Structural highlights
Function
[ADHE_ECOLI] This enzyme has three activities: ADH, ACDH, and PFL-deactivase. In aerobic conditions it acts as a hydrogen peroxide scavenger. The PFL deactivase activity catalyzes the quenching of the pyruvate-formate-lyase catalyst in an iron, NAD, and CoA dependent reaction.
Publication Abstract from PubMed
The bifunctional alcohol/aldehyde dehydrogenase (AdhE) comprises both an N-terminal aldehyde dehydrogenase (AldDH) and a C-terminal alcohol dehydrogenase (ADH). In vivo, full-length AdhE oligomerizes into long oligomers known as spirosomes. However, structural analysis of AdhE is challenging owing to the heterogeneity of the spirosomes. Therefore, the domains of AdhE are best characterized separately. Here, the structure of ADH from the pathogenic Escherichia coli O157:H7 was determined to 1.65 A resolution. The dimeric crystal structure was confirmed in solution by small-angle X-ray scattering.
High-resolution structure of the alcohol dehydrogenase domain of the bifunctional bacterial enzyme AdhE.,Azmi L, Bragginton EC, Cadby IT, Byron O, Roe AJ, Lovering AL, Gabrielsen M Acta Crystallogr F Struct Biol Commun. 2020 Sep 1;76(Pt 9):414-421. doi:, 10.1107/S2053230X20010237. Epub 2020 Aug 19. PMID:32880589[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Azmi L, Bragginton EC, Cadby IT, Byron O, Roe AJ, Lovering AL, Gabrielsen M. High-resolution structure of the alcohol dehydrogenase domain of the bifunctional bacterial enzyme AdhE. Acta Crystallogr F Struct Biol Commun. 2020 Sep 1;76(Pt 9):414-421. doi:, 10.1107/S2053230X20010237. Epub 2020 Aug 19. PMID:32880589 doi:http://dx.doi.org/10.1107/S2053230X20010237
