An enzymatic Finkelstein reaction: fluorinase catalyses direct halogen exchange

Phillip T. Lowe; Steven L. Cobb; David O'Hagan

doi:10.1039/C9OB01625B

An enzymatic Finkelstein reaction: fluorinase catalyses direct halogen exchange

Phillip T. Lowe, Steven L. Cobb, David O'Hagan

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

Abstract

The fluorinase enzyme from Streptomyces cattleya is shown to catalyse a direct displacement of bromide and iodide by fluoride ion from 5′-bromodeoxyadenosine (5′-BrDA) and 5′-iododeoxyadenosine (5′-IDA) respectively to form 5′-fluorodeoxyadenosine (5′-FDA) in the absence of L-methionine (L-Met) or S-adenosyl-L-methionine (SAM). 5′-BrDA is the most efficient substrate for this enzyme catalysed Finkelstein reaction.

Original language	English
Pages (from-to)	7493-7496
Number of pages	4
Journal	Organic & Biomolecular Chemistry
Volume	17
Issue number	32
Early online date	25 Jul 2019
DOIs	https://doi.org/10.1039/C9OB01625B
Publication status	Published - 28 Aug 2019

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Copyright © 2019 The Author(s). This work has been made available online in accordance with publisher policies or with permission. Permission for further reuse of this content should be sought from the publisher or the rights holder. This is the author created accepted manuscript following peer review and may differ slightly from the final published version. The final published version of this work is available at https://doi.org/10.1039/C9OB01625B
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title = "An enzymatic Finkelstein reaction: fluorinase catalyses direct halogen exchange",

abstract = "The fluorinase enzyme from Streptomyces cattleya is shown to catalyse a direct displacement of bromide and iodide by fluoride ion from 5′-bromodeoxyadenosine (5′-BrDA) and 5′-iododeoxyadenosine (5′-IDA) respectively to form 5′-fluorodeoxyadenosine (5′-FDA) in the absence of L-methionine (L-Met) or S-adenosyl-L-methionine (SAM). 5′-BrDA is the most efficient substrate for this enzyme catalysed Finkelstein reaction.",

author = "Lowe, \{Phillip T.\} and Cobb, \{Steven L.\} and David O'Hagan",

note = "We thank the Engineering and Physical Sciences Research Council, UK, for a research grant.",

year = "2019",

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doi = "10.1039/C9OB01625B",

language = "English",

volume = "17",

pages = "7493--7496",

journal = "Organic \& Biomolecular Chemistry",

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publisher = "Royal Society of Chemistry",

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TY - JOUR

T1 - An enzymatic Finkelstein reaction

T2 - fluorinase catalyses direct halogen exchange

AU - Lowe, Phillip T.

AU - Cobb, Steven L.

AU - O'Hagan, David

N1 - We thank the Engineering and Physical Sciences Research Council, UK, for a research grant.

PY - 2019/8/28

Y1 - 2019/8/28

N2 - The fluorinase enzyme from Streptomyces cattleya is shown to catalyse a direct displacement of bromide and iodide by fluoride ion from 5′-bromodeoxyadenosine (5′-BrDA) and 5′-iododeoxyadenosine (5′-IDA) respectively to form 5′-fluorodeoxyadenosine (5′-FDA) in the absence of L-methionine (L-Met) or S-adenosyl-L-methionine (SAM). 5′-BrDA is the most efficient substrate for this enzyme catalysed Finkelstein reaction.

AB - The fluorinase enzyme from Streptomyces cattleya is shown to catalyse a direct displacement of bromide and iodide by fluoride ion from 5′-bromodeoxyadenosine (5′-BrDA) and 5′-iododeoxyadenosine (5′-IDA) respectively to form 5′-fluorodeoxyadenosine (5′-FDA) in the absence of L-methionine (L-Met) or S-adenosyl-L-methionine (SAM). 5′-BrDA is the most efficient substrate for this enzyme catalysed Finkelstein reaction.

UR - https://www.scopus.com/pages/publications/85070705601

U2 - 10.1039/C9OB01625B

DO - 10.1039/C9OB01625B

M3 - Article

SN - 1477-0520

VL - 17

SP - 7493

EP - 7496

JO - Organic & Biomolecular Chemistry

JF - Organic & Biomolecular Chemistry

IS - 32

ER -

An enzymatic Finkelstein reaction: fluorinase catalyses direct halogen exchange

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