Triose phosphate translocator: Difference between revisions
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The '''triose phosphate translocator''' is an integral membrane protein found in the inner membrane of [[chloroplasts]]. It exports triose phosphate ([[Dihydroxyacetone phosphate]]) in exchange for inorganic phosphate and is therefore classified as an [[antiporter]]. The imported phosphate is then used for ATP regeneration via the light-dependent-reaction; the ATP may then for example be used for further reactions in the Calvin-cycle. The translocator protein is responsible for exporting all the [[carbohydrate]] produced in [[photosynthesis]] by plants and therefore most of the carbon in food that one eats has been transported by the triose phosphate translocator.<ref>{{Cite journal| last1 = Walters | first1 = R.| last2 = Ibrahim | first2 = D.| last3 = Horton | first3 = P.| last4 = Kruger | first4 = N.| title = A mutant of Arabidopsis lacking the triose-phosphate/phosphate translocator reveals metabolic regulation of starch breakdown in the light| journal = Plant Physiology| volume = 135| issue = 2| pages = 891–906| year = 2004| pmid = 15173568| pmc = 514124| doi = 10.1104/pp.104.040469}}</ref> Its three-dimensional structure was reported in 2017, revealing how it recognizes two different substrates to catalyze the strict 1:1 exchange.<ref>{{Cite journal|last1=Lee|first1=Y.|last2=Nishizawa|first2=T.|last3=Takemoto|first3=M.|last4=Kumazaki|first4=K.|last5=Yamashita|first5=K.|last6=Hirata|first6=K.|last7=Minoda|first7=A.|last8=Nagatoishi|first8=S.|last9=Tsumoto|first9=K.|last10=Ishitani|first10=R.|last11=Nureki|first11=O.|year=2017|title=Structure of the triose-phosphate/phosphate translocator reveals the basis of substrate specificity|url=https://www.nature.com/articles/s41477-017-0022-8|journal=Nature Plants|language=en|volume=3|issue=10|pages=825–832|doi=10.1038/s41477-017-0022-8|pmid=28970497 |s2cid=46804514 |issn=2055-0278}}</ref> |
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The triose phosphate translocator is an integral membrane protein found in the outer membrane of [[chloroplasts]]. It exports triose phosphate ([[Dihydroxyacetone phosphate]]) in exchange for inorganic phosphate and is therefore classified as an [[antiporter]]. The imported phosphate is then used for ATP regenereation via the light-dependend-reaction; the ATP may then for example be used for further reactions in the Clavin-cycle.The Translocator protein is responsible for exporting all the [[carbohydrate]] produced in [[photosynthesis]] by plants and therefore most of the carbon in food that one eats has been transported by the triose phosphate translocator.<ref>{{cite doi|10.1104/pp.104.040469}}</ref> |
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==References== |
==References== |
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[[Category:Metabolism]] |
[[Category:Metabolism]] |
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[[Category:Agronomy]] |
[[Category:Agronomy]] |
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{{Photosynthesis-stub}} |
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Latest revision as of 21:51, 19 August 2023
The triose phosphate translocator is an integral membrane protein found in the inner membrane of chloroplasts. It exports triose phosphate (Dihydroxyacetone phosphate) in exchange for inorganic phosphate and is therefore classified as an antiporter. The imported phosphate is then used for ATP regeneration via the light-dependent-reaction; the ATP may then for example be used for further reactions in the Calvin-cycle. The translocator protein is responsible for exporting all the carbohydrate produced in photosynthesis by plants and therefore most of the carbon in food that one eats has been transported by the triose phosphate translocator.[1] Its three-dimensional structure was reported in 2017, revealing how it recognizes two different substrates to catalyze the strict 1:1 exchange.[2]
References
[edit]- ^ Walters, R.; Ibrahim, D.; Horton, P.; Kruger, N. (2004). "A mutant of Arabidopsis lacking the triose-phosphate/phosphate translocator reveals metabolic regulation of starch breakdown in the light". Plant Physiology. 135 (2): 891–906. doi:10.1104/pp.104.040469. PMC 514124. PMID 15173568.
- ^ Lee, Y.; Nishizawa, T.; Takemoto, M.; Kumazaki, K.; Yamashita, K.; Hirata, K.; Minoda, A.; Nagatoishi, S.; Tsumoto, K.; Ishitani, R.; Nureki, O. (2017). "Structure of the triose-phosphate/phosphate translocator reveals the basis of substrate specificity". Nature Plants. 3 (10): 825–832. doi:10.1038/s41477-017-0022-8. ISSN 2055-0278. PMID 28970497. S2CID 46804514.
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