Esterase catalysed enantioselective ring closure

C. Vivienne Barker; Stewart R. Korn; Michael Monteith; Michael I. Page

doi:10.1039/A901204D

Esterase catalysed enantioselective ring closure

C. Vivienne Barker, Stewart R. Korn, Michael Monteith, Michael I. Page

School of Applied Sciences

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

10 Citations (Scopus)

Abstract

Porcine liver esterase catalyses the reaction of γ-amino esters in water to give a mixture of the corresponding γ-lactam and the hydrolysis product, deacylation of the acyl enzyme intermediate by ring closure occurs with a high enantioselectivity giving an ee of 90% for the formation of (S)-5-phenyl-2-pyrrolidone from racemic ethyl 4-phenyl-4-aminobutanoate.

Original language	English
Pages (from-to)	721-722
Number of pages	2
Journal	Chemical Communications
Issue number	8
DOIs	https://doi.org/10.1039/A901204D
Publication status	Published - 21 Apr 1999

Access to Document

10.1039/A901204D

Cite this

@article{c73893c832594344bb03c4d51d3952ca,

title = "Esterase catalysed enantioselective ring closure",

abstract = "Porcine liver esterase catalyses the reaction of γ-amino esters in water to give a mixture of the corresponding γ-lactam and the hydrolysis product, deacylation of the acyl enzyme intermediate by ring closure occurs with a high enantioselectivity giving an ee of 90% for the formation of (S)-5-phenyl-2-pyrrolidone from racemic ethyl 4-phenyl-4-aminobutanoate.",

author = "Barker, {C. Vivienne} and Korn, {Stewart R.} and Michael Monteith and Page, {Michael I.}",

year = "1999",

month = apr,

day = "21",

doi = "10.1039/A901204D",

language = "English",

pages = "721--722",

journal = "Chemical Communications",

issn = "1359-7345",

publisher = "Royal Society of Chemistry",

number = "8",

}

TY - JOUR

T1 - Esterase catalysed enantioselective ring closure

AU - Barker, C. Vivienne

AU - Korn, Stewart R.

AU - Monteith, Michael

AU - Page, Michael I.

PY - 1999/4/21

Y1 - 1999/4/21

N2 - Porcine liver esterase catalyses the reaction of γ-amino esters in water to give a mixture of the corresponding γ-lactam and the hydrolysis product, deacylation of the acyl enzyme intermediate by ring closure occurs with a high enantioselectivity giving an ee of 90% for the formation of (S)-5-phenyl-2-pyrrolidone from racemic ethyl 4-phenyl-4-aminobutanoate.

AB - Porcine liver esterase catalyses the reaction of γ-amino esters in water to give a mixture of the corresponding γ-lactam and the hydrolysis product, deacylation of the acyl enzyme intermediate by ring closure occurs with a high enantioselectivity giving an ee of 90% for the formation of (S)-5-phenyl-2-pyrrolidone from racemic ethyl 4-phenyl-4-aminobutanoate.

UR - http://www.scopus.com/inward/record.url?scp=0033590967&partnerID=8YFLogxK

U2 - 10.1039/A901204D

DO - 10.1039/A901204D

M3 - Article

AN - SCOPUS:0033590967

SP - 721

EP - 722

JO - Chemical Communications

JF - Chemical Communications

SN - 1359-7345

IS - 8

ER -

Esterase catalysed enantioselective ring closure

Abstract

Access to Document

Other files and links

Fingerprint

Cite this