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Results 1 - 7 of 7
EC Number Subunits Commentary Reference
Show all pathways known for 1.23.5.1Display the word mapDisplay the reaction diagram Show all sequences 1.23.5.1? x * 39600, calculated, mature protein 732626
Show all pathways known for 1.23.5.1Display the word mapDisplay the reaction diagram Show all sequences 1.23.5.1? x * 43000, recombinant wild-type enzyme, SDS-PAGE 745996
Show all pathways known for 1.23.5.1Display the word mapDisplay the reaction diagram Show all sequences 1.23.5.1? x * 43000, SDS-PAGE 660205
Show all pathways known for 1.23.5.1Display the word mapDisplay the reaction diagram Show all sequences 1.23.5.1? x * 53000, recombinant enzyme, SDS-PAGE 746052
Show all pathways known for 1.23.5.1Display the word mapDisplay the reaction diagram Show all sequences 1.23.5.1monomer 1 * 43300, SDS-PAGE 660276
Show all pathways known for 1.23.5.1Display the word mapDisplay the reaction diagram Show all sequences 1.23.5.1More 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
Show all pathways known for 1.23.5.1Display the word mapDisplay the reaction diagram Show all sequences 1.23.5.1More 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
Results 1 - 7 of 7