Enantioselective desymmetrisation of citric acid catalysed by the substrate-tolerant petrobactin biosynthetic enzyme AsbA

Daniel Oves-Costales; Lijiang Song; Gregory L. Challis

doi:10.1039/b823147h

Enantioselective desymmetrisation of citric acid catalysed by the substrate-tolerant petrobactin biosynthetic enzyme AsbA

Daniel Oves-Costales, Lijiang Song, Gregory L. Challis

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

16 Citations (Scopus)

Abstract

AsbA catalyses the highly enantioselective desymmetrisation of citric acid via ATP-dependent condensation with spermidine, as well as the condensation of citric acid with several spermidine analogues and the condensation of the citric acid analogue tricarballylic acid with spermidine, suggesting that it may be a useful biocatalyst for asymmetric synthesis.

Original language	English
Pages (from-to)	1389-1391
Number of pages	3
Journal	Chemical Communications
Issue number	11
DOIs	https://doi.org/10.1039/b823147h
Publication status	Published - 2009
Externally published	Yes

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abstract = "AsbA catalyses the highly enantioselective desymmetrisation of citric acid via ATP-dependent condensation with spermidine, as well as the condensation of citric acid with several spermidine analogues and the condensation of the citric acid analogue tricarballylic acid with spermidine, suggesting that it may be a useful biocatalyst for asymmetric synthesis.",

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AU - Challis, Gregory L.

PY - 2009

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AB - AsbA catalyses the highly enantioselective desymmetrisation of citric acid via ATP-dependent condensation with spermidine, as well as the condensation of citric acid with several spermidine analogues and the condensation of the citric acid analogue tricarballylic acid with spermidine, suggesting that it may be a useful biocatalyst for asymmetric synthesis.

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Enantioselective desymmetrisation of citric acid catalysed by the substrate-tolerant petrobactin biosynthetic enzyme AsbA

Abstract

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