Publication

Characterization of the caprolactam degradation pathway in Pseudomonas jessenii using mass spectrometry-based proteomics

Otzen, M., Palacio, C. & Janssen, D. B., Aug-2018, In : Applied Microbiology and Biotechnology. 15, p. 6699-6711 13 p.

Research output: Contribution to journalArticleAcademicpeer-review

APA

Otzen, M., Palacio, C., & Janssen, D. B. (2018). Characterization of the caprolactam degradation pathway in Pseudomonas jessenii using mass spectrometry-based proteomics. Applied Microbiology and Biotechnology, 15, 6699-6711. https://doi.org/10.1007/s00253-018-9073-7

Author

Otzen, Marleen ; Palacio, Cyntia ; Janssen, Dick B. / Characterization of the caprolactam degradation pathway in Pseudomonas jessenii using mass spectrometry-based proteomics. In: Applied Microbiology and Biotechnology. 2018 ; Vol. 15. pp. 6699-6711.

Harvard

Otzen, M, Palacio, C & Janssen, DB 2018, 'Characterization of the caprolactam degradation pathway in Pseudomonas jessenii using mass spectrometry-based proteomics', Applied Microbiology and Biotechnology, vol. 15, pp. 6699-6711. https://doi.org/10.1007/s00253-018-9073-7

Standard

Characterization of the caprolactam degradation pathway in Pseudomonas jessenii using mass spectrometry-based proteomics. / Otzen, Marleen; Palacio, Cyntia; Janssen, Dick B.

In: Applied Microbiology and Biotechnology, Vol. 15, 08.2018, p. 6699-6711.

Research output: Contribution to journalArticleAcademicpeer-review

Vancouver

Otzen M, Palacio C, Janssen DB. Characterization of the caprolactam degradation pathway in Pseudomonas jessenii using mass spectrometry-based proteomics. Applied Microbiology and Biotechnology. 2018 Aug;15:6699-6711. https://doi.org/10.1007/s00253-018-9073-7


BibTeX

@article{e292e9e119e54996aecd28580a57941e,
title = "Characterization of the caprolactam degradation pathway in Pseudomonas jessenii using mass spectrometry-based proteomics",
abstract = "Some bacterial cultures are capable of growth on caprolactam as sole carbon and nitrogen source, but the enzymes of the catabolic pathway have not been described. We isolated a caprolactam-degrading strain of Pseudomonas jessenii from soil and identified proteins and genes putatively involved in caprolactam metabolism using quantitative mass spectrometry-based proteomics. This led to the discovery of a caprolactamase and an aminotransferase that are involved in the initial steps of caprolactam conversion. Additionally, various proteins were identified that likely are involved in later steps of the pathway. The caprolactamase consists of two subunits and demonstrated high sequence identity to the 5-oxoprolinases. Escherichia coli cells expressing this caprolactamase did not convert 5-oxoproline but were able to hydrolyze caprolactam to form 6-aminocaproic acid in an ATP-dependent manner. Characterization of the aminotransferase revealed that the enzyme deaminates 6-aminocaproic acid to produce 6-oxohexanoate with pyruvate as amino acceptor. The amino acid sequence of the aminotransferase showed high similarity to subgroup II ω-aminotransferases of the PLP-fold type I proteins. Finally, analyses of the genome sequence revealed the presence of a caprolactam catabolism gene cluster comprising a set of genes involved in the conversion of caprolactam to adipate.",
keywords = "Caprolactam, Caprolactamase, Omega aminostransferase, Mass spectrometry, proteomics, Pseudomonas jessenii",
author = "Marleen Otzen and Cyntia Palacio and Janssen, {Dick B}",
year = "2018",
month = aug,
doi = "10.1007/s00253-018-9073-7",
language = "English",
volume = "15",
pages = "6699--6711",
journal = "Applied Microbiology and Biotechnology",
issn = "0175-7598",
publisher = "SPRINGER",

}

RIS

TY - JOUR

T1 - Characterization of the caprolactam degradation pathway in Pseudomonas jessenii using mass spectrometry-based proteomics

AU - Otzen, Marleen

AU - Palacio, Cyntia

AU - Janssen, Dick B

PY - 2018/8

Y1 - 2018/8

N2 - Some bacterial cultures are capable of growth on caprolactam as sole carbon and nitrogen source, but the enzymes of the catabolic pathway have not been described. We isolated a caprolactam-degrading strain of Pseudomonas jessenii from soil and identified proteins and genes putatively involved in caprolactam metabolism using quantitative mass spectrometry-based proteomics. This led to the discovery of a caprolactamase and an aminotransferase that are involved in the initial steps of caprolactam conversion. Additionally, various proteins were identified that likely are involved in later steps of the pathway. The caprolactamase consists of two subunits and demonstrated high sequence identity to the 5-oxoprolinases. Escherichia coli cells expressing this caprolactamase did not convert 5-oxoproline but were able to hydrolyze caprolactam to form 6-aminocaproic acid in an ATP-dependent manner. Characterization of the aminotransferase revealed that the enzyme deaminates 6-aminocaproic acid to produce 6-oxohexanoate with pyruvate as amino acceptor. The amino acid sequence of the aminotransferase showed high similarity to subgroup II ω-aminotransferases of the PLP-fold type I proteins. Finally, analyses of the genome sequence revealed the presence of a caprolactam catabolism gene cluster comprising a set of genes involved in the conversion of caprolactam to adipate.

AB - Some bacterial cultures are capable of growth on caprolactam as sole carbon and nitrogen source, but the enzymes of the catabolic pathway have not been described. We isolated a caprolactam-degrading strain of Pseudomonas jessenii from soil and identified proteins and genes putatively involved in caprolactam metabolism using quantitative mass spectrometry-based proteomics. This led to the discovery of a caprolactamase and an aminotransferase that are involved in the initial steps of caprolactam conversion. Additionally, various proteins were identified that likely are involved in later steps of the pathway. The caprolactamase consists of two subunits and demonstrated high sequence identity to the 5-oxoprolinases. Escherichia coli cells expressing this caprolactamase did not convert 5-oxoproline but were able to hydrolyze caprolactam to form 6-aminocaproic acid in an ATP-dependent manner. Characterization of the aminotransferase revealed that the enzyme deaminates 6-aminocaproic acid to produce 6-oxohexanoate with pyruvate as amino acceptor. The amino acid sequence of the aminotransferase showed high similarity to subgroup II ω-aminotransferases of the PLP-fold type I proteins. Finally, analyses of the genome sequence revealed the presence of a caprolactam catabolism gene cluster comprising a set of genes involved in the conversion of caprolactam to adipate.

KW - Caprolactam

KW - Caprolactamase

KW - Omega aminostransferase

KW - Mass spectrometry

KW - proteomics

KW - Pseudomonas jessenii

U2 - 10.1007/s00253-018-9073-7

DO - 10.1007/s00253-018-9073-7

M3 - Article

C2 - 29850960

VL - 15

SP - 6699

EP - 6711

JO - Applied Microbiology and Biotechnology

JF - Applied Microbiology and Biotechnology

SN - 0175-7598

ER -

ID: 61402700