Difference between revisions of "Part:BBa K2448021"

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

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]

@@ Line 14: / Line 14: @@
 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].
+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.
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