| Type: | Family | Name: | 1-aminocyclopropane-1-carboxylate deaminase/D-cysteine desulfhydrase |
| Description: | This entry represents the 1-aminocyclopropane-1-carboxylate deaminase/D-cysteine desulfhydrase family. Proteins in this family include deaminase, D-cysteine desulfhydrase, phenylserine dehydratase and L-cysteate sulfo-lyase. 1-aminocyclopropane-1-carboxylate deaminase () catalyses a cyclopropane ring-opening reaction, the irreversible conversion of 1-aminocyclopropane-1-carboxylate (ACC) to ammonia and alpha-ketobutyrate []. Some plant growth-promoting rhizobacteria can produce 1-aminocyclopropane-1-carboxylate deaminase to enhance plant growth [, ]. D-cysteine desulfhydrase (d-CDes) () catalyses the alpha, beta-elimination reaction of D-cysteine and of several D-cysteine derivatives. The Escherichia coli d-CDes catalyses D-cysteine into pyruvate, H2S, and NH3 [, , ]. The physiological function of bacterial d-CDes is not clear. L-cysteate sulfo-lyase () catalyses the desulfonation and deamination of L-cysteate, yielding pyruvate, sulphite and ammonium. It is involved in a L-cysteate degradation pathway that allows Silicibacter pomeroyi to grow on L-cysteate as the sole source of carbon and energy. To a lesser extent, it can also act on D-cysteine in vitro, leading to the production of pyruvate, sulfide and ammonium []. | Short Name: | ACCD_DCysDesulf |
