Publication

Biochemical properties of a Pseudomonas aminotransferase involved in caprolactam metabolism

Palacio, C. M., Rozeboom, H. J., Lanfranchi, E., Meng, Q., Otzen, M. & Janssen, D. B., Oct-2019, In : The FEBS Journal. 286, 20, p. 4086-4102 17 p., 14950.

Research output: Contribution to journalArticleAcademicpeer-review

APA

Palacio, C. M., Rozeboom, H. J., Lanfranchi, E., Meng, Q., Otzen, M., & Janssen, D. B. (2019). Biochemical properties of a Pseudomonas aminotransferase involved in caprolactam metabolism. The FEBS Journal, 286(20), 4086-4102. [14950]. https://doi.org/10.1111/febs.14950

Author

Palacio, Cyntia M. ; Rozeboom, Henriëtte J. ; Lanfranchi, Elisa ; Meng, Qinglong ; Otzen, Marleen ; Janssen, Dick B. / Biochemical properties of a Pseudomonas aminotransferase involved in caprolactam metabolism. In: The FEBS Journal. 2019 ; Vol. 286, No. 20. pp. 4086-4102.

Harvard

Palacio, CM, Rozeboom, HJ, Lanfranchi, E, Meng, Q, Otzen, M & Janssen, DB 2019, 'Biochemical properties of a Pseudomonas aminotransferase involved in caprolactam metabolism', The FEBS Journal, vol. 286, no. 20, 14950, pp. 4086-4102. https://doi.org/10.1111/febs.14950

Standard

Biochemical properties of a Pseudomonas aminotransferase involved in caprolactam metabolism. / Palacio, Cyntia M.; Rozeboom, Henriëtte J.; Lanfranchi, Elisa; Meng, Qinglong; Otzen, Marleen; Janssen, Dick B.

In: The FEBS Journal, Vol. 286, No. 20, 14950, 10.2019, p. 4086-4102.

Research output: Contribution to journalArticleAcademicpeer-review

Vancouver

Palacio CM, Rozeboom HJ, Lanfranchi E, Meng Q, Otzen M, Janssen DB. Biochemical properties of a Pseudomonas aminotransferase involved in caprolactam metabolism. The FEBS Journal. 2019 Oct;286(20):4086-4102. 14950. https://doi.org/10.1111/febs.14950


BibTeX

@article{5a47474f43654a3bbb61238713f699cd,
title = "Biochemical properties of a Pseudomonas aminotransferase involved in caprolactam metabolism",
abstract = "The biodegradation of the nylon-6 precursor caprolactam by a strain of Pseudomonas jessenii proceeds via ATP-dependent hydrolytic ring-opening to 6-aminohexanoate. This non-natural ω-amino acid is converted to 6-oxohexanoic acid by an aminotransferase (PjAT) belonging to the fold type I PLP enzymes. To understand the structural basis of 6-aminohexanoatate conversion, we solved different crystal structures and determined the substrate scope with a range of aliphatic and aromatic amines. Comparison with the homologous aminotransferases from Chromobacterium violaceum (CvAT) and Vibrio fluvialis (VfAT) showed that the PjAT enzyme has the lowest KM values (highest affinity) and highest specificity constant (kcat /KM ) with the caprolactam degradation intermediates 6-aminohexanoate and 6-oxohexanoic acid, in accordance with its proposed in vivo function. Five distinct three-dimensional structures of PjAT were solved by protein crystallography. The structure of the aldimine intermediate formed from 6-aminohexanoate and the PLP cofactor revealed the presence of a narrow hydrophobic substrate-binding tunnel leading to the cofactor and covered by a flexible arginine, which explains the high activity and selectivity of the PjAT with 6-aminohexanoate. The results suggest that the degradation pathway for caprolactam has recruited an aminotransferase that is well adapted to 6-aminohexanoate degradation. This article is protected by copyright. All rights reserved.",
keywords = "Caprolactam, nylon 6, 6-aminohexanoic acid, deamination, aminotransferase, protein structure, substrate specificity, pyridoxal phosphate, LYSINE EPSILON-AMINOTRANSFERASE, AMINE-PYRUVATE TRANSAMINASE, SUBSTRATE-SPECIFICITY, CRYSTAL-STRUCTURES, VIBRIO-FLUVIALIS, ACTIVE-SITE, OMEGA-AMINOTRANSFERASE, ASYMMETRIC-SYNTHESIS, KINETIC RESOLUTION, WASTE-WATER",
author = "Palacio, {Cyntia M.} and Rozeboom, {Henri{\"e}tte J.} and Elisa Lanfranchi and Qinglong Meng and Marleen Otzen and Janssen, {Dick B.}",
note = "This article is protected by copyright. All rights reserved.",
year = "2019",
month = oct,
doi = "10.1111/febs.14950",
language = "English",
volume = "286",
pages = "4086--4102",
journal = "Febs Journal",
issn = "1742-464X",
publisher = "NLM (Medline)",
number = "20",

}

RIS

TY - JOUR

T1 - Biochemical properties of a Pseudomonas aminotransferase involved in caprolactam metabolism

AU - Palacio, Cyntia M.

