ArticleMicrobial biotechnology2015
Identification of novel transaminases from a 12-aminododecanoic acid-metabolizing Pseudomonas strain.
Article in Microbial biotechnology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
7 citing papers in PubMed, 21 citations in OpenAlex.
- Development of A Spectrometric Enzyme-Coupled Assay for 11-Aminoundecanoic Acid Transaminase and Its Detection inmicroPublication biology · 2026Article
- Transaminases for industrial biocatalysis: novel enzyme discovery.Applied microbiology and biotechnology · 2020Review
- The biotechnological potential of marine bacteria in the novel lineage of Pseudomonas pertucinogena.Microbial biotechnology · 2020Review
- Computer-Guided Surface Engineering for Enzyme Improvement.Scientific reports · 2018Article
- Amine transaminases in chiral amines synthesis: recent advances and challenges.World journal of microbiology & biotechnology · 2017Review
- Crystal structure of a putrescine aminotransferase from Pseudomonas sp. strain AAC.Acta crystallographica. Section F, Structural biology communications · 2017Article
- A β-Alanine Catabolism Pathway Containing a Highly Promiscuous ω-Transaminase in the 12-Aminododecanate-Degrading Pseudomonas sp. Strain AAC.Applied and environmental microbiology · 2016Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A Pseudomonas species [Pseudomonas sp. strain amino alkanoate catabolism (AAC)] was identified that has the capacity to use 12-aminododecanoic acid, the constituent building block of homo-nylon-12, as a sole nitrogen source. Growth of Pseudomonas sp. strain AAC could also be supported using a range of additional ω-amino alkanoates. This metabolic function was shown to be most probably dependent upon one or more transaminases (TAs). Fourteen genes encoding putative TAs were identified from the genome of Pseudomonas sp. AAC. Each of the 14 genes was cloned, 11 of which were successfully expressed in Escherichia coli and tested for activity against 12-aminododecanoic acid. In addition, physiological functions were proposed for 9 of the 14 TAs. Of the 14 proteins, activity was demonstrated in 9, and of note, 3 TAs were shown to be able to catalyse the transfer of the ω-amine from 12-aminododecanoic acid to pyruvate. Based on this study, three enzymes have been identified that are promising biocatalysts for the production of nylon and related polymers.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.