Transketolase: 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'>
_TOC_
== 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>.  '''Split-gene TKT''' is found in the hyperthermophilic bacterium ''Carboxydothermus hydrogenoformans'' and is reconstituted from 2 separate polypeptide chains<ref>PMID:33193259</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>.
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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>.
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>.
[[Transketolase 3D structures]]
</StructureSection>
</StructureSection>