Open AccessPolyethylene glycol dehydrogenase activity of Rhodopseudomonas acidophila derives from a type I quinohaemoprotein alcohol dehydrogenase
Author(s) -
Yasuda Masaaki,
Cherepanov Alexey,
Duine Johannis A.
Publication year - 1996
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1996.tb08129.x
Subject(s) - comamonas testosteroni , alcohol dehydrogenase , dehydrogenase , polyethylene glycol , biochemistry , chemistry , rhodopseudomonas , pseudomonas putida , alcohol oxidoreductase , enzyme , isoelectric point , stereochemistry , nad+ kinase , photosynthesis
Dye‐linked alcohol dehydrogenase from Rhodopseudomonas acidophila strain M402, able to oxidize polyethylene glycols, was purified to homogeneity. The monomeric enzyme, having a molecular mass of 72 kDa, contains one PQQ and one haem c per enzyme molecule. In other respects also, the enzyme is very similar to the type I quinohaemoprotein alcohol dehydrogenases known to occur in Comamonas testosteroni, Comamonas acidovorans , and Pseudomonas putida species. However, dissimilarities exist with respect to the isoelectric points and the substrate specificities. On reinvestigating the substrate specificity of the C. testosteroni enzyme, it also appeared to exhibit good activity towards polyethylene glycols. Based on what has been reported for the polyethylene glycol‐oxidizing alcohol dehydrogenase of Sphingomonas macrogoltabidus , this enzyme is quite different from that of R. acidophila . Keywords: Polyethylene glycol dehydrogenase activity; Alcohol dehydrogenase; PQQ; Haem c ; Rhodopseudomonas acidophila