LIS - Legume Information System
Information about legume traits for crop improvement
GlycineMine
v5.1.0.3
Glycine data from LIS
v5.1.0.3
Glycine data from LIS
| Type | Domain |
| Description | Phytochelatins are well known as the heavy metal-detoxifying peptides in higher plants, eukaryotic algae, fungi, nematode and cyanobacteria. Phytochelatin synthase (PCS, also known as glutathione gamma-glutamylcysteinyltransferase; ) is involved in the synthesis of phytochelatins (PC) and homophytochelatins (hPC). This enzyme is required for detoxification of heavy metals such as cadmium and arsenate. The N-terminal region of phytochelatin synthase contains the active site, as well as four highly conserved cysteine residues that appear to play an important role in heavy-metal-induced phytochelatin catalysis. The C-terminal region is rich in cysteines, and may act as a metal sensor, whereby the Cys residues bind cadmium ions to bring them into closer proximity and transferring them to the activation site in the N-terminal catalytic domain [ ]. The C-terminal region displays homology to the functional domains of metallothionein and metallochaperone. This entry represents the N-terminal catalytic PCS domain, which belongs to the petidase family C83 of the papain superfamily of cysteine proteases, with a structurally conserved "catalytic triad"and oxyanion hole in the active site. It has an overall "crescent"shape with alpha/beta fold containing eight α-helices and six β-strands [ ]. |
| Short Name | PCS_N |
