6YAK
Split gene transketolase, active alpha2beta2 heterotetramer
This is a non-PDB format compatible entry.
Summary for 6YAK
| Entry DOI | 10.2210/pdb6yak/pdb |
| Descriptor | N-terminal component of the split chain transketolase, C-terminal component of the split chain transketolase, 2-[3-[(4-azanyl-2-methyl-pyrimidin-5-yl)methyl]-4-methyl-2H-1,3-thiazol-5-yl]ethyl phosphono hydrogen phosphate, ... (8 entities in total) |
| Functional Keywords | hyperthermophilic, split-gene transketolase, thermal stability, industrial applications, transferase |
| Biological source | Carboxydothermus hydrogenoformans More |
| Total number of polymer chains | 4 |
| Total formula weight | 143162.15 |
| Authors | Isupov, M.N.,Littlechild, J.A.,James, P. (deposition date: 2020-03-12, release date: 2020-11-25, Last modification date: 2024-01-24) |
| Primary citation | James, P.,Isupov, M.N.,De Rose, S.A.,Sayer, C.,Cole, I.S.,Littlechild, J.A. A 'Split-Gene' Transketolase From the Hyper-Thermophilic Bacterium Carboxydothermus hydrogenoformans : Structure and Biochemical Characterization. Front Microbiol, 11:592353-592353, 2020 Cited by PubMed Abstract: A novel transketolase has been reconstituted from two separate polypeptide chains encoded by a 'split-gene' identified in the genome of the hyperthermophilic bacterium, . The reconstituted active αβ tetrameric enzyme has been biochemically characterized and its activity has been determined using a range of aldehydes including glycolaldehyde, phenylacetaldehyde and cyclohexanecarboxaldehyde as the ketol acceptor and hydroxypyruvate as the donor. This reaction proceeds to near 100% completion due to the release of the product carbon dioxide and can be used for the synthesis of a range of sugars of interest to the pharmaceutical industry. This novel reconstituted transketolase is thermally stable with no loss of activity after incubation for 1 h at 70°C and is stable after 1 h incubation with 50% of the organic solvents methanol, ethanol, isopropanol, DMSO, acetonitrile and acetone. The X-ray structure of the holo reconstituted αβ tetrameric transketolase has been determined to 1.4 Å resolution. In addition, the structure of an inactive tetrameric β protein has been determined to 1.9 Å resolution. The structure of the active reconstituted αβ enzyme has been compared to the structures of related enzymes; the E1 component of the pyruvate dehydrogenase complex and D-xylulose-5-phosphate synthase, in an attempt to rationalize differences in structure and substrate specificity between these enzymes. This is the first example of a reconstituted 'split-gene' transketolase to be biochemically and structurally characterized allowing its potential for industrial biocatalysis to be evaluated. PubMed: 33193259DOI: 10.3389/fmicb.2020.592353 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.34 Å) |
Structure validation
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