Precorrin-6A synthase (deacetylating)

Precorrin-6A synthase (deacetylating) is an enzyme that catalyzes a specific step in the biosynthesis of cobalamin (vitamin B12). It is involved in the conversion of precorrin-6A to precorrin-6X. This enzymatic reaction involves the removal of an acetyl group from precorrin-6A.

Specifically, Precorrin-6A synthase (deacetylating) is classified as a hydrolase, acting on carbon-oxygen bonds. Its systematic name is precorrin-6A acetylhydrolase. The enzyme's activity is crucial for the proper progression of the corrin ring formation, a key structural component of cobalamin. The removal of the acetyl group is essential for subsequent modifications and ultimately, the formation of the complete cobalamin molecule.

The enzyme is found in microorganisms, particularly in bacteria that synthesize cobalamin. Its detailed structure and mechanism have been the subject of biochemical investigations. Understanding the function and regulation of Precorrin-6A synthase (deacetylating) is important for comprehending the complete biosynthetic pathway of cobalamin and potential applications in biotechnology and medicine related to vitamin B12 production and metabolic engineering.