Bacterial Anabaena variabilis phenylalanine ammonia lyase: A biocatalyst with broad substrate specificityCitation formats

Standard

Bacterial Anabaena variabilis phenylalanine ammonia lyase: A biocatalyst with broad substrate specificity. / Lovelock, Sarah; Turner, Nicholas.

In: Bioorganic and Medicinal Chemistry, Vol. 22, No. 20, 2014, p. 5555-5557.

Research output: Contribution to journalArticle

Harvard

APA

Vancouver

Author

Lovelock, Sarah ; Turner, Nicholas. / Bacterial Anabaena variabilis phenylalanine ammonia lyase: A biocatalyst with broad substrate specificity. In: Bioorganic and Medicinal Chemistry. 2014 ; Vol. 22, No. 20. pp. 5555-5557.

Bibtex

@article{14c0ce9a5eb7468a9f03e0e3f2ce432b,
title = "Bacterial Anabaena variabilis phenylalanine ammonia lyase: A biocatalyst with broad substrate specificity",
abstract = "Phenylalanine ammonia lyases (PALs) catalyse the regio- and stereoselective hydroamination of cinnamic acid analogues to yield optically enriched α-amino acids. Herein, we demonstrate that a bacterial PAL from Anabaena variabilis (AvPAL) displays significantly higher activity towards a series of non-natural substrates than previously described eukaryotic PALs. Biotransformations performed on a preparative scale led to the synthesis of the 2-chloro- and 4-trifluoromethyl-phenylalanine derivatives in excellent ee, highlighting the enormous potential of bacterial PALs as biocatalysts for the synthesis of high value, non-natural amino acids.",
author = "Sarah Lovelock and Nicholas Turner",
year = "2014",
doi = "10.1016/j.bmc.2014.06.035",
language = "English",
volume = "22",
pages = "5555--5557",
journal = "Bioorganic & Medicinal Chemistry",
issn = "0968-0896",
publisher = "Elsevier BV",
number = "20",

}

RIS

TY - JOUR

T1 - Bacterial Anabaena variabilis phenylalanine ammonia lyase: A biocatalyst with broad substrate specificity

AU - Lovelock, Sarah

AU - Turner, Nicholas

PY - 2014

Y1 - 2014

N2 - Phenylalanine ammonia lyases (PALs) catalyse the regio- and stereoselective hydroamination of cinnamic acid analogues to yield optically enriched α-amino acids. Herein, we demonstrate that a bacterial PAL from Anabaena variabilis (AvPAL) displays significantly higher activity towards a series of non-natural substrates than previously described eukaryotic PALs. Biotransformations performed on a preparative scale led to the synthesis of the 2-chloro- and 4-trifluoromethyl-phenylalanine derivatives in excellent ee, highlighting the enormous potential of bacterial PALs as biocatalysts for the synthesis of high value, non-natural amino acids.

AB - Phenylalanine ammonia lyases (PALs) catalyse the regio- and stereoselective hydroamination of cinnamic acid analogues to yield optically enriched α-amino acids. Herein, we demonstrate that a bacterial PAL from Anabaena variabilis (AvPAL) displays significantly higher activity towards a series of non-natural substrates than previously described eukaryotic PALs. Biotransformations performed on a preparative scale led to the synthesis of the 2-chloro- and 4-trifluoromethyl-phenylalanine derivatives in excellent ee, highlighting the enormous potential of bacterial PALs as biocatalysts for the synthesis of high value, non-natural amino acids.

U2 - 10.1016/j.bmc.2014.06.035

DO - 10.1016/j.bmc.2014.06.035

M3 - Article

VL - 22

SP - 5555

EP - 5557

JO - Bioorganic & Medicinal Chemistry

JF - Bioorganic & Medicinal Chemistry

SN - 0968-0896

IS - 20

ER -