Identification of novel transaminases from a 12‐aminododecanoic acid‐metabolizing Pseudomonas strain |
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| Authors: | Matthew Wilding Ellen F. A. Walsh Susan J. Dorrian Colin Scott |
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| Affiliation: | 1. CSIRO Land and Water Flagship, Black Mountain, Canberra, ACT, Australia;2. CSIRO Food and Nutrition Flagship, Black Mountain, Canberra, ACT, Australia;3. Research School of Chemistry, Australian National University, Canberra, ACT, Australia |
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| 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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