Alcohol dehydrogenase (cytochrome c)

Alcohol dehydrogenase (cytochrome c)
Identifiers
EC number 1.1.2.8
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

Alcohol dehydrogenase (cytochrome c) (EC 1.1.2.8, type I quinoprotein alcohol dehydrogenase, quinoprotein ethanol dehydrogenase) is an enzyme with systematic name alcohol:cytochrome c oxidoreductase.[1][2][3][4][5][6] This enzyme catalyses the following chemical reaction

a primary alcohol + 2 ferricytochrome c an aldehyde + 2 ferrocytochrome c + 2 H+

A periplasmic PQQ-containing quinoprotein is present in Pseudomonas and Rhodopseudomonas.

References

  1. ↑ Rupp, M.; Gorisch, H. (1988). "Purification, crystallisation and characterization of quinoprotein ethanol dehydrogenase from Pseudomonas aeruginosa". Biol. Chem. Hoppe-Seyler. 369 (6): 431–439. doi:10.1515/bchm3.1988.369.1.431. PMID 3144289.
  2. ↑ Toyama, H.; Fujii, A.; Matsushita, K.; Shinagawa, E.; Ameyama, M.; Adachi, O. (1995). "Three distinct quinoprotein alcohol dehydrogenases are expressed when Pseudomonas putida is grown on different alcohols". J. Bacteriol. 177 (9): 2442–2450. PMC 176903. PMID 7730276.
  3. ↑ Schobert, M.; Gorisch, H. (1999). "Cytochrome c550 is an essential component of the quinoprotein ethanol oxidation system in Pseudomonas aeruginosa: cloning and sequencing of the genes encoding cytochrome c550 and an adjacent acetaldehyde dehydrogenase". Microbiology. 145: 471–481. doi:10.1099/13500872-145-2-471. PMID 10075429.
  4. ↑ Keitel, T.; Diehl, A.; Knaute, T.; Stezowski, J.J.; Hohne, W.; Gorisch, H. (2000). "X-ray structure of the quinoprotein ethanol dehydrogenase from Pseudomonas aeruginosa: basis of substrate specificity". J. Mol. Biol. 297 (4): 961–974. doi:10.1006/jmbi.2000.3603. PMID 10736230.
  5. ↑ Kay, C.W.; Mennenga, B.; Gorisch, H.; Bittl, R. (2004). "Characterisation of the PQQ cofactor radical in quinoprotein ethanol dehydrogenase of Pseudomonas aeruginosa by electron paramagnetic resonance spectroscopy". FEBS Lett. 564 (1–2): 69–72. doi:10.1016/S0014-5793(04)00317-5. PMID 15094044.
  6. ↑ Mennenga, B.; Kay, C.W.; Gorisch, H. (2009). "Quinoprotein ethanol dehydrogenase from Pseudomonas aeruginosa: the unusual disulfide ring formed by adjacent cysteine residues is essential for efficient electron transfer to cytochrome c550". Arch. Microbiol. 191 (4): 361–367. doi:10.1007/s00203-009-0460-4. PMID 19224199.
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