
transketolase
Sign in to saveAlso known as glycoaldehyde transferase, glycolaldehydetransferase
Transketolase (abbreviated as TK) is an enzyme that, in humans, is encoded by the TKT gene. It participates in both the pentose phosphate pathway in all organisms and the Calvin cycle of photosynthesis. Transketolase catalyzes two important reactions, which operate in opposite directions in these two pathways. In the first reaction of the non-oxidative pentose phosphate pathway, the cofactor thiamine diphosphate accepts a 2-carbon fragment from a 5-carbon ketose (D-xylulose-5-P), then transfers this fragment to a 5-carbon aldose (D-ribose-5-P) to form a 7-carbon ketose (sedoheptulose-7-P). The
In the Vinony graph
Within Vinony's link graph, transketolase is referenced by 95 other articles, and connects out to Q180686, thiamine(1+) diphosphate and liver.
Vinony files it under EC 2.2.1, Genes on human chromosome 3 and Inborn errors of carbohydrate metabolism.
Its subject is documented across 15 Wikipedia language editions.
Key facts
- Enzyme.Name
- transketolase
- Enzyme.EC_number
- 2.2.1.1
- Enzyme.CAS_number
- 9014-48-6
- Enzyme.GO_code
- 0004802
- Protein.Name
- transketolase
- Protein.image
- E4P in Transketolase Active Site.jpg
- Protein.HGNCid
- 11834
- Protein.Symbol
- TKT
- Protein.EntrezGene
- 7086
- Protein.OMIM
- 606781
- Protein.RefSeq
- NM_001064
- Protein.UniProt
- P29401
- Protein.ECnumber
- 2.2.1.1
- Protein.Chromosome
- 3
- Protein.Arm
- p
- Protein.Band
- 14.3
via Wikipedia infobox
Research
2,510 papers- Engineering transketolase for stereoselective α-hydroxyketone synthesis.Methods in enzymology · 2025
- Transketolase: observations in alcohol-related brain damage research.The international journal of biochemistry & cell biology · 2009
- Transketolase enzyme discovery and engineering.Methods in enzymology · 2025
- Structure and functioning mechanism of transketolase.Biochimica et biophysica acta · 2014
- Reassessing Transketolase Assays: Methodological Considerations for Detecting Functional Thiamine Deficiency.Annals of the New York Academy of Sciences · 2026
via PubMed
Wikidata facts
Show 2 more facts
- EC enzyme number
- 2.2.1.1
- Commons category
- Transketolase
Sources (2)
via Wikidata · CC0
~9 min read
Encyclopedic overview
6 sectionsContents
- Species distribution
- Structure
- Mechanism
- Role in disease
- Diagnostic use
- References
Transketolase (abbreviated as TK) is an enzyme that, in humans, is encoded by the TKT gene. It participates in both the pentose phosphate pathway in all organisms and the Calvin cycle of photosynthesis. Transketolase catalyzes two important reactions, which operate in opposite directions in these two pathways. In the first reaction of the non-oxidative pentose phosphate pathway, the cofactor thiamine diphosphate accepts a 2-carbon fragment from a 5-carbon ketose (D-xylulose-5-P), then transfers this fragment to a 5-carbon aldose (D-ribose-5-P) to form a 7-carbon ketose (sedoheptulose-7-P). The abstraction of two carbons from D-xylulose-5-P yields the 3-carbon aldose glyceraldehyde-3-P. In the Calvin cycle, transketolase catalyzes the reverse reaction, the conversion of sedoheptulose-7-P and glyceraldehyde-3-P to pentoses, the aldose D-ribose-5-P and the ketose D-xylulose-5-P.
The second reaction catalyzed by transketolase in the pentose phosphate pathway involves the same thiamine diphosphate-mediated transfer of a 2-carbon fragment from D-xylulose-5-P to the aldose erythrose-4-phosphate, affording fructose 6-phosphate and glyceraldehyde-3-P. Again, the same reaction occurs in the Calvin cycle but in the opposite direction. Moreover, in the Calvin cycle, this is the first reaction catalyzed by transketolase rather than the second.
Excerpted from Wikipedia’s “transketolase” article, available under the CC BY-SA 4.0 licence.