Difference between revisions of "Part:BBa K2448021"
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This enzyme is highly specific for D-psicose, but it is also able to catalyse with very low activity the epimerization of D-tagatose [1]. For optimal activity, it requires cofactors such as Mn2+ or Co2+, although it has a low basal activity without ions. The native Dpe shows a tetrameric arrangement of 132 kDa, and each subunit has 293 amino acids with a molecular weight of 33 kDa. The topology of each subunit is a TIM-barrel fold with a cluster of eight β-strands surrounded by twelve α-helices [2]. | This enzyme is highly specific for D-psicose, but it is also able to catalyse with very low activity the epimerization of D-tagatose [1]. For optimal activity, it requires cofactors such as Mn2+ or Co2+, although it has a low basal activity without ions. The native Dpe shows a tetrameric arrangement of 132 kDa, and each subunit has 293 amino acids with a molecular weight of 33 kDa. The topology of each subunit is a TIM-barrel fold with a cluster of eight β-strands surrounded by twelve α-helices [2]. | ||
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| + | ===References=== | ||
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| + | [1] Mu W, Chu F, Xing Q, Yu S, Zhou L, Jiang B. Cloning, expression, and characterization of a D-psicose 3-epimerase from ''Clostridium cellulolyticum'' H10. J Agric Food Chem. (2011) 59, 7785-7792. | ||
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| + | [2] Chan HC, Zhu Y, Hu Y, Ko TP, Huang CH, Ren F, Chen CC, Ma Y, Guo RT, Sun Y. Crystal structures of D-psicose 3-epimerase from ''Clostridium cellulolyticum'' H10 and its complex with ketohexose sugars. Protein Cell. (2012) 3, 123-131. | ||
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Latest revision as of 13:14, 27 December 2018
D-Psicose 3-epimerase (Dpe) from Clostridium cellulolyticum
This part is an E. coli codon optimized version of the D-Psicose 3-epimerase (Dpe) from Clostridium cellulolyticum str. ATCC 35319 (Uniprot B8I944).
Usage and Biology
D-Psicose 3-epimerase (EC: 5.1.3.30) catalyses the reversible epimerization of D-fructose into D-psicose, D-psicose being the carbon-3 (C3) epimer of D-fructose.
The C. cellulolyticum Dpe is a 33.034 kDa protein of 293 amino acids.
This enzyme is highly specific for D-psicose, but it is also able to catalyse with very low activity the epimerization of D-tagatose [1]. For optimal activity, it requires cofactors such as Mn2+ or Co2+, although it has a low basal activity without ions. The native Dpe shows a tetrameric arrangement of 132 kDa, and each subunit has 293 amino acids with a molecular weight of 33 kDa. The topology of each subunit is a TIM-barrel fold with a cluster of eight β-strands surrounded by twelve α-helices [2].
References
[1] Mu W, Chu F, Xing Q, Yu S, Zhou L, Jiang B. Cloning, expression, and characterization of a D-psicose 3-epimerase from Clostridium cellulolyticum H10. J Agric Food Chem. (2011) 59, 7785-7792.
[2] Chan HC, Zhu Y, Hu Y, Ko TP, Huang CH, Ren F, Chen CC, Ma Y, Guo RT, Sun Y. Crystal structures of D-psicose 3-epimerase from Clostridium cellulolyticum H10 and its complex with ketohexose sugars. Protein Cell. (2012) 3, 123-131.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25INCOMPATIBLE WITH RFC[25]Illegal AgeI site found at 628
- 1000COMPATIBLE WITH RFC[1000]