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CYP105-diverse structures, functions and roles in an intriguing family of enzymes in Streptomyces.

Moody SC, Loveridge EJ - J. Appl. Microbiol. (2014)

Bottom Line: The cytochromes P450 (CYP or P450) are a large superfamily of haem-containing enzymes found in all domains of life.Homologues of one family, CYP105, have been found in all Streptomyces species thus far sequenced.Recent developments in biotechnological applications which utilize CYP105s are described, alongside a brief overview of the benefits and drawbacks of using P450s in commercial applications.

View Article: PubMed Central - PubMed

Affiliation: Department of Biosciences, College of Science, Swansea University, Swansea, UK.

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Secondary metabolites whose biosynthesis requires the action of a CYP105. The structural feature introduced by the CYP105 is arrowed, and the CYP105 involved is indicated. The site of modification of coelibactin is not known.
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fig03: Secondary metabolites whose biosynthesis requires the action of a CYP105. The structural feature introduced by the CYP105 is arrowed, and the CYP105 involved is indicated. The site of modification of coelibactin is not known.

Mentions: A driving factor in much of the research on streptomycetes has been the abundance of secondary metabolites produced by this genus. Over the last 10 years, there has been increasing appreciation of the intricate tailoring role of P450s in many biosynthetic pathways, as they are often associated with the final steps of specialized metabolite production, refining the final product by complex regio- and stereospecific oxidative tailoring (Zhao and Waterman 2007). There are now several examples of CYP105s known to play important roles in biosynthesis of bioactive molecules (Fig.3), and new pathways are still being revealed, suggesting further CYP105 involvement may be uncovered.


CYP105-diverse structures, functions and roles in an intriguing family of enzymes in Streptomyces.

Moody SC, Loveridge EJ - J. Appl. Microbiol. (2014)

Secondary metabolites whose biosynthesis requires the action of a CYP105. The structural feature introduced by the CYP105 is arrowed, and the CYP105 involved is indicated. The site of modification of coelibactin is not known.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4265290&req=5

fig03: Secondary metabolites whose biosynthesis requires the action of a CYP105. The structural feature introduced by the CYP105 is arrowed, and the CYP105 involved is indicated. The site of modification of coelibactin is not known.
Mentions: A driving factor in much of the research on streptomycetes has been the abundance of secondary metabolites produced by this genus. Over the last 10 years, there has been increasing appreciation of the intricate tailoring role of P450s in many biosynthetic pathways, as they are often associated with the final steps of specialized metabolite production, refining the final product by complex regio- and stereospecific oxidative tailoring (Zhao and Waterman 2007). There are now several examples of CYP105s known to play important roles in biosynthesis of bioactive molecules (Fig.3), and new pathways are still being revealed, suggesting further CYP105 involvement may be uncovered.

Bottom Line: The cytochromes P450 (CYP or P450) are a large superfamily of haem-containing enzymes found in all domains of life.Homologues of one family, CYP105, have been found in all Streptomyces species thus far sequenced.Recent developments in biotechnological applications which utilize CYP105s are described, alongside a brief overview of the benefits and drawbacks of using P450s in commercial applications.

View Article: PubMed Central - PubMed

Affiliation: Department of Biosciences, College of Science, Swansea University, Swansea, UK.

Show MeSH