Prokaryotic acetaldehyde dehydrogenase dimerisation domain

From Wikipedia, the free encyclopedia
Jump to navigation Jump to search
PDB 1nvm EBI.jpg
crystal structure of a bifunctional aldolase-dehydrogenase : sequestering a reactive and volatile intermediate
Symbol AcetDehyd-dimer
Pfam PF09290
InterPro IPR015426
SCOP 1nvm

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.[1]

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.[2]


  1. ^ 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 165818Freely accessible. PMID 12764229. 
  2. ^ 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 206147Freely accessible. PMID 1732207. 
This article incorporates text from the public domain Pfam and InterPro: IPR015426