Supramolecular templating in kirromycin biosynthesis: the acyltransferase KirCII loads ethylmalonyl-CoA extender onto a specific ACP of the trans-AT PKS: Chemistry and Biology

Ewa M. Musiol; Thomas Härtner; Andreas Kulik; Jana Moldenhauer; Jörn Piel; Wolfgang Wohlleben; Tilmann Weber

doi:10.1016/j.chembiol.2011.02.007

Supramolecular templating in kirromycin biosynthesis: the acyltransferase KirCII loads ethylmalonyl-CoA extender onto a specific ACP of the trans-AT PKS: Chemistry and Biology

Ewa M. Musiol, Thomas Härtner, Andreas Kulik, Jana Moldenhauer, Jörn Piel, Wolfgang Wohlleben, Tilmann Weber

Research output: Contribution to journal › Journal article › Research › peer-review

Abstract

In the biosynthesis of complex polyketides, acyltransferase domains (ATs) are key determinants of structural diversity. Their specificity and position in polyketide synthases (PKSs) usually controls the location and structure of building blocks in polyketides. Many bioactive polyketides, however, are generated by trans-AT PKSs lacking internal AT domains. They were previously believed to use mainly malonyl-specific free-standing ATs. Here, we report a mechanism of structural diversification, in which the trans-AT KirCII regiospecifically incorporates the unusual extender unit ethylmalonyl-CoA in kirromycin polyketide biosynthesis.

Original language	English
Journal	Chemistry & Biology
Volume	18
Pages (from-to)	438-444
Number of pages	7
ISSN	1879-1301
DOIs	https://doi.org/10.1016/j.chembiol.2011.02.007
Publication status	Published - 2011
Externally published	Yes

Keywords

Acyl Carrier Protein/*metabolism Acyl Coenzyme A/*chemistry/*metabolism Acyltransferases/*chemistry/genetics/*metabolism Anti-Bacterial Agents/biosynthesis Polyketide Synthases/chemistry/*metabolism Protein Structure, Tertiary Pyridones/metabolism Stereoisomerism Streptomyces/genetics/metabolism Substrate Specificity

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10.1016/j.chembiol.2011.02.007

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title = "Supramolecular templating in kirromycin biosynthesis: the acyltransferase KirCII loads ethylmalonyl-CoA extender onto a specific ACP of the trans-AT PKS: Chemistry and Biology",

abstract = "In the biosynthesis of complex polyketides, acyltransferase domains (ATs) are key determinants of structural diversity. Their specificity and position in polyketide synthases (PKSs) usually controls the location and structure of building blocks in polyketides. Many bioactive polyketides, however, are generated by trans-AT PKSs lacking internal AT domains. They were previously believed to use mainly malonyl-specific free-standing ATs. Here, we report a mechanism of structural diversification, in which the trans-AT KirCII regiospecifically incorporates the unusual extender unit ethylmalonyl-CoA in kirromycin polyketide biosynthesis.",

keywords = "Acyl Carrier Protein/*metabolism Acyl Coenzyme A/*chemistry/*metabolism Acyltransferases/*chemistry/genetics/*metabolism Anti-Bacterial Agents/biosynthesis Polyketide Synthases/chemistry/*metabolism Protein Structure, Tertiary Pyridones/metabolism Stereoisomerism Streptomyces/genetics/metabolism Substrate Specificity",

author = "Musiol, {Ewa M.} and Thomas H{\"a}rtner and Andreas Kulik and Jana Moldenhauer and J{\"o}rn Piel and Wolfgang Wohlleben and Tilmann Weber",

year = "2011",

doi = "10.1016/j.chembiol.2011.02.007",

language = "English",

volume = "18",

pages = "438--444",

journal = "Chemistry & Biology",

issn = "1879-1301",

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Supramolecular templating in kirromycin biosynthesis: the acyltransferase KirCII loads ethylmalonyl-CoA extender onto a specific ACP of the trans-AT PKS: Chemistry and Biology. / Musiol, Ewa M.; Härtner, Thomas; Kulik, Andreas et al.
In: Chemistry & Biology, Vol. 18, 2011, p. 438-444.

Research output: Contribution to journal › Journal article › Research › peer-review

TY - JOUR

T1 - Supramolecular templating in kirromycin biosynthesis: the acyltransferase KirCII loads ethylmalonyl-CoA extender onto a specific ACP of the trans-AT PKS

T2 - Chemistry and Biology

AU - Musiol, Ewa M.

AU - Härtner, Thomas

AU - Kulik, Andreas

AU - Moldenhauer, Jana

AU - Piel, Jörn

AU - Wohlleben, Wolfgang

AU - Weber, Tilmann

PY - 2011

Y1 - 2011

N2 - In the biosynthesis of complex polyketides, acyltransferase domains (ATs) are key determinants of structural diversity. Their specificity and position in polyketide synthases (PKSs) usually controls the location and structure of building blocks in polyketides. Many bioactive polyketides, however, are generated by trans-AT PKSs lacking internal AT domains. They were previously believed to use mainly malonyl-specific free-standing ATs. Here, we report a mechanism of structural diversification, in which the trans-AT KirCII regiospecifically incorporates the unusual extender unit ethylmalonyl-CoA in kirromycin polyketide biosynthesis.

AB - In the biosynthesis of complex polyketides, acyltransferase domains (ATs) are key determinants of structural diversity. Their specificity and position in polyketide synthases (PKSs) usually controls the location and structure of building blocks in polyketides. Many bioactive polyketides, however, are generated by trans-AT PKSs lacking internal AT domains. They were previously believed to use mainly malonyl-specific free-standing ATs. Here, we report a mechanism of structural diversification, in which the trans-AT KirCII regiospecifically incorporates the unusual extender unit ethylmalonyl-CoA in kirromycin polyketide biosynthesis.

KW - Acyl Carrier Protein/metabolism Acyl Coenzyme A/chemistry/metabolism Acyltransferases/chemistry/genetics/metabolism Anti-Bacterial Agents/biosynthesis Polyketide Synthases/chemistry/metabolism Protein Structure, Tertiary Pyridones/metabolism Stereoisomeri

U2 - 10.1016/j.chembiol.2011.02.007

DO - 10.1016/j.chembiol.2011.02.007

M3 - Journal article

C2 - 21513880

SN - 1879-1301

VL - 18

SP - 438

EP - 444

JO - Chemistry & Biology

JF - Chemistry & Biology

ER -

Supramolecular templating in kirromycin biosynthesis: the acyltransferase KirCII loads ethylmalonyl-CoA extender onto a specific ACP of the trans-AT PKS: Chemistry and Biology

Abstract

Keywords

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