Proteomics

Dataset Information

0

D. magna CT448 protease specificity


ABSTRACT: Mass developments of toxin-producing cyanobacteria are frequently observed in freshwater ecosystems due to eutrophication and global warming. These mass developments can partly be attributed to cyanobacterial toxins, such as protease inhibitors (PIs), which inhibit digestive serine proteases of Daphnia, the major herbivore of phytoplankton and cyanobacteria. To date, mechanisms of this inhibition in the gut of the crustacean Daphnia magna are not known. Here, we characterize a single serine protease, chymotrypsin 448 (CT448), which is present in the gut of the crustacean D. magna.

INSTRUMENT(S): maXis

ORGANISM(S): Daphnia Magna

SUBMITTER: Fatih Demir  

LAB HEAD: Pitter Florian Huesgen

PROVIDER: PXD010978 | Pride | 2018-10-04

REPOSITORIES: pride

Dataset's files

Source:
Action DRS
170112CT448PICS1_RG2_01_1340.d.zip Other
170112CT448PICS1_RG2_01_1341.d.zip Other
170112CT448PICS2_RG3_01_1342.d.zip Other
170112CT448PICS2_RG3_02_1343.d.zip Other
CT448.fasta Fasta
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Publications

Heterologous expression and characterization of a novel serine protease from Daphnia magna: A possible role in susceptibility to toxic cyanobacteria.

Lange Jacqueline J   Demir Fatih F   Huesgen Pitter F PF   Baumann Ulrich U   von Elert Eric E   Pichlo Christian C  

Aquatic toxicology (Amsterdam, Netherlands) 20180926


Mass developments of toxin-producing cyanobacteria are frequently observed in freshwater ecosystems due to eutrophication and global warming. These mass developments can partly be attributed to cyanobacterial toxins, such as protease inhibitors (PIs), which inhibit digestive serine proteases of Daphnia, the major herbivore of phytoplankton and cyanobacteria. To date, mechanisms of this inhibition in the gut of the crustacean Daphnia magna are not known. Here, we characterize a single serine prot  ...[more]

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