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| {{STRUCTURE_2ps5| PDB=2ps5 | SCENE= }} | | {{STRUCTURE_2ps5| PDB=2ps5 | SCENE= }} |
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| '''N225D Trichodiene Synthase: Complex With Mg and Pyrophosphate'''
| | ===N225D Trichodiene Synthase: Complex With Mg and Pyrophosphate=== |
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| ==Overview==
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| Trichodiene synthase from Fusarium sporotrichioides contains two metal ion-binding motifs required for the cyclization of farnesyl diphosphate: the "aspartate-rich" motif D(100)DXX(D/E) that coordinates to Mg2+A and Mg2+C, and the "NSE/DTE" motif N(225)DXXSXXXE that chelates Mg2+B (boldface indicates metal ion ligands). Here, we report steady-state kinetic parameters, product array analyses, and X-ray crystal structures of trichodiene synthase mutants in which the fungal NSE motif is progressively converted into a plant-like DDXXTXXXE motif, resulting in a degradation in both steady-state kinetic parameters and product specificity. Each catalytically active mutant generates a different distribution of sesquiterpene products, and three newly detected sesquiterpenes are identified. In addition, the kinetic and structural properties of the Y295F mutant of trichodiene synthase were found to be similar to those of the wild-type enzyme, thereby ruling out a proposed role for Y295 in catalysis.
| | The line below this paragraph, {{ABSTRACT_PUBMED_17996718}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 17996718 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_17996718}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Site-directed mutagenesis]] | | [[Category: Site-directed mutagenesis]] |
| [[Category: Terpenoid synthase fold]] | | [[Category: Terpenoid synthase fold]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 13:42:47 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 20:08:50 2008'' |