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	additional information	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	additional information	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