Family

D-cysteine desulfhydrase (IPR005966)

Short name: D-Cys_desShydrase

Family relationships

Description

This entry represents a family of pyridoxal phosphate-dependent enzymes closely related to (and often designated as putative examples of) 1-aminocyclopropane-1-carboxylate deaminase. Members of this family include D-cysteine desulfhydrase (EC:4.4.1.15) , 1-aminocyclopropane-1-carboxylate deaminase (EC:3.5.99.7), and L-cysteate sulfo-lyase (EC:4.4.1.25).

1-aminocyclopropane-1-carboxylate deaminase (EC:3.5.99.7) catalyses a cyclopropane ring-opening reaction, the irreversible conversion of 1-aminocyclopropane-1-carboxylate (ACC) to ammonia and alpha-ketobutyrate [PMID: 21244019]. Some plant growth-promoting rhizobacteria can produce 1-aminocyclopropane-1-carboxylate deaminase to enhance plant growth [PMID: 22805914, PMID: 21523387].

D-cysteine desulfhydrase (d-CDes) (EC: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 [PMID: 3908101, PMID: 3132906, PMID: 15720402]. The physiological function of bacterial d-CDes is not clear.

L-cysteate sulfo-lyase (EC: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 [PMID: 16302849].

GO terms

Biological Process

No terms assigned in this category.

Molecular Function

GO:0003824 catalytic activity

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
TIGRFAMs