P. oleovorans GPol

Relative activity was based on the activity with P. oleovorans GPol. 

Figure 6. Hydroxylation of alkanes catalyzed by recombinant microbes harboring the alkane monooxygenase (AMO) of P. putida GPol (formerly known as P. oleovorans GPol). A fraction ofthe broad substrate spectrum of AMO is shown [102].

Previously, we have screened the literature for relevant biochemical studies on enzyme systems that oxidize medium chain-length alkanes (1). The Pseudomonas strains mentioned in this paper have been studied in varying detail with respect to the enzymology of medium chain-length alkane metabolism. The alkane hydroxylase systems in these strains show a number of differences, such as the apparent absence of rubredoxin in P. aeruginosa 196 Aa (12). On the whole, however, they resemble each other, and the system of P. oleovorans GPol. As an example, we found that the described substrate range of the paraffin hydroxylase of... 

In conclusion, the four P. aeruginosa strains able to grow on n-octane contain alkane hydroxylase systems that are almost -if not completely- identical to the P. oleovorans GPol system. The differences observed in the earlier biochemical papers are probably due to host factors, different relative expression levels of the alkane hydroxylase components, or the methods used to study the respective strains, not to the primary sequence of the proteins. 

Many bacteria are able grow on medium chain-length alkanes. Of these strains, only P. oleovorans TF4-1L (GPol) has been studied in detail with respect to both the genetics and enzymology of alkane metabolism (Fig. 1) (1), also because this strain has proven to be a versatile biocatalyst (2, and references therein). 

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