Fluorinase mediated C-F-18 bond formation, an enzymatic tool for PET labelling

H  Deng; S L  Cobb; A D  Gee; A  Lockhart; L  Martarello; R P  McGlinchey; D  O'Hagan; M  Onega

doi:10.1039/b516861a

Fluorinase mediated C-F-18 bond formation, an enzymatic tool for PET labelling

H Deng, S L Cobb, A D Gee, A Lockhart, L Martarello, R P McGlinchey, D O'Hagan, M Onega

School of Chemistry

Research output: Contribution to journal › Article › peer-review

Abstract

The fluorinase enzyme from S. cattleya is applied as a catalyst for the efficient incorporation of [F-18]-fluoride into [F-18]-5'-fluoro-5'-deoxyadenosine, [F-18]-5'-fluoro-5'-deoxyinosine and [F-18]-5-fluoro-5-deoxyribose for positron emission tomography (PET) applications.

Original language	English
Pages (from-to)	652-654
Number of pages	3
Journal	Chemical Communications
Issue number	6
DOIs	https://doi.org/10.1039/b516861a
Publication status	Published - 14 Feb 2006

Keywords

STREPTOMYCES-CATTLEYA
BIOSYNTHESIS
MECHANISM
ACID

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10.1039/b516861a

Cite this

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title = "Fluorinase mediated C-F-18 bond formation, an enzymatic tool for PET labelling",

abstract = "The fluorinase enzyme from S. cattleya is applied as a catalyst for the efficient incorporation of [F-18]-fluoride into [F-18]-5'-fluoro-5'-deoxyadenosine, [F-18]-5'-fluoro-5'-deoxyinosine and [F-18]-5-fluoro-5-deoxyribose for positron emission tomography (PET) applications.",

keywords = "STREPTOMYCES-CATTLEYA, BIOSYNTHESIS, MECHANISM, ACID",

author = "H Deng and Cobb, \{S L\} and Gee, \{A D\} and A Lockhart and L Martarello and McGlinchey, \{R P\} and D O'Hagan and M Onega",

year = "2006",

month = feb,

day = "14",

doi = "10.1039/b516861a",

language = "English",

pages = "652--654",

journal = "Chemical Communications",

issn = "1359-7345",

publisher = "Royal Society of Chemistry",

number = "6",

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T1 - Fluorinase mediated C-F-18 bond formation, an enzymatic tool for PET labelling

AU - Deng, H

AU - Cobb, S L

AU - Gee, A D

AU - Lockhart, A

AU - Martarello, L

AU - McGlinchey, R P

AU - O'Hagan, D

AU - Onega, M

PY - 2006/2/14

Y1 - 2006/2/14

N2 - The fluorinase enzyme from S. cattleya is applied as a catalyst for the efficient incorporation of [F-18]-fluoride into [F-18]-5'-fluoro-5'-deoxyadenosine, [F-18]-5'-fluoro-5'-deoxyinosine and [F-18]-5-fluoro-5-deoxyribose for positron emission tomography (PET) applications.

AB - The fluorinase enzyme from S. cattleya is applied as a catalyst for the efficient incorporation of [F-18]-fluoride into [F-18]-5'-fluoro-5'-deoxyadenosine, [F-18]-5'-fluoro-5'-deoxyinosine and [F-18]-5-fluoro-5-deoxyribose for positron emission tomography (PET) applications.

KW - STREPTOMYCES-CATTLEYA

KW - BIOSYNTHESIS

KW - MECHANISM

KW - ACID

UR - https://www.scopus.com/pages/publications/33645460289

U2 - 10.1039/b516861a

DO - 10.1039/b516861a

M3 - Article

SN - 1359-7345

SP - 652

EP - 654

JO - Chemical Communications

JF - Chemical Communications

IS - 6

ER -

Fluorinase mediated C-F-18 bond formation, an enzymatic tool for PET labelling

Abstract

Keywords

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GR/S97491/01: Extending the substratespecificity of enzymatic fluorination. An entirely novel biocatalysis

BBS/B/04579: Structural, mechanistic and genetic studies of a fluorination enzyme and fluorometabolite pathway in Streptomyces cattleya

Cite this

Fluorinase mediated C-F-18 bond formation, an enzymatic tool for PET labelling

Abstract

Keywords

Access to Document

Other files and links

Fingerprint

Projects

GR/S97491/01: Extending the substratespecificity of enzymatic fluorination. An entirely novel biocatalysis

BBS/B/04579: Structural, mechanistic and genetic studies of a fluorination enzyme and fluorometabolite pathway in Streptomyces cattleya

Cite this