Difference between revisions of "Part:BBa K2448022"

Latest revision as of 18:39, 1 November 2017

D-Psicose 3-epimerase (Dpe) from Agrobacterium tumefaciens

This is the original sequence of the D-Psicose 3-epimerase (Dpe) from Agrobacterium tumefaciens str. C58 (Atu4750, UniProt A9CH28).

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 A. tumefaciens Dpe is a 31.56 kDa protein of 289 amino acids.

This enzyme is highly specific for D-Psicose, but it is also able to catalyse with very low activity the epimerization of other D-ketoses (in the decreased substrate specificity) : D-fructose, D-tagatose, D-ribulose, D-xylulose and D-sorbose [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 289 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].

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 NgoMIV site found at 190
Illegal NgoMIV site found at 250
Illegal NgoMIV site found at 601
Illegal AgeI site found at 628
1000
INCOMPATIBLE WITH RFC[1000]
Illegal SapI.rc site found at 156

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 <partinfo>BBa_K2448022 short</partinfo>
-Dpe At
+This is the original sequence of the D-Psicose 3-epimerase (Dpe) from ''Agrobacterium tumefaciens'' str. C58 (Atu4750, UniProt A9CH28).
-<!-- Add more about the biology of this part here
 ===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.
+[[File: T--Evry_Paris-Saclay--EC 5.1.3.30.png|300px]]
+The ''A. tumefaciens'' Dpe is a 31.56 kDa protein of 289 amino acids.
+This enzyme is highly specific for D-Psicose, but it is also able to catalyse with very low activity the epimerization of other D-ketoses (in the decreased substrate specificity) : D-fructose, D-tagatose, D-ribulose, D-xylulose and D-sorbose [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 289 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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