Investigating nonribosomal peptide and polyketide biosynthesis by direct detection of intermediates on > 70 kDa polypeptides by using Fourier-transform mass spectrometry

Leslie M. Hicks; Matthew T. Mazur; Leah M. Miller; Pieter C. Dorrestein; Nathan A. Schnarr; Chaitan Khosla; Neil L. Kelleher

doi:10.1002/cbic.200500416

Investigating nonribosomal peptide and polyketide biosynthesis by direct detection of intermediates on > 70 kDa polypeptides by using Fourier-transform mass spectrometry

Leslie M. Hicks, Matthew T. Mazur, Leah M. Miller, Pieter C. Dorrestein, Nathan A. Schnarr, Chaitan Khosla, Neil L. Kelleher^*

^*Corresponding author for this work

Molecular Biosciences

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

20 Scopus citations

Abstract

Many therapeutic natural products emanate from NRPS and PKS enzymes, and there is an ongoing effort to engineer these systems for the generation of novel natural products. Here, direct interrogation by Fourier-transform mass spectrometry is extended to 70-127 kDa polypeptides as a robust method to investigate these megaenzymes and facilitate deeper fundamental understanding and rational engineering efforts.

Original language	English (US)
Pages (from-to)	904-907
Number of pages	4
Journal	ChemBioChem
Volume	7
Issue number	6
DOIs	https://doi.org/10.1002/cbic.200500416
State	Published - Jun 2006

Keywords

Biosynthesis
Fourier-transfrom mass spectrometry
Nonribosomal peptide synthesis
Polyketides
Protein modifications

ASJC Scopus subject areas

Molecular Medicine
Molecular Biology
Biochemistry
Organic Chemistry

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10.1002/cbic.200500416

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abstract = "Many therapeutic natural products emanate from NRPS and PKS enzymes, and there is an ongoing effort to engineer these systems for the generation of novel natural products. Here, direct interrogation by Fourier-transform mass spectrometry is extended to 70-127 kDa polypeptides as a robust method to investigate these megaenzymes and facilitate deeper fundamental understanding and rational engineering efforts.",

keywords = "Biosynthesis, Fourier-transfrom mass spectrometry, Nonribosomal peptide synthesis, Polyketides, Protein modifications",

author = "Hicks, {Leslie M.} and Mazur, {Matthew T.} and Miller, {Leah M.} and Dorrestein, {Pieter C.} and Schnarr, {Nathan A.} and Chaitan Khosla and Kelleher, {Neil L.}",

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AU - Hicks, Leslie M.

AU - Mazur, Matthew T.

AU - Miller, Leah M.

AU - Dorrestein, Pieter C.

AU - Schnarr, Nathan A.

AU - Khosla, Chaitan

AU - Kelleher, Neil L.

PY - 2006/6

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N2 - Many therapeutic natural products emanate from NRPS and PKS enzymes, and there is an ongoing effort to engineer these systems for the generation of novel natural products. Here, direct interrogation by Fourier-transform mass spectrometry is extended to 70-127 kDa polypeptides as a robust method to investigate these megaenzymes and facilitate deeper fundamental understanding and rational engineering efforts.

AB - Many therapeutic natural products emanate from NRPS and PKS enzymes, and there is an ongoing effort to engineer these systems for the generation of novel natural products. Here, direct interrogation by Fourier-transform mass spectrometry is extended to 70-127 kDa polypeptides as a robust method to investigate these megaenzymes and facilitate deeper fundamental understanding and rational engineering efforts.

KW - Biosynthesis

KW - Fourier-transfrom mass spectrometry

KW - Nonribosomal peptide synthesis

KW - Polyketides

KW - Protein modifications

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Investigating nonribosomal peptide and polyketide biosynthesis by direct detection of intermediates on > 70 kDa polypeptides by using Fourier-transform mass spectrometry

Abstract

Keywords

ASJC Scopus subject areas

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