InterPro domain: IPR027278

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 ( 3.5.99.7 ) catalyses a cyclopropane ring-opening reaction, the irreversible conversion of 1-aminocyclopropane-1-carboxylate (ACC) to ammonia and alpha-ketobutyrate [ 1 ]. Some plant growth-promoting rhizobacteria can produce 1-aminocyclopropane-1-carboxylate deaminase to enhance plant growth [ 2 , 3 ].

D-cysteine desulfhydrase (d-CDes) ( 4.4.1.15 ) 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 [ 4 , 5 , 6 ]. The physiological function of bacterial d-CDes is not clear.

L-cysteate sulfo-lyase ( 4.4.1.25 ) 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 [ 7 ].

1. Mechanistic studies of 1-aminocyclopropane-1-carboxylate deaminase: characterization of an unusual pyridoxal 5'-phosphate-dependent reaction. Biochemistry 50, 1950-62
2. Plant growth-promoting rhizobacteria (PGPR): emergence in agriculture. World J. Microbiol. Biotechnol. 28, 1327-50
3. Metagenomic analysis of the 1-aminocyclopropane-1-carboxylate deaminase gene (acdS) operon of an uncultured bacterial endophyte colonizing Solanum tuberosum L. Arch. Microbiol. 193, 665-76
4. D-Cysteine desulfhydrase of Escherichia coli. Purification and characterization. Eur. J. Biochem. 153, 541-51
5. Physiological comparison of D-cysteine desulfhydrase of Escherichia coli with 3-chloro-D-alanine dehydrochlorinase of Pseudomonas putida CR 1-1. Arch. Microbiol. 149, 413-6
6. Isolation and characterization of a D-cysteine desulfhydrase protein from Arabidopsis thaliana. FEBS J. 272, 1291-304
7. L-cysteate sulpho-lyase, a widespread pyridoxal 5'-phosphate-coupled desulphonative enzyme purified from Silicibacter pomeroyi DSS-3(T). Biochem. J. 394, 657-64