Molecular and Low-Resolution Structural Characterization of the Na⁺-Translocating Glutaconyl-CoA Decarboxylase From Clostridium symbiosum.

ABSTRACT: Some anaerobic bacteria use biotin-dependent Na⁺-translocating decarboxylases (Bdc) of β-keto acids or their thioester analogs as key enzymes in their energy metabolism. Glutaconyl-CoA decarboxylase (Gcd), a member of this protein family, drives the endergonic translocation of Na⁺ across the membrane with the exergonic decarboxylation of glutaconyl-CoA (ΔG ⁰' ≈-30 kJ/mol) to crotonyl-CoA. Here, we report on the molecular characterization of Gcd from Clostridium symbiosum based on native PAGE, size exclusion chromatography (SEC) and laser-induced liquid bead ion desorption mass spectrometry (LILBID-MS). The obtained molecular mass of ca. 400 kDa fits to the DNA sequence-derived mass of 379 kDa with a subunit composition of 4 GcdA (65 kDa), 2 Gc

SUBMITTER: Vitt S 

PROVIDER: S-EPMC7145394 | biostudies-literature | 2020

REPOSITORIES: biostudies-literature