Characterization of the Suillus grevillei Quinone Synthetase GreA Supports a Nonribosomal Code for Aromatic α-Keto Acids

B. Wackler, G. Lackner, Heng Chooi, D. Hoffmeister

Research output: Contribution to journalArticle

23 Citations (Scopus)

Abstract

The gene greA was cloned from the genome of the basidiomycete Suillus grevillei. It encodes a monomodular natural product biosynthesis protein composed of three domains for adenylation, thiolation, and thioesterase and, hence, is reminiscent of a nonribosomal peptide synthetase (NRPS). GreA was biochemically characterized in vitro. It was identified as atromentin synthetase and therefore represents one of only a limited number of biochemically characterized NRPS-like enzymes which accept an aromatic α-keto acid. Specificity-conferring amino acid residues-collectively referred to as the nonribosomal code-were predicted for the primary sequence of the GreA adenylation domain and were an unprecedented combination for aromatic α-keto acids. Plausible support for this new code came from in silico simulation of the adenylation domain structure. According to the model, the predicted residues line the active site and, therefore, very likely contribute to substrate specificity. © 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
Original languageEnglish
Pages (from-to)1798-1804
JournalChemBioChem
Volume13
Issue number12
DOIs
Publication statusPublished - 2012

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Peptide Synthases
Keto Acids
Ligases
Carboxylic acids
Genes
Basidiomycota
Biosynthesis
Protein Biosynthesis
Substrate Specificity
Biological Products
Computer Simulation
Catalytic Domain
Genome
Amino Acids
Substrates
Enzymes
Proteins
benzoquinone
atromentin
In Vitro Techniques

Cite this

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title = "Characterization of the Suillus grevillei Quinone Synthetase GreA Supports a Nonribosomal Code for Aromatic α-Keto Acids",
abstract = "The gene greA was cloned from the genome of the basidiomycete Suillus grevillei. It encodes a monomodular natural product biosynthesis protein composed of three domains for adenylation, thiolation, and thioesterase and, hence, is reminiscent of a nonribosomal peptide synthetase (NRPS). GreA was biochemically characterized in vitro. It was identified as atromentin synthetase and therefore represents one of only a limited number of biochemically characterized NRPS-like enzymes which accept an aromatic α-keto acid. Specificity-conferring amino acid residues-collectively referred to as the nonribosomal code-were predicted for the primary sequence of the GreA adenylation domain and were an unprecedented combination for aromatic α-keto acids. Plausible support for this new code came from in silico simulation of the adenylation domain structure. According to the model, the predicted residues line the active site and, therefore, very likely contribute to substrate specificity. {\circledC} 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.",
author = "B. Wackler and G. Lackner and Heng Chooi and D. Hoffmeister",
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pages = "1798--1804",
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Characterization of the Suillus grevillei Quinone Synthetase GreA Supports a Nonribosomal Code for Aromatic α-Keto Acids. / Wackler, B.; Lackner, G.; Chooi, Heng; Hoffmeister, D.

In: ChemBioChem, Vol. 13, No. 12, 2012, p. 1798-1804.

Research output: Contribution to journalArticle

TY - JOUR

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AU - Lackner, G.

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AU - Hoffmeister, D.

PY - 2012

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AB - The gene greA was cloned from the genome of the basidiomycete Suillus grevillei. It encodes a monomodular natural product biosynthesis protein composed of three domains for adenylation, thiolation, and thioesterase and, hence, is reminiscent of a nonribosomal peptide synthetase (NRPS). GreA was biochemically characterized in vitro. It was identified as atromentin synthetase and therefore represents one of only a limited number of biochemically characterized NRPS-like enzymes which accept an aromatic α-keto acid. Specificity-conferring amino acid residues-collectively referred to as the nonribosomal code-were predicted for the primary sequence of the GreA adenylation domain and were an unprecedented combination for aromatic α-keto acids. Plausible support for this new code came from in silico simulation of the adenylation domain structure. According to the model, the predicted residues line the active site and, therefore, very likely contribute to substrate specificity. © 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

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