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 is part of the biosynthetic pathway to cobalamin (vitamin B12) in .


See also
  • Cobalamin biosynthesis


Further reading
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