Polyvinyl_alcohol_dehydrogenase_(cytochrome)

Polyvinyl alcohol dehydrogenase (cytochrome)

Polyvinyl alcohol dehydrogenase (cytochrome)

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Polyvinyl alcohol dehydrogenase (cytochrome) (EC 1.1.2.6, PVA dehydrogenase, PVADH) is an enzyme with systematic name polyvinyl alcohol:ferricytochrome-c oxidoreductase.[1][2][3][4][5][6] This enzyme catalyses the following chemical reaction

polyvinyl alcohol + ferricytochrome c oxidized polyvinyl alcohol + ferrocytochrome c + H+
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This enzyme participates in bacterial polyvinyl alcohol degradation.


References

  1. Shimao M, Ninomiya K, Kuno O, Kato N, Sakazawa C (February 1986). "Existence of a novel enzyme, pyrroloquinoline quinone-dependent polyvinyl alcohol dehydrogenase, in a bacterial symbiont, Pseudomonas sp. strain VM15C". Applied and Environmental Microbiology. 51 (2): 268–75. PMC 238858. PMID 3513704.
  2. Shimao M, Onishi S, Kato N, Sakazawa C (February 1989). "Pyrroloquinoline Quinone-Dependent Cytochrome Reduction in Polyvinyl Alcohol-Degrading Pseudomonas sp. Strain VM15C". Applied and Environmental Microbiology. 55 (2): 275–8. PMC 184100. PMID 16347841.
  3. Mamoto R, Hu X, Chiue H, Fujioka Y, Kawai F (February 2008). "Cloning and expression of soluble cytochrome c and its role in polyvinyl alcohol degradation by polyvinyl alcohol-utilizing Sphingopyxis sp. strain 113P3". Journal of Bioscience and Bioengineering. 105 (2): 147–51. doi:10.1263/jbb.105.147. PMID 18343342.
  4. Hu X, Mamoto R, Fujioka Y, Tani A, Kimbara K, Kawai F (March 2008). "The pva operon is located on the megaplasmid of Sphingopyxis sp. strain 113P3 and is constitutively expressed, although expression is enhanced by PVA". Applied Microbiology and Biotechnology. 78 (4): 685–93. doi:10.1007/s00253-008-1348-y. PMID 18214469.
  5. Kawai F, Hu X (August 2009). "Biochemistry of microbial polyvinyl alcohol degradation". Applied Microbiology and Biotechnology. 84 (2): 227–37. doi:10.1007/s00253-009-2113-6. PMID 19590867.

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