Enzymatic fluorination in Streptomyces cattleya takes place with an inversion of configuration consistent with an SN2 reaction mechanism

Cosimo Damiano Cadicamo; J Courtieu; H Deng; A Meddour; David O'Hagan

doi:10.1002/cbic.200300839

Enzymatic fluorination in Streptomyces cattleya takes place with an inversion of configuration consistent with an S_N2 reaction mechanism

Cosimo Damiano Cadicamo, J Courtieu, H Deng, A Meddour, David O'Hagan

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

Abstract

The stereochemical course of the recently isolated fluorination enzyme from Streptomyces cattleya has been evaluated. The enzyme mediates a reaction between fluoride ion and S-adenosyl-L-methionine (SAM) to generate 5'-fluoro-5'-deoxy-adenosine (5'-FDA). Preparation of (5'R)-[5-H-2(1)]-ATP generated (5'-R)-[5-H-2(1)]-5'-FDA in a coupled enzyme assay involving SAM synthase and the fluorinase. The stereochemical analysis of the product relied on H-2 NMR analysis in a chiral liquid-crystalline medium. It is concluded that the enzyme catalyses the fluorination with an inversion of configuration consistent with an S(N)2 reaction mechanism.

Original language	English
Pages (from-to)	685-690
Number of pages	6
Journal	ChemBioChem
Volume	5
Issue number	5
DOIs	https://doi.org/10.1002/cbic.200300839
Publication status	Published - 3 May 2004

Keywords

bioorganic chemistry
fluorine
NMR spectroscopy
stereochemistry
LIQUID-CRYSTALLINE SOLVENT
ENANTIOMERIC ANALYSIS
BOND FORMATION
BAKERS-YEAST
BIOSYNTHESIS
4-FLUOROTHREONINE
FLUOROACETATE
METHIONINE
ADENOSINE
ACID

Access to Document

10.1002/cbic.200300839

Cite this

@article{05e4e7d3a11940e197bc350753ba2846,

title = "Enzymatic fluorination in Streptomyces cattleya takes place with an inversion of configuration consistent with an SN2 reaction mechanism",

abstract = "The stereochemical course of the recently isolated fluorination enzyme from Streptomyces cattleya has been evaluated. The enzyme mediates a reaction between fluoride ion and S-adenosyl-L-methionine (SAM) to generate 5'-fluoro-5'-deoxy-adenosine (5'-FDA). Preparation of (5'R)-[5-H-2(1)]-ATP generated (5'-R)-[5-H-2(1)]-5'-FDA in a coupled enzyme assay involving SAM synthase and the fluorinase. The stereochemical analysis of the product relied on H-2 NMR analysis in a chiral liquid-crystalline medium. It is concluded that the enzyme catalyses the fluorination with an inversion of configuration consistent with an S(N)2 reaction mechanism.",

keywords = "bioorganic chemistry, fluorine, NMR spectroscopy, stereochemistry, LIQUID-CRYSTALLINE SOLVENT, ENANTIOMERIC ANALYSIS, BOND FORMATION, BAKERS-YEAST, BIOSYNTHESIS, 4-FLUOROTHREONINE, FLUOROACETATE, METHIONINE, ADENOSINE, ACID",

author = "Cadicamo, {Cosimo Damiano} and J Courtieu and H Deng and A Meddour and David O'Hagan",

year = "2004",

month = may,

day = "3",

doi = "10.1002/cbic.200300839",

language = "English",

volume = "5",

pages = "685--690",

journal = "ChemBioChem",

issn = "1439-4227",

publisher = "John Wiley & Sons, Ltd",

number = "5",

}

TY - JOUR

T1 - Enzymatic fluorination in Streptomyces cattleya takes place with an inversion of configuration consistent with an SN2 reaction mechanism

AU - Cadicamo, Cosimo Damiano

AU - Courtieu, J

AU - Deng, H

AU - Meddour, A

AU - O'Hagan, David

PY - 2004/5/3

Y1 - 2004/5/3

N2 - The stereochemical course of the recently isolated fluorination enzyme from Streptomyces cattleya has been evaluated. The enzyme mediates a reaction between fluoride ion and S-adenosyl-L-methionine (SAM) to generate 5'-fluoro-5'-deoxy-adenosine (5'-FDA). Preparation of (5'R)-[5-H-2(1)]-ATP generated (5'-R)-[5-H-2(1)]-5'-FDA in a coupled enzyme assay involving SAM synthase and the fluorinase. The stereochemical analysis of the product relied on H-2 NMR analysis in a chiral liquid-crystalline medium. It is concluded that the enzyme catalyses the fluorination with an inversion of configuration consistent with an S(N)2 reaction mechanism.

AB - The stereochemical course of the recently isolated fluorination enzyme from Streptomyces cattleya has been evaluated. The enzyme mediates a reaction between fluoride ion and S-adenosyl-L-methionine (SAM) to generate 5'-fluoro-5'-deoxy-adenosine (5'-FDA). Preparation of (5'R)-[5-H-2(1)]-ATP generated (5'-R)-[5-H-2(1)]-5'-FDA in a coupled enzyme assay involving SAM synthase and the fluorinase. The stereochemical analysis of the product relied on H-2 NMR analysis in a chiral liquid-crystalline medium. It is concluded that the enzyme catalyses the fluorination with an inversion of configuration consistent with an S(N)2 reaction mechanism.

KW - bioorganic chemistry

KW - fluorine

KW - NMR spectroscopy

KW - stereochemistry

KW - LIQUID-CRYSTALLINE SOLVENT

KW - ENANTIOMERIC ANALYSIS

KW - BOND FORMATION

KW - BAKERS-YEAST

KW - BIOSYNTHESIS

KW - 4-FLUOROTHREONINE

KW - FLUOROACETATE

KW - METHIONINE

KW - ADENOSINE

KW - ACID

UR - http://www.scopus.com/inward/record.url?scp=4544247116&partnerID=8YFLogxK

UR - http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=15122641

U2 - 10.1002/cbic.200300839

DO - 10.1002/cbic.200300839

M3 - Article

SN - 1439-4227

VL - 5

SP - 685

EP - 690

JO - ChemBioChem

JF - ChemBioChem

IS - 5

ER -

Enzymatic fluorination in Streptomyces cattleya takes place with an inversion of configuration consistent with an S_N2 reaction mechanism

Abstract

Keywords

Access to Document

Other files and links

Fingerprint

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

Cite this

Enzymatic fluorination in Streptomyces cattleya takes place with an inversion of configuration consistent with an SN2 reaction mechanism

Abstract

Keywords

Access to Document

Other files and links

Fingerprint

Projects

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

Cite this

Enzymatic fluorination in Streptomyces cattleya takes place with an inversion of configuration consistent with an S_N2 reaction mechanism