The enzymatic resolution of an _- fluoroamide by an acylase

JW Banks; David O'Hagan

The enzymatic resolution of an _- fluoroamide by an acylase

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Abstract

The acylase from Aspergillus melleus was able to hydrolyse the amide bond of (S)-phenylalanine-N-2-(R,S)-fluoropropionamide and discriminate the diastereoisomers such that the (S,S)-diastereoisomer was hydrolysed by an order of magnitude faster than the (S,R)diasteroisomer. The origin of the kinetic discrimination is attributed to both binding and kinetic effects. (C) 2000 Elsevier Science S.A. All rights reserved.

Original language	English
Pages (from-to)	235-238
Number of pages	4
Journal	Journal of Fluorine Chemistry
Volume	102
Publication status	Published - Mar 2000

Keywords

F-19-NMR
acylase
Aspergillus melleus
alpha-fluoroamide
enzyme resolution
PYRIDINE
FLUORINE

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title = "The enzymatic resolution of an \_- fluoroamide by an acylase",

abstract = "The acylase from Aspergillus melleus was able to hydrolyse the amide bond of (S)-phenylalanine-N-2-(R,S)-fluoropropionamide and discriminate the diastereoisomers such that the (S,S)-diastereoisomer was hydrolysed by an order of magnitude faster than the (S,R)diasteroisomer. The origin of the kinetic discrimination is attributed to both binding and kinetic effects. (C) 2000 Elsevier Science S.A. All rights reserved.",

keywords = "F-19-NMR, acylase, Aspergillus melleus, alpha-fluoroamide, enzyme resolution, PYRIDINE, FLUORINE",

author = "JW Banks and David O'Hagan",

year = "2000",

month = mar,

language = "English",

volume = "102",

pages = "235--238",

journal = "Journal of Fluorine Chemistry",

issn = "0022-1139",

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TY - JOUR

T1 - The enzymatic resolution of an _- fluoroamide by an acylase

AU - Banks, JW

AU - O'Hagan, David

PY - 2000/3

Y1 - 2000/3

N2 - The acylase from Aspergillus melleus was able to hydrolyse the amide bond of (S)-phenylalanine-N-2-(R,S)-fluoropropionamide and discriminate the diastereoisomers such that the (S,S)-diastereoisomer was hydrolysed by an order of magnitude faster than the (S,R)diasteroisomer. The origin of the kinetic discrimination is attributed to both binding and kinetic effects. (C) 2000 Elsevier Science S.A. All rights reserved.

AB - The acylase from Aspergillus melleus was able to hydrolyse the amide bond of (S)-phenylalanine-N-2-(R,S)-fluoropropionamide and discriminate the diastereoisomers such that the (S,S)-diastereoisomer was hydrolysed by an order of magnitude faster than the (S,R)diasteroisomer. The origin of the kinetic discrimination is attributed to both binding and kinetic effects. (C) 2000 Elsevier Science S.A. All rights reserved.

KW - F-19-NMR

KW - acylase

KW - Aspergillus melleus

KW - alpha-fluoroamide

KW - enzyme resolution

KW - PYRIDINE

KW - FLUORINE

UR - https://www.scopus.com/pages/publications/0000118293

M3 - Article

SN - 0022-1139

VL - 102

SP - 235

EP - 238

JO - Journal of Fluorine Chemistry

JF - Journal of Fluorine Chemistry

ER -

The enzymatic resolution of an _- fluoroamide by an acylase

Abstract

Keywords

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