From Wikipedia, the free encyclopedia
Alcohol dehydrogenase (cytochrome c)
Identifiers
EC no. 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
Search
PMC articles
PubMed articles
NCBI proteins

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, Görisch H (June 1988). "Purification, crystallisation and characterization of quinoprotein ethanol dehydrogenase from Pseudomonas aeruginosa". Biological Chemistry Hoppe-Seyler. 369 (6): 431–9. doi: 10.1515/bchm3.1988.369.1.431. PMID  3144289.
  2. ^ Toyama H, Fujii A, Matsushita K, Shinagawa E, Ameyama M, Adachi O (May 1995). "Three distinct quinoprotein alcohol dehydrogenases are expressed when Pseudomonas putida is grown on different alcohols". Journal of Bacteriology. 177 (9): 2442–50. doi: 10.1128/jb.177.9.2442-2450.1995. PMC  176903. PMID  7730276.
  3. ^ Schobert M, Görisch H (February 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 ( Pt 2): 471–81. doi: 10.1099/13500872-145-2-471. PMID  10075429.
  4. ^ Keitel T, Diehl A, Knaute T, Stezowski JJ, Höhne W, Görisch H (April 2000). "X-ray structure of the quinoprotein ethanol dehydrogenase from Pseudomonas aeruginosa: basis of substrate specificity". Journal of Molecular Biology. 297 (4): 961–74. doi: 10.1006/jmbi.2000.3603. PMID  10736230.
  5. ^ Kay CW, Mennenga B, Görisch H, Bittl R (April 2004). "Characterisation of the PQQ cofactor radical in quinoprotein ethanol dehydrogenase of Pseudomonas aeruginosa by electron paramagnetic resonance spectroscopy". FEBS Letters. 564 (1–2): 69–72. doi: 10.1016/S0014-5793(04)00317-5. PMID  15094044.
  6. ^ Mennenga B, Kay CW, Görisch H (April 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". Archives of Microbiology. 191 (4): 361–7. doi: 10.1007/s00203-009-0460-4. PMID  19224199.

External links