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| The <scene name='46/466534/Cv/5'>active site of TKT contains a ligand-cofactor adduct</scene>.<ref>PMID:17914867</ref> <scene name='46/466534/Cv/6'>Ca coordination site</scene>. | | 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>. |
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Revision as of 13:51, 26 September 2019
| 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] Water molecules are shown as red spheres. Ca coordination site.
- ↑ 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 26-September-2019
{"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
- 5i4i, 5xry - PsTKT – Pichia stipitis
- 5hgx, 5i5g - PsTKT (mutant)
- 5nd6 - CrTKT – Chlamydomonas reinhardtii
- 5vrb - TKT – Neisseria gonorrhoeae
- 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
- 5hht - EcTKT (mutant) + TDP
- 1r9j - TKT + TPP – Leishmania mexicana
- 4c7x - LsTKT + TPP
- 5hyv, 5x56, 5xuf, 5xvt - PsTKT + TPP
- 5xsa, 5xsb, 5xsm, 5xt0, 5xt4, 5xtv, 5xtx - PsTKT + TPP intermediate
- 5xtl - PsTKT + pyrimidine derivative
- 5nd5 - CrTKT + 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,5xqa - BtTKT + TPP + ribose 5-P
- 2r8o, 5xqk - 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
- 5hje - PsTKT + TPP + seduheptulose 7-P
- 5i51, 5xrv, 5xu2 - PsTKT + TPP + fructose 6-P
- 5xps, 5xu9 - PsTKT + TPP + erythrose 4-P
- 5i5e - PsTKT (mutant) + TPP + xylulose 5-P
References
