Difference between revisions of "Part:BBa K2448021"
 
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<partinfo>BBa_K2448021 short</partinfo>
 
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D-Psicose 3-epimerase (Dpe) from Clostridium cellulolyticum str. ATCC 35319
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This part is an ''E. coli'' codon optimized version of the D-Psicose 3-epimerase (Dpe) from ''Clostridium cellulolyticum'' str. ATCC 35319
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(Uniprot B8I944)
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(Uniprot B8I944).
  
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===Usage and Biology===
 
===Usage and Biology===
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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.
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[[File: T--Evry_Paris-Saclay--EC 5.1.3.30.png|300px]]
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The ''C. cellulolyticum'' Dpe is a 33.034 kDa protein of 293 amino acids.
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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].
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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.

T--Evry Paris-Saclay--EC 5.1.3.30.png

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


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    INCOMPATIBLE WITH RFC[25]
    Illegal AgeI site found at 628
  • 1000
    COMPATIBLE WITH RFC[1000]