Alcohol dehydrogenase (cytochrome c)
| 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 | ||||||||
| |||||||||
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
- ^ 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.
- ^ 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.
- ^ 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.
- ^ 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.
- ^ 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.
- ^ 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
- Alcohol+dehydrogenase+(cytochrome+c) at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
