The use of an altered specificity engineered enzyme for asymmetric synthesis: enantioselective reduction of 4-methyl-2-oxopent-3-enoic acid

G  CASY; T V  LEE; H  LOVELL; B J  NICHOLS; R B  SESSIONS; J J  HOLBROOK

The use of an altered specificity engineered enzyme for asymmetric synthesis: enantioselective reduction of 4-methyl-2-oxopent-3-enoic acid

G CASY
, T V LEE
, H LOVELL
, B J NICHOLS
, R B SESSIONS
, J J HOLBROOK

Research output: Contribution to journal › Article (Academic Journal) › peer-review

11 Citations (Scopus)

Abstract

A genetically engineered version of Bacillus stearothermophilus lactate dehydrogenase, incorporating structural motifs which serve to alter substrate specificity in favour of alpha-keto acids with bulky aliphatic side chains, was used to effect enantioselective reduction of 4-methyl-2-oxopent-3-enoic acid.

Original language	English
Pages (from-to)	924-926
Number of pages	3
Journal	Journal of the Chemical Society: Chemical Communications
Volume	30
Issue number	13
Publication status	Published - 1 Jul 1992

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@article{466409f6290b41e28a5b03f25fa303d1,

title = "The use of an altered specificity engineered enzyme for asymmetric synthesis: enantioselective reduction of 4-methyl-2-oxopent-3-enoic acid",

abstract = "A genetically engineered version of Bacillus stearothermophilus lactate dehydrogenase, incorporating structural motifs which serve to alter substrate specificity in favour of alpha-keto acids with bulky aliphatic side chains, was used to effect enantioselective reduction of 4-methyl-2-oxopent-3-enoic acid.",

author = "G CASY and LEE, \{T V\} and H LOVELL and NICHOLS, \{B J\} and SESSIONS, \{R B\} and HOLBROOK, \{J J\}",

year = "1992",

month = jul,

day = "1",

language = "English",

volume = "30",

pages = "924--926",

journal = "Journal of the Chemical Society: Chemical Communications",

issn = "0022-4936",

publisher = "Royal Society of Chemistry",

number = "13",

}

The use of an altered specificity engineered enzyme for asymmetric synthesis: enantioselective reduction of 4-methyl-2-oxopent-3-enoic acid. / CASY, G ; LEE, T V ; LOVELL, H et al.
In: Journal of the Chemical Society: Chemical Communications, Vol. 30, No. 13, 01.07.1992, p. 924-926.

Research output: Contribution to journal › Article (Academic Journal) › peer-review

TY - JOUR

T1 - The use of an altered specificity engineered enzyme for asymmetric synthesis

T2 - enantioselective reduction of 4-methyl-2-oxopent-3-enoic acid

AU - CASY, G

AU - LEE, T V

AU - LOVELL, H

AU - NICHOLS, B J

AU - SESSIONS, R B

AU - HOLBROOK, J J

PY - 1992/7/1

Y1 - 1992/7/1

N2 - A genetically engineered version of Bacillus stearothermophilus lactate dehydrogenase, incorporating structural motifs which serve to alter substrate specificity in favour of alpha-keto acids with bulky aliphatic side chains, was used to effect enantioselective reduction of 4-methyl-2-oxopent-3-enoic acid.

AB - A genetically engineered version of Bacillus stearothermophilus lactate dehydrogenase, incorporating structural motifs which serve to alter substrate specificity in favour of alpha-keto acids with bulky aliphatic side chains, was used to effect enantioselective reduction of 4-methyl-2-oxopent-3-enoic acid.

M3 - Article (Academic Journal)

SN - 0022-4936

VL - 30

SP - 924

EP - 926

JO - Journal of the Chemical Society: Chemical Communications

JF - Journal of the Chemical Society: Chemical Communications

IS - 13

ER -

The use of an altered specificity engineered enzyme for asymmetric synthesis: enantioselective reduction of 4-methyl-2-oxopent-3-enoic acid

Abstract

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