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CYP 105—diverse structures, functions and roles in an intriguing family of enzymes in Streptomyces
Author(s) -
Moody Suzy C.,
Loveridge E. Joel
Publication year - 2014
Publication title -
journal of applied microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.889
H-Index - 156
eISSN - 1365-2672
pISSN - 1364-5072
DOI - 10.1111/jam.12662
Subject(s) - streptomyces , biology , enzyme , biochemistry , computational biology , function (biology) , catabolism , superfamily , metabolic pathway , metabolite , genetics , gene , bacteria
Summary;?> The cytochromes P450 ( CYP or P450) are a large superfamily of haem‐containing enzymes found in all domains of life. They catalyse a variety of complex reactions, predominantly mixed‐function oxidations, often displaying highly regio‐ and/or stereospecific chemistry. In streptomycetes, they are predominantly associated with secondary metabolite biosynthetic pathways or with xenobiotic catabolism. Homologues of one family, CYP 105, have been found in all Streptomyces species thus far sequenced. This review looks at the diverse biological functions of CYP 105s and the biosynthetic/catabolic pathways they are associated with. Examples are presented showing a range of biotransformative abilities and different contexts. As biocatalysts capable of some remarkable chemistry, CYP 105s have great biotechnological potential and merit detailed study. Recent developments in biotechnological applications which utilize CYP 105s are described, alongside a brief overview of the benefits and drawbacks of using P450s in commercial applications. The role of CYP 105s in vivo is in many cases undefined and provides a rich source for further investigation into the functions these enzymes fulfil and the metabolic pathways they participate in, in the natural environment.