4UHO
Characterization of a Novel Transaminase from Pseudomonas sp. Strain AAC
Summary for 4UHO
| Entry DOI | 10.2210/pdb4uho/pdb |
| Related | 4UHM 4UHN |
| Descriptor | OMEGA AMINO ACID-PYRUVATE AMINOTRANSFERASE, UNKNOWN LIGAND, MAGNESIUM ION, ... (9 entities in total) |
| Functional Keywords | transferase, biocatalysis, aminotransferase, pyridoxal-5'-phosphate |
| Biological source | PSEUDOMONAS SP. |
| Total number of polymer chains | 1 |
| Total formula weight | 51516.79 |
| Authors | Wilding, M.,Peat, T.S.,Newman, J.,Scott, C. (deposition date: 2015-03-25, release date: 2016-04-13, Last modification date: 2024-01-10) |
| Primary citation | Wilding, M.,Peat, T.S.,Newman, J.,Scott, C. A Beta-Alanine Catabolism Pathway Containing a Highly Promiscuous Omega-Transaminase in the 12-Aminododecanate-Degrading Pseudomonas Sp. Strain Aac. Appl.Environ.Microbiol., 82:3846-, 2016 Cited by PubMed Abstract: We previously isolated the transaminase KES23458 from Pseudomonas sp. strain AAC as a promising biocatalyst for the production of 12-aminododecanoic acid, a constituent building block of nylon-12. Here, we report the subsequent characterization of this transaminase. It exhibits activity with a broad substrate range which includes α-, β-, and ω-amino acids, as well as α,ω-diamines and a number of other industrially relevant compounds. It is therefore a prospective candidate for the biosynthesis of a range of polyamide monomers. The crystal structure of KES23458 revealed that the protein forms a dimer containing a large active site pocket and unusual phosphorylated histidine residues. To infer the physiological role of the transaminase, we expressed, purified, and characterized a dehydrogenase from the same operon, KES23460. Unlike the transaminase, the dehydrogenase was shown to be quite selective, catalyzing the oxidation of malonic acid semialdehyde, formed from β-alanine transamination via KES23458. In keeping with previous reports, the dehydrogenase was shown to catalyze both a coenzyme A (CoA)-dependent reaction to form acetyl-CoA and a significantly slower CoA-independent reaction to form acetate. These findings support the original functional assignment of KES23458 as a β-alanine transaminase. However, a seemingly well-adapted active site and promiscuity toward unnatural compounds, such as 12-aminododecanoic acid, suggest that this enzyme could perform multiple functions for Pseudomonas sp. strain AAC. PubMed: 27107110DOI: 10.1128/AEM.00665-16 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.24 Å) |
Structure validation
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