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Transketolase
From Proteopedia
(Difference between revisions)
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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'> | <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 == | == 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>. | + | '''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 == | == Structural highlights == | ||
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**[[1qgd]] - EcTKT + TPP <br /> | **[[1qgd]] - EcTKT + TPP <br /> | ||
| + | **[[6tj8]] - EcTKT 1 + TPP analog <br /> | ||
**[[5hht]] - EcTKT (mutant) + TDP <br /> | **[[5hht]] - EcTKT (mutant) + TDP <br /> | ||
**[[1r9j]] - TKT + TPP – ''Leishmania mexicana''<br /> | **[[1r9j]] - TKT + TPP – ''Leishmania mexicana''<br /> | ||
**[[4c7x]] - LsTKT + TPP <br /> | **[[4c7x]] - LsTKT + TPP <br /> | ||
| - | **[[5hyv]], [[5x56]], [[5xuf]], [[5xvt]] - PsTKT + TPP <br /> | + | **[[5hyv]], [[5x56]], [[5xuf]], [[5xvt]], [[5xs6]] - PsTKT + TPP <br /> |
**[[5xsa]], [[5xsb]], [[5xsm]], [[5xt0]], [[5xt4]], [[5xtv]], [[5xtx]] - PsTKT + TPP intermediate<br /> | **[[5xsa]], [[5xsb]], [[5xsm]], [[5xt0]], [[5xt4]], [[5xtv]], [[5xtx]] - PsTKT + TPP intermediate<br /> | ||
| + | **[[5xqk]] - PsTKT + xylulose-5-P<br /> | ||
| + | **[[5xqa]] - PsTKT + ribose-5-P<br /> | ||
| + | **[[5xps]] - PsTKT + erythrose-4-P<br /> | ||
| + | **[[5xrv]] - PsTKT + fructose-6-P<br /> | ||
| + | **[[5i51]] - PsTKT (mutant) + fructose-6-P<br /> | ||
**[[5xtl]] - PsTKT + pyrimidine derivative <br /> | **[[5xtl]] - PsTKT + pyrimidine derivative <br /> | ||
**[[5nd5]] - CrTKT + TPP <br /> | **[[5nd5]] - CrTKT + TPP <br /> | ||
**[[3m49]] – BaTKT + TPP<br /> | **[[3m49]] – BaTKT + TPP<br /> | ||
| - | + | ||
*Transketolase ternary complexes | *Transketolase ternary complexes | ||
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**[[2r5n]] – EcTKT 1 + TPP + ribose 5-P<br /> | **[[2r5n]] – EcTKT 1 + TPP + ribose 5-P<br /> | ||
**[[3upt]],[[5xqa]] - BtTKT + TPP + ribose 5-P<br /> | **[[3upt]],[[5xqa]] - BtTKT + TPP + ribose 5-P<br /> | ||
| - | **[[2r8o]], [[5xqk]] - EcTKT 1 + TPP + xylulose 5-P | + | **[[2r8o]], [[5xqk]] - EcTKT 1 + TPP + xylulose 5-P<br /> |
| - | + | **[[6tj9]] - EcTKT 1 + TPP analog + xylulose 5-P<br /> | |
**[[2r8p]] - EcTKT 1 + TPP + fructose 6-P<br /> | **[[2r8p]] - EcTKT 1 + TPP + fructose 6-P<br /> | ||
**[[5hje]] - PsTKT + TPP + seduheptulose 7-P<br /> | **[[5hje]] - PsTKT + TPP + seduheptulose 7-P<br /> | ||
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**[[5xps]], [[5xu9]] - PsTKT + TPP + erythrose 4-P<br /> | **[[5xps]], [[5xu9]] - PsTKT + TPP + erythrose 4-P<br /> | ||
**[[5i5e]] - PsTKT (mutant) + TPP + xylulose 5-P<br /> | **[[5i5e]] - PsTKT (mutant) + TPP + xylulose 5-P<br /> | ||
| + | |||
| + | *Split-gene transketolase | ||
| + | |||
| + | **[[6yak]] - ChTKT N-terminal + C-terminal chain – ''Carboxydothermus hydrogenoformans''<br /> | ||
| + | **[[6yaj]] - ChTKT C-terminal chain<br /> | ||
}} | }} | ||
== References == | == References == | ||
<references/> | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Revision as of 09:44, 14 December 2020
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3D Structures of transketolase
Updated on 14-December-2020
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
