EC Number |
Subunits |
Reference |
---|
1.23.5.1 | ? |
x * 39600, calculated, mature protein |
732626 |
1.23.5.1 | ? |
x * 43000, recombinant wild-type enzyme, SDS-PAGE |
745996 |
1.23.5.1 | ? |
x * 43000, SDS-PAGE |
660205 |
1.23.5.1 | ? |
x * 53000, recombinant enzyme, SDS-PAGE |
746052 |
1.23.5.1 | monomer |
1 * 43300, SDS-PAGE |
660276 |
1.23.5.1 | More |
enzyme VDE consists of a cysteine-rich N-terminal domain, a lipocalin-like domain and a negatively charged C-terminal domain. A disulphide pattern in VDE of C9-C27, C14-C21, C33-C50, C37-C46, C65-C72 and C118-C284 is obtained after digestion of VDE with thermolysin followed by mass spectroscopy analysis of reduced versus non-reduced samples. Reduction of the disulfides results in loss of a rigid structure and a decrease in thermal stability of 15°C. Peptide mapping, mass spectroscopy, overview |
745983 |
1.23.5.1 | More |
enzyme VDE consists of three domains with the central lipocalin-like domain. VDE enzyme activity is possible without the C-terminal domain but not without the N-terminal domain. The N-terminal domain shows no VDE activity by itself, but when separately expressed domains are mixed, VDE activity is possible. Presence of alpha-helical structure in both the N- and C-terminal domains |
745996 |