Transaldolase
From Proteopedia
(Difference between revisions)
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**[[3clm]] – TAL – ''Neisseria gonorrhoeae''<br /> | **[[3clm]] – TAL – ''Neisseria gonorrhoeae''<br /> | ||
**[[3cwn]], [[1onr]], [[1ucw]] - EcTAL B – ''Escherichia coli''<br /> | **[[3cwn]], [[1onr]], [[1ucw]] - EcTAL B – ''Escherichia coli''<br /> | ||
| - | **[[3kof]], [[1i2n]], [[1i2o]], [[1i2p]], [[1i2q]], [[1i2r]] - EcTAL B (mutant)<br /> | + | **[[3kof]], [[1i2n]], [[1i2o]], [[1i2p]], [[1i2q]], [[1i2r]], [[4rz5]], [[4rz6]] - EcTAL B (mutant)<br /> |
**[[3hjz]] – TAL B – ''Prochlorococcus marinus''<br /> | **[[3hjz]] – TAL B – ''Prochlorococcus marinus''<br /> | ||
**[[3igx]], [[4e0c]] – FtTAL B – ''Francisella tularensis''<br /> | **[[3igx]], [[4e0c]] – FtTAL B – ''Francisella tularensis''<br /> | ||
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**[[3tno]] - FtTAL B + seduheptulose 7-phosphate<br /> | **[[3tno]] - FtTAL B + seduheptulose 7-phosphate<br /> | ||
**[[3upb]] - FtTAL B + arabinose 5-phosphate<br /> | **[[3upb]] - FtTAL B + arabinose 5-phosphate<br /> | ||
| + | **[[4s2b]] - EcTAL B + tagatose 6-phosphate<br /> | ||
| + | **[[4s2c]], [[4s1f]] - EcTAL B + fructose 6-phosphate<br /> | ||
| + | **[[4rxf]], [[4rxg]], [[4rz4]] - EcTAL B (mutant) + fructose 6-phosphate<br /> | ||
| + | **[[4xz9]] - TAL + glycerol 3-phosphate – ''Thermoplasma acidophilum''<br /> | ||
| + | |||
}} | }} | ||
== References == | == References == | ||
<references/> | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Revision as of 07:10, 19 September 2016
Contents |
Function
Transaldolase (TAL) is part of the pentose phosphate pathway. It catalyzes the transformation of sedoheptulose 7-phosphate and glyceraldehyde 3-phosphate to erythrose 4-phosphate and fructose 6-phosphate[1].
Disease
TAL deficiency influences mitochondrial homeostasis, Ca+2 fluxing and apoptosis[2].
Structural highlights
TAL overall structure is of a TIM barrel. The active site contains a Schiff-base-bound phosphosugar at Lys135[3].
3D Structures of transaldolase
Updated on 19-September-2016
References
- ↑ Caillau M, Paul Quick W. New insights into plant transaldolase. Plant J. 2005 Jul;43(1):1-16. PMID:15960612 doi:http://dx.doi.org/TPJ2427
- ↑ Qian Y, Banerjee S, Grossman CE, Amidon W, Nagy G, Barcza M, Niland B, Karp DR, Middleton FA, Banki K, Perl A. Transaldolase deficiency influences the pentose phosphate pathway, mitochondrial homoeostasis and apoptosis signal processing. Biochem J. 2008 Oct 1;415(1):123-34. doi: 10.1042/BJ20080722. PMID:18498245 doi:http://dx.doi.org/10.1042/BJ20080722
- ↑ Light SH, Minasov G, Duban ME, Anderson WF. Adherence to Burgi-Dunitz stereochemical principles requires significant structural rearrangements in Schiff-base formation: insights from transaldolase complexes. Acta Crystallogr D Biol Crystallogr. 2014 Feb;70(Pt 2):544-52. doi:, 10.1107/S1399004713030666. Epub 2014 Jan 31. PMID:24531488 doi:http://dx.doi.org/10.1107/S1399004713030666