AU - Rozeboom, Henriëtte J.

AU - Lanfranchi, Elisa

AU - Meng, Qinglong

AU - Otzen, Marleen

AU - Janssen, Dick B.

N1 - This article is protected by copyright. All rights reserved.

PY - 2019/10

Y1 - 2019/10

N2 - The biodegradation of the nylon-6 precursor caprolactam by a strain of Pseudomonas jessenii proceeds via ATP-dependent hydrolytic ring-opening to 6-aminohexanoate. This non-natural ω-amino acid is converted to 6-oxohexanoic acid by an aminotransferase (PjAT) belonging to the fold type I PLP enzymes. To understand the structural basis of 6-aminohexanoatate conversion, we solved different crystal structures and determined the substrate scope with a range of aliphatic and aromatic amines. Comparison with the homologous aminotransferases from Chromobacterium violaceum (CvAT) and Vibrio fluvialis (VfAT) showed that the PjAT enzyme has the lowest KM values (highest affinity) and highest specificity constant (kcat /KM ) with the caprolactam degradation intermediates 6-aminohexanoate and 6-oxohexanoic acid, in accordance with its proposed in vivo function. Five distinct three-dimensional structures of PjAT were solved by protein crystallography. The structure of the aldimine intermediate formed from 6-aminohexanoate and the PLP cofactor revealed the presence of a narrow hydrophobic substrate-binding tunnel leading to the cofactor and covered by a flexible arginine, which explains the high activity and selectivity of the PjAT with 6-aminohexanoate. The results suggest that the degradation pathway for caprolactam has recruited an aminotransferase that is well adapted to 6-aminohexanoate degradation. This article is protected by copyright. All rights reserved.

AB - The biodegradation of the nylon-6 precursor caprolactam by a strain of Pseudomonas jessenii proceeds via ATP-dependent hydrolytic ring-opening to 6-aminohexanoate. This non-natural ω-amino acid is converted to 6-oxohexanoic acid by an aminotransferase (PjAT) belonging to the fold type I PLP enzymes. To understand the structural basis of 6-aminohexanoatate conversion, we solved different crystal structures and determined the substrate scope with a range of aliphatic and aromatic amines. Comparison with the homologous aminotransferases from Chromobacterium violaceum (CvAT) and Vibrio fluvialis (VfAT) showed that the PjAT enzyme has the lowest KM values (highest affinity) and highest specificity constant (kcat /KM ) with the caprolactam degradation intermediates 6-aminohexanoate and 6-oxohexanoic acid, in accordance with its proposed in vivo function. Five distinct three-dimensional structures of PjAT were solved by protein crystallography. The structure of the aldimine intermediate formed from 6-aminohexanoate and the PLP cofactor revealed the presence of a narrow hydrophobic substrate-binding tunnel leading to the cofactor and covered by a flexible arginine, which explains the high activity and selectivity of the PjAT with 6-aminohexanoate. The results suggest that the degradation pathway for caprolactam has recruited an aminotransferase that is well adapted to 6-aminohexanoate degradation. This article is protected by copyright. All rights reserved.

KW - Caprolactam

KW - nylon 6

KW - 6-aminohexanoic acid

KW - deamination

KW - aminotransferase

KW - protein structure

KW - substrate specificity

KW - pyridoxal phosphate

KW - LYSINE EPSILON-AMINOTRANSFERASE

KW - AMINE-PYRUVATE TRANSAMINASE

KW - SUBSTRATE-SPECIFICITY

KW - CRYSTAL-STRUCTURES

KW - VIBRIO-FLUVIALIS

KW - ACTIVE-SITE

KW - OMEGA-AMINOTRANSFERASE

KW - ASYMMETRIC-SYNTHESIS

KW - KINETIC RESOLUTION

KW - WASTE-WATER

U2 - 10.1111/febs.14950

DO - 10.1111/febs.14950

M3 - Article

C2 - 31162815

VL - 286

SP - 4086

EP - 4102

JO - Febs Journal

JF - Febs Journal

SN - 1742-464X

IS - 20

M1 - 14950

ER -

ID: 84548213