Biology:Prokaryotic acetaldehyde dehydrogenase dimerisation domain
From HandWiki
| AcetDehyd-dimer | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 crystal structure of a bifunctional aldolase-dehydrogenase : sequestering a reactive and volatile intermediate | |||||||||
| Identifiers | |||||||||
| Symbol | AcetDehyd-dimer | ||||||||
| Pfam | PF09290 | ||||||||
| InterPro | IPR015426 | ||||||||
| SCOP2 | 1nvm / SCOPe / SUPFAM | ||||||||
| |||||||||
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]
References
- ↑ "Crystal structure of a bifunctional aldolase-dehydrogenase: sequestering a reactive and volatile intermediate". Proc. Natl. Acad. Sci. U.S.A. 100 (12): 6992–7. June 2003. doi:10.1073/pnas.1236794100. PMID 12764229. Bibcode: 2003PNAS..100.6992M.
- ↑ "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. February 1992. doi:10.1128/jb.174.3.711-724.1992. PMID 1732207.
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