Prokaryotic acetaldehyde dehydrogenase dimerisation domain
crystal structure of a bifunctional aldolase-dehydrogenase : sequestering a reactive and volatile intermediate
In molecular biology, prokaryotic acetaldehyde dehydrogenase dimerisation domain is a protein domain found at the C-terminus of prokaryotic acetaldehyde dehydrogenases, it adopts a structure consisting of an alpha-beta-alpha-beta(3) core, which mediates dimerisation of the protein.
The acetaldehyde dehydrogenase family of bacterial enzymes catalyses the formation of acetyl-CoA from acetaldehyde in the 3-hydroxyphenylpropinoate degradation pathway. It occurs as a late step in the meta-cleavage pathways of a variety of compounds, including catechol, biphenyl, toluene, salicylate.
- Manjasetty BA, Powlowski J, Vrielink A (June 2003). "Crystal structure of a bifunctional aldolase-dehydrogenase: sequestering a reactive and volatile intermediate". Proc. Natl. Acad. Sci. U.S.A. 100 (12): 6992–7. doi:10.1073/pnas.1236794100. PMC . PMID 12764229.
- Shingler V, Powlowski J, Marklund U (February 1992). "Nucleotide sequence and functional analysis of the complete phenol/3,4-dimethylphenol catabolic pathway of Pseudomonas sp. strain CF600". J. Bacteriol. 174 (3): 711–24. PMC . PMID 1732207.