Metabolic pathway of 6-aminohexanoate in the nylon oligomer-degrading bacterium Arthrobacter sp. KI72: identification of the enzymes responsible for the conversion of 6-aminohexanoate to adipate

Takehara, Ikki; Fujii, Tsubasa; Tanimoto, Yuuki; Kato, Dai‐ichiro; Takeo, Masahiro; Negoro, Seiji

doi:10.1007/s00253-017-8657-y

Cited by 19 publications

(13 citation statements)

References 42 publications

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“…Thus, in comparison to Orn-AT, PjAT has a different mechanism for rejecting a-amino acids and ketoglutarate as substrates. PjAT is also different from the 6-AHA-deaminating aminotransferase proposed by Takehara et al [9] to be involved in 6-AHA degradation by Arthrobacter sp. KI72.…”

Section: Discussioncontrasting

confidence: 73%

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Biochemical properties of a Pseudomonas aminotransferase involved in caprolactam metabolism

et al. 2019

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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 pyridoxal 5′‐phosphate (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. Database The atomic coordinates and structure factors P. jessenii 6‐aminohexanoate aminotransferase have been deposited in the PDB as entries http://www.rcsb.org/pdb/search/structidSearch.do?structureId=6G4B (E∙succinate complex), http://www.rcsb.org/pdb/search/structidSearch.do?structureId=6G4C (E∙phosphate complex), http://www.rcsb.org/pdb/search/structidSearch.do?structureId=6G4D (E∙PLP complex), http://www.rcsb.org/pdb/search/structidSearch.do?structureId=6G4E (E∙PLP‐6‐aminohexanoate intermediate), and http://www.rcsb.org/pdb/search/structidSearch.do?structureId=6G4F (E∙PMP complex).

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Section: Discussioncontrasting

confidence: 73%

“…Pj AT is also different from the 6‐AHA‐deaminating aminotransferase proposed by Takehara et al . to be involved in 6‐AHA degradation by Arthrobacter sp. KI72.…”

Section: Discussionmentioning

confidence: 99%

Biochemical properties of a Pseudomonas aminotransferase involved in caprolactam metabolism

et al. 2019

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“…The Pj AT aminotransferase has 27.3% pairwise sequence identity with the NylD1 aminotransferase recently described in the nylon oligomer degrader Arthrobacter sp. KI72 (Takehara et al 2018). The closest homolog of the latter enzyme in the P. jessenii genome is ORF2380 (48.6% pairwise identify), but an upregulation of this protein was not detected by proteomic analysis of caprolactam-grown P. jessenii cultures.…”

Section: Discussionmentioning

confidence: 99%

“…NCIMB 9871. Subsequently, an aminotransferase might catalyze the conversion of 6-ACA to 6-oxohexanoate in the cell (Takehara et al 2018 ; Iwaki et al 1999 ).…”

Section: Introductionmentioning

confidence: 99%

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

Otzen

Palacio

Janssen

2018

Appl Microbiol Biotechnol

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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.Electronic supplementary materialThe online version of this article (10.1007/s00253-018-9073-7) contains supplementary material, which is available to authorized users.

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“…Metabolism of 11-aminoundecanoic acid has never been reported. A recent study of the cellular metabolism of 6-aminohexanoate (the hydrolysis product of nylon 6) identified involvement of 5-aminovalerate aminotransferase/ Gammaaminbutyrate:alpha-ketoglutarate aminotransferase (NylD) [28]. While 6-aminohexanoate and 11aminoundecanoic acid differs significantly in the length of carbon chain (i.e.…”

Section: Resultsmentioning

confidence: 99%

Isolation and genomic analysis of 11-aminoundecanoic acid-degrading bacterium Pseudomonas sp. JG-B from nylon 11 enrichment culture

Gatz-Schrupp¹,

Deckard²,

Hufford³

et al. 2020

J. Genomics

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Nylon 11 is a polymer synthesized from 11-aminoundecanoic acid, and widely used in commercial manufacturing. In this study, we describe the isolation of the first organism capable of metabolizing 11-aminoundecanoic acid from nylon 11 enrichment culture. The strain shows rapid growth on 11-aminoundecanoic acid as a sole source of carbon, nitrogen, and energy. Furthermore, the genome sequence of strain JG-B was deciphered and shown to belong to genus Pseudomonas. Many genes encoding putative extracellular hydrolases, as well as homologues of nylon 6 hydrolases (NylB and NylA) were identified, suggesting the metabolic versatility and possibility that this organism could also depolymerase nylon 11 polymers.

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Metabolic pathway of 6-aminohexanoate in the nylon oligomer-degrading bacterium Arthrobacter sp. KI72: identification of the enzymes responsible for the conversion of 6-aminohexanoate to adipate

Cited by 19 publications

References 42 publications

Biochemical properties of a Pseudomonas aminotransferase involved in caprolactam metabolism

Biochemical properties of a Pseudomonas aminotransferase involved in caprolactam metabolism

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

Isolation and genomic analysis of 11-aminoundecanoic acid-degrading bacterium Pseudomonas sp. JG-B from nylon 11 enrichment culture

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