Biology:Alcohol dehydrogenase (cytochrome c)
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Short description: Class of enzymes
| 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 [math]\displaystyle{ \rightleftharpoons }[/math] an aldehyde + 2 ferrocytochrome c + 2 H+
A periplasmic PQQ-containing quinoprotein is present in Pseudomonas and Rhodopseudomonas.
References
- ↑ "Purification, crystallisation and characterization of quinoprotein ethanol dehydrogenase from Pseudomonas aeruginosa". Biological Chemistry Hoppe-Seyler 369 (6): 431–9. June 1988. doi:10.1515/bchm3.1988.369.1.431. PMID 3144289.
- ↑ "Three distinct quinoprotein alcohol dehydrogenases are expressed when Pseudomonas putida is grown on different alcohols". Journal of Bacteriology 177 (9): 2442–50. May 1995. doi:10.1128/jb.177.9.2442-2450.1995. PMID 7730276.
- ↑ "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. February 1999. doi:10.1099/13500872-145-2-471. PMID 10075429.
- ↑ "X-ray structure of the quinoprotein ethanol dehydrogenase from Pseudomonas aeruginosa: basis of substrate specificity". Journal of Molecular Biology 297 (4): 961–74. April 2000. doi:10.1006/jmbi.2000.3603. PMID 10736230.
- ↑ "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. April 2004. doi:10.1016/S0014-5793(04)00317-5. PMID 15094044.
- ↑ "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. April 2009. doi:10.1007/s00203-009-0460-4. PMID 19224199.
External links
- Alcohol+dehydrogenase+(cytochrome+c) at the US National Library of Medicine Medical Subject Headings (MeSH)
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