Nonactin biosynthesis: The product of the resistance gene degrades nonactin stereospecifically to form homochiral nonactate dimers

James E. Cox; Nigel D. Priestley

doi:10.1021/ja050068k

Nonactin biosynthesis: The product of the resistance gene degrades nonactin stereospecifically to form homochiral nonactate dimers

James E. Cox, Nigel D. Priestley

University of Montana

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

10 Scopus citations

Abstract

Heterologous expression of the tetranactin resistance gene nonR in E. coli gave a his6-tagged protein that catalyzed the stereoselective hydrolysis of the chiral macrotetrolide antibiotic nonactin into equivalent, chiral, inactive nonactate dimer species. No trimeric nonactate was produced in the reaction.

Original language	English
Pages (from-to)	7976-7977
Number of pages	2
Journal	Journal of the American Chemical Society
Volume	127
Issue number	22
DOIs	https://doi.org/10.1021/ja050068k
State	Published - Jun 8 2005

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title = "Nonactin biosynthesis: The product of the resistance gene degrades nonactin stereospecifically to form homochiral nonactate dimers",

abstract = "Heterologous expression of the tetranactin resistance gene nonR in E. coli gave a his6-tagged protein that catalyzed the stereoselective hydrolysis of the chiral macrotetrolide antibiotic nonactin into equivalent, chiral, inactive nonactate dimer species. No trimeric nonactate was produced in the reaction.",

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year = "2005",

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AU - Cox, James E.

AU - Priestley, Nigel D.

PY - 2005/6/8

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N2 - Heterologous expression of the tetranactin resistance gene nonR in E. coli gave a his6-tagged protein that catalyzed the stereoselective hydrolysis of the chiral macrotetrolide antibiotic nonactin into equivalent, chiral, inactive nonactate dimer species. No trimeric nonactate was produced in the reaction.

AB - Heterologous expression of the tetranactin resistance gene nonR in E. coli gave a his6-tagged protein that catalyzed the stereoselective hydrolysis of the chiral macrotetrolide antibiotic nonactin into equivalent, chiral, inactive nonactate dimer species. No trimeric nonactate was produced in the reaction.

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U2 - 10.1021/ja050068k

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SN - 0002-7863

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JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

IS - 22

ER -

Nonactin biosynthesis: The product of the resistance gene degrades nonactin stereospecifically to form homochiral nonactate dimers

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