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| <StructureSection load='2r8o' 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=''> | | <StructureSection load='2r8o' 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=''> |
| == Function == | | == Function == |
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| **[[1tka]], [[1tkb]], [[1tkc]] – yTKT + TPP analog | | **[[1tka]], [[1tkb]], [[1tkc]] – yTKT + TPP analog |
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| **[[1gpu]] - yTKT + TPP derivative | | **[[1gpu]] - yTKT 1 + TPP derivative |
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| **[[1itz]] - TKT + TPP – maize | | **[[1itz]] - TKT + TPP – maize |
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| **[[1ngs]] - yTKT + TPP + Ca + erythrose-4-P | | **[[1ngs]] - yTKT + TPP + Ca + erythrose-4-P |
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| **[[2r5n]] – EcTKT + TPP + ribose 5-P<br /> | | **[[2r5n]] – EcTKT 1 + TPP + ribose 5-P<br /> |
| **[[3upt]] - BtTKT + TPP + ribose 5-P<br /> | | **[[3upt]] - BtTKT + TPP + ribose 5-P<br /> |
| **[[2r8o]] - EcTKT 1 + TPP + xylulose 5-P | | **[[2r8o]] - EcTKT 1 + TPP + xylulose 5-P |
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| **[[2r8p]] - EcTKT + TPP + fructose 6-P<br /> | | **[[2r8p]] - EcTKT 1 + TPP + fructose 6-P<br /> |
| **[[4kxu]] - hTKT + TPP + sorbitol 6-P<br /> | | **[[4kxu]] - hTKT + TPP + sorbitol 6-P<br /> |
| **[[4kxv]], [[4kxw]] - hTKT + TPP + xylitol 5-P<br /> | | **[[4kxv]], [[4kxw]] - hTKT + TPP + xylitol 5-P<br /> |
| 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[1].
Structural highlights
The active site of TKT contains a ligand-cofactor adduct. [2]
- ↑ 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
- ↑ 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
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3D Structures of transketolase
Updated on 21-September-2016
{"openlevels":0}
- Transketolase
- 1trk – yTKT – yeast
- 1ay0 – yTKT (mutant)
- 2e6k – TKT – Thermus thermophilus
- 3hyl – BaTKT – Bacillus anthracis
- 3kom – TKT (mutant) – Francisella tularensis
- 3l84 – CjTKT – Campylobacter jejuni
- 3rim – TKT – Mycobacterium tuberculosis
- 3uk1 – BtTKT – Burkholderia thailandensis
- 4c7v - LsTKT – Lactobacillus salivarius
- 4xeu - TKT – Pseudomonas aeruginosa
- Transketolase binary complexes
- 3m49 – BaTKT + TPP
- 3mos, 3ooy – hTKT + TPP - human
- 4kxy - hTKT + TPP analog
- 1tka, 1tkb, 1tkc – yTKT + TPP analog
- 1gpu - yTKT 1 + TPP derivative
- 1itz - TKT + TPP – maize
- 1qgd - EcTKT + TPP – Escherichia coli
- 1r9j - TKT + TPP – Leishmania mexicana
- 4c7x - LsTKT + TPP
- Transketolase ternary complexes
- 3m7i, 3m6l – CjTKT + TPP + ribose 5-P
- 3m34 - CjTKT + TPP + Ca
- 1ngs - yTKT + TPP + Ca + erythrose-4-P
- 2r5n – EcTKT 1 + TPP + ribose 5-P
- 3upt - BtTKT + TPP + ribose 5-P
- 2r8o - EcTKT 1 + TPP + xylulose 5-P
- 2r8p - EcTKT 1 + TPP + fructose 6-P
- 4kxu - hTKT + TPP + sorbitol 6-P
- 4kxv, 4kxw - hTKT + TPP + xylitol 5-P
- 4kxx - hTKT + TPP + seduheptulose 7-P
References
