Transketolase
From Proteopedia
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| - | + | <StructureSection load='' size='350' side='right' caption='E. coli transketolase 1 dimer complex with xylulose-5-phosphate-thiamine diphosphate adduct, ethylene glycol and Ca+2 ion (green) (PDB code [[2r8o]]).' scene='46/466534/Cv/1'> | |
| + | == Function == | ||
| + | '''Transketolase''' (TKT) catalyzes two opposite reactions. The synthesis of sedoheptulose-7-P in the pentose phosphate pathway using thiamine diphosphate (TPP) as co-factor; and the conversion of sedoheptulose-7-P and glyceraldehyde-3-P to aldose and ketose in the [[Calvin cycle]]<ref>PMID:8369276</ref>. '''Split-gene TKT''' is found in the hyperthermophilic bacterium ''Carboxydothermus hydrogenoformans'' and is reconstituted from 2 separate polypeptide chains<ref>PMID:33193259</ref>. | ||
| - | + | == Structural highlights == | |
| - | + | The <scene name='46/466534/Cv/7'>active site of TKT contains a ligand-cofactor adduct</scene>.<ref>PMID:17914867</ref> Water molecules are shown as red spheres. <scene name='46/466534/Cv/8'>Ca coordination site</scene>. | |
== 3D Structures of transketolase == | == 3D Structures of transketolase == | ||
| - | + | [[Transketolase 3D structures]] | |
| + | </StructureSection> | ||
| - | [[1trk]] – yTKT – yeast | ||
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| - | [[1ay0]] – yTKT (mutant) | ||
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| - | [[2e6k]] – TKT – ''Thermus thermophilus'' | ||
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| - | [[3hyl]] – BaTKT – ''Bacillus anthracis'' | ||
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| - | [[3kom]] – TKT (mutant) – ''Francisella tularensis'' | ||
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| - | [[3l84]] – CjTKT – ''Campylobacter jejuni''<br /> | ||
| - | [[3rim]] – TKT – ''Mycobacterium tuberculosis''<br /> | ||
| - | [[3uk1]] – BtTKT – ''Burkholderia thailandensis'' | ||
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| - | ===Transketolase binary complexes=== | ||
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| - | [[3m49]] – BaTKT + TPP | ||
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| - | [[3mos]], [[3ooy]] – TKT + TPP - human | ||
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| - | [[1tka]], [[1tkb]], [[1tkc]] – yTKT + TPP analog | ||
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| - | [[1gpu]] - yTKT + TPP derivative | ||
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| - | [[1itz]] - TKT + TPP – maize | ||
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| - | [[1qgd]] - EcTKT + TPP – ''Escherichia coli'' | ||
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| - | [[1r9j]] - TKT + TPP – ''Leishmania mexicana'' | ||
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| - | ===Transketolase ternary complexes=== | ||
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| - | [[3m7i]], [[3m6l]] – CjTKT + TPP + ribose 5-P | ||
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| - | [[3m34]] - CjTKT + TPP + Ca | ||
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| - | [[1ngs]] - yTKT + TPP + Ca + erythrose-4-P | ||
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| - | [[2r5n]] – EcTKT + TPP + ribose 5-P<br /> | ||
| - | [[3upt]] - BtTKT + TPP + ribose 5-P<br /> | ||
| - | [[2r8o]] - EcTKT + TPP + xylulose 5-P | ||
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| - | [[2r8p]] - EcTKT + TPP + fructose 6-P | ||
| + | == References == | ||
| + | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Current revision
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References
- ↑ Verschueren KH, Kingma J, Rozeboom HJ, Kalk KH, Janssen DB, Dijkstra BW. Crystallographic and fluorescence studies of the interaction of haloalkane dehalogenase with halide ions. Studies with halide compounds reveal a halide binding site in the active site. Biochemistry. 1993 Sep 7;32(35):9031-7. PMID:8369276
- ↑ James P, Isupov MN, De Rose SA, Sayer C, Cole IS, Littlechild JA. A 'Split-Gene' Transketolase From the Hyper-Thermophilic Bacterium Carboxydothermus hydrogenoformans: Structure and Biochemical Characterization. Front Microbiol. 2020 Oct 30;11:592353. doi: 10.3389/fmicb.2020.592353., eCollection 2020. PMID:33193259 doi:http://dx.doi.org/10.3389/fmicb.2020.592353
- ↑ Asztalos P, Parthier C, Golbik R, Kleinschmidt M, Hubner G, Weiss MS, Friedemann R, Wille G, Tittmann K. Strain and near attack conformers in enzymic thiamin catalysis: X-ray crystallographic snapshots of bacterial transketolase in covalent complex with donor ketoses xylulose 5-phosphate and fructose 6-phosphate, and in noncovalent complex with acceptor aldose ribose 5-phosphate. Biochemistry. 2007 Oct 30;46(43):12037-52. Epub 2007 Oct 3. PMID:17914867 doi:10.1021/bi700844m
