5IKH
Tobacco 5-epi-aristolochene synthase M4 mutant with (-)-premnaspirodiene
Summary for 5IKH
| Entry DOI | 10.2210/pdb5ikh/pdb |
| Related | 5IK0 5IK6 5IK9 5IKA 5IL3 5IL8 5ILD 5ILH 5ILI 5ILJ 5ILK 5ILY 5ILZ 5IM1 |
| Descriptor | 5-epi-aristolochene synthase, (2R,5S,10R)-6,10-dimethyl-2-(prop-1-en-2-yl)spiro[4.5]dec-6-ene, MAGNESIUM ION, ... (4 entities in total) |
| Functional Keywords | terpene synthase, teas, teas-m4, premnaspirodiene, lyase |
| Biological source | Nicotiana tabacum (Common tobacco) |
| Cellular location | Cytoplasm: Q40577 |
| Total number of polymer chains | 1 |
| Total formula weight | 63462.72 |
| Authors | Koo, H.J.,O'Maille, P.E.,Louie, G.V.,Bowman, M.,Noel, J.P. (deposition date: 2016-03-03, release date: 2016-10-05, Last modification date: 2023-09-27) |
| Primary citation | Koo, H.J.,Vickery, C.R.,Xu, Y.,Louie, G.V.,O'Maille, P.E.,Bowman, M.,Nartey, C.M.,Burkart, M.D.,Noel, J.P. Biosynthetic potential of sesquiterpene synthases: product profiles of Egyptian Henbane premnaspirodiene synthase and related mutants. J.Antibiot., 69:524-533, 2016 Cited by PubMed Abstract: The plant terpene synthase (TPS) family is responsible for the biosynthesis of a variety of terpenoid natural products possessing diverse biological functions. TPSs catalyze the ionization and, most commonly, rearrangement and cyclization of prenyl diphosphate substrates, forming linear and cyclic hydrocarbons. Moreover, a single TPS often produces several minor products in addition to a dominant product. We characterized the catalytic profiles of Hyoscyamus muticus premnaspirodiene synthase (HPS) and compared it with the profile of a closely related TPS, Nicotiana tabacum 5-epi-aristolochene synthase (TEAS). The profiles of two previously studied HPS and TEAS mutants, each containing nine interconverting mutations, dubbed HPS-M9 and TEAS-M9, were also characterized. All four TPSs were compared under varying temperature and pH conditions. In addition, we solved the X-ray crystal structures of TEAS and a TEAS quadruple mutant complexed with substrate and products to gain insight into the enzymatic features modulating product formation. These informative structures, along with product profiles, provide new insight into plant TPS catalytic promiscuity. PubMed: 27328867DOI: 10.1038/ja.2016.68 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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