Transketolase
From Proteopedia
(Difference between revisions)
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| - | {{STRUCTURE_1tka| PDB=1tka | SIZE=400| SCENE= |right|CAPTION=Transketolase dimer complex with deazo-thiamine diphosphate and Ca+2 ion (green) [[1tka]] }} | ||
| - | '''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. | + | <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 == | ||
| + | '''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>. | ||
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| + | == Structural highlights == | ||
| + | |||
| + | The active site of TKT contains a ligand-cofactor adduct. <ref>PMID:17914867</ref> | ||
| + | </StructureSection> | ||
== 3D Structures of transketolase == | == 3D Structures of transketolase == | ||
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**[[2r5n]] – EcTKT + TPP + ribose 5-P<br /> | **[[2r5n]] – EcTKT + TPP + ribose 5-P<br /> | ||
**[[3upt]] - BtTKT + TPP + ribose 5-P<br /> | **[[3upt]] - BtTKT + TPP + ribose 5-P<br /> | ||
| - | **[[2r8o]] - EcTKT + TPP + xylulose 5-P | + | **[[2r8o]] - EcTKT 1 + TPP + xylulose 5-P |
**[[2r8p]] - EcTKT + TPP + fructose 6-P<br /> | **[[2r8p]] - EcTKT + TPP + fructose 6-P<br /> | ||
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**[[4kxx]] - hTKT + TPP + seduheptulose 7-P<br /> | **[[4kxx]] - hTKT + TPP + seduheptulose 7-P<br /> | ||
}} | }} | ||
| - | + | == References == | |
| + | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Revision as of 09:03, 21 September 2016
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3D Structures of transketolase
Updated on 21-September-2016
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
- ↑ 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
