v5.1.0.3
Cicer data from the Legume Information System
| Type | Family |
| Description | This family of peptidases consists of hydrogenase expression/formation proteins, such as HoxM from Alcaligenes eutrophus and HybD from E. coli. They belong to the MEROPS peptidase family A31.Nickel/iron hydrogenases are synthesized as two subunits, with the larger subunit containing the metallo centre. Once nickel has bound, the large subunit is activated by processing at a conserved site near the C terminus [ ]. The HycI endopeptidase releases a 32-residue peptide by cleavage of an Arg+Met bond []. A 15-residue peptide is released from hydrogenase 2 by cleavage of a His+Met bond by the HybD endopeptidase [ ].The tertiary structure of HybD has been solved, and shows a twisted beta sheet with three alpha helices on one side and four on the other [ ]. The molecule binds a single cadmium ion, which led to the peptidase being incorrectly identified as a metallopeptidase. It is possible that the metal binding site interacts with the nickel in the hydrogenase substrate []. The fold is similar to that of members of family A25, and both families A25 and A31 are included in the same clan, AE. |
| Short Name | Pept_A31_hyd_express |