Cardiff University | Prifysgol Caerdydd ORCA
Online Research @ Cardiff 
WelshClear Cookie - decide language by browser settings

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

Moody, Suzy C. and Loveridge, Edric Joel 2014. CYP105-diverse structures, functions and roles in an intriguing family of enzymes in Streptomyces. Journal of Applied Microbiology 117 (6) , pp. 1549-1563. 10.1111/jam.12662

[thumbnail of Moody_et_al-2014-Journal_of_Applied_Microbiology.pdf] PDF - Published Version
Available under License Creative Commons Attribution.

Download (0B)


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, CYP105, have been found in all Streptomyces species thus far sequenced. This review looks at the diverse biological functions of CYP105s 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, CYP105s have great biotechnological potential and merit detailed study. 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. The role of CYP105s 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.

Item Type: Article
Date Type: Publication
Status: Published
Schools: Chemistry
Subjects: Q Science > QD Chemistry
Publisher: Wiley-Blackwell
ISSN: 1364-5072
Date of First Compliant Deposit: 30 March 2016
Last Modified: 25 Feb 2019 16:33

Citation Data

Cited 14 times in Scopus. View in Scopus. Powered By Scopus® Data

Actions (repository staff only)

Edit Item Edit Item


Downloads per month over past year

View more statistics