Identification of fluorinases from streptomyces sp MA37, norcardia brasiliensis, and actinoplanes sp N902-109 by genome mining

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dc.contributor.authorDeng, H.
dc.contributor.authorMa, L.
dc.contributor.authorBandaranayaka, N.
dc.contributor.authorQin, Z.
dc.contributor.authorMann, G.
dc.contributor.authorKyeremeh, K.
dc.contributor.authorYu, Y.
dc.contributor.authorShepherd, T.
dc.contributor.authorNaismith, J.H.
dc.contributor.authorO'Hagan, D.
dc.date.accessioned2018-11-02T16:38:44Z
dc.date.available2018-11-02T16:38:44Z
dc.date.issued2014
dc.description.abstractThe fluorinase is an enzyme that catalyses the combination of S-adenosyl-L-methionine (SAM) and a fluoride ion to generate 5′-fluorodeoxy adenosine (FDA) and L-methionine through a nucleophilic substitution reaction with a fluoride ion as the nucleophile. It is the only native fluorination enzyme that has been characterised. The fluorinase was isolated in 2002 from Streptomyces cattleya, and, to date, this has been the only source of the fluorinase enzyme. Herein, we report three new fluorinase isolates that have been identified by genome mining. The novel fluorinases from Streptomyces sp. MA37, Nocardia brasiliensis, and an Actinoplanes sp. have high homology (80-87 % identity) to the original S. cattleya enzyme. They all possess a characteristic 21-residue loop. The three newly identified genes were overexpressed in E. coli and shown to be fluorination enzymes. An X-ray crystallographic study of the Streptomyces sp. MA37 enzyme demonstrated that it is almost identical in structure to the original fluorinase. Culturing of the Streptomyces sp. MA37 strain demonstrated that it not only also elaborates the fluorometabolites, fluoroacetate and 4-fluorothreonine, similar to S. cattleya, but this strain also produces a range of unidentified fluorometabolites. These are the first new fluorinases to be reported since the first isolate, over a decade ago, and their identification extends the range of fluorination genes available for fluorination biotechnology. Get on the fluor! The fluorinase enzyme from Streptomyces cattleya was identified in 2002 as the only fluorination enzyme known in biochemistry. Three additional fluorinases expressed through bacterial genome mining are now reported. These new fluorinases extend the range of genes available for developing fluorination biotechnology. Copyright © 2014 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.en_US
dc.identifier.other10.1002/cbic.201300732
dc.identifier.urihttp://ugspace.ug.edu.gh/handle/123456789/25215
dc.language.isoenen_US
dc.publisherChemBioChemen_US
dc.subjectbiotransformationsen_US
dc.subjectenzyme catalysisen_US
dc.subjectfluorinasesen_US
dc.subjectgenome miningen_US
dc.subjectStreptomyces sp. MAen_US
dc.titleIdentification of fluorinases from streptomyces sp MA37, norcardia brasiliensis, and actinoplanes sp N902-109 by genome miningen_US
dc.typeArticleen_US

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