EC 1.2.1.87 - Propanal dehydrogenase (CoA-propanoylating)

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IntEnz Enzyme Nomenclature
EC 1.2.1.87

Names

Accepted name:
propanal dehydrogenase (CoA-propanoylating)
Other name:
BphJ
Systematic name:
propanal:NAD+ oxidoreductase (CoA-propanoylating)

Reaction

Comments:

The enzyme forms a bifunctional complex with EC 4.1.3.43, 4-hydroxy-2-oxohexanoate aldolase, with a tight channel connecting the two subunits [1,2,3]. Also acts, more slowly, on glycolaldehyde and butanal. In Pseudomonas species the enzyme forms a bifunctional complex with EC 4.1.3.39, 4-hydroxy-2-oxovalerate aldolase. The enzymes from the bacteria Burkholderia xenovorans and Thermus thermophilus also perform the reaction of EC 1.2.1.10, acetaldehyde dehydrogenase (acetylating). NADP+ can replace NAD+ with a much slower rate [3].

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot:

References

  1. Baker, P., Pan, D., Carere, J., Rossi, A., Wang, W., Seah, S. Y.
    Characterization of an aldolase-dehydrogenase complex that exhibits substrate channeling in the polychlorinated biphenyls degradation pathway.
    Biochemistry 48 : 6551-6558 (2009). [PMID: 19476337]
  2. Carere, J., Baker, P., Seah, S. Y.
    Investigating the molecular determinants for substrate channeling in BphI-BphJ, an aldolase-dehydrogenase complex from the polychlorinated biphenyls degradation pathway.
    Biochemistry 50 : 8407-8416 (2011). [PMID: 21838275]
  3. Baker, P., Hillis, C., Carere, J., Seah, S. Y.
    Protein-protein interactions and substrate channeling in orthologous and chimeric aldolase-dehydrogenase complexes.
    Biochemistry 51 : 1942-1952 (2012). [PMID: 22316175]

[EC 1.2.1.87 created 2013]