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Literature summary for 5.1.3.30 extracted from

  • Zhang, W.; Li, H.; Zhang, T.; Jiang, B.; Zhou, L.; Mu, W.
    Characterization of a D-psicose 3-epimerase from Dorea sp. CAG317 with an acidic pH optimum and a high specific activity (2015), J. Mol. Catal. B, 120, 68-74 .
No PubMed abstract available
Search for more literature for 5.1.3.30

Application

Application Comment Organism
synthesis the recombinant Dorea sp. DPEase displays significantly higher specific activity at acidic pHs and remarkably higher productivity of D-psicose at pH 6.0, indicating that it is appropriate for use as a different source of D-psicose producing enzyme Dorea sp. CAG:317

Cloned(Commentary)

Cloned (Comment) Organism
gene dpe, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) Dorea sp. CAG:317

Inhibitors

Inhibitors Comment Organism Structure
Ba2+
-
 Dorea sp. CAG:317
Ca2+
-
 Dorea sp. CAG:317
Cu2+
-
 Dorea sp. CAG:317

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ best metal cofactor, has no effect on pH stability and slightly imporves temperature Dorea sp. CAG:317
Fe2+ 26.59% of the activity with Co2+ at 1 mM Dorea sp. CAG:317
Mn2+ 81.24% of the activity with Co2+ at 1 mM Dorea sp. CAG:317
additional information metal-dependent enzyme, no activity without presence of divalent metal ion Dorea sp. CAG:317
Ni2+ 7.96% of the activity with Co2+ at 1 mM Dorea sp. CAG:317
Zn2+ 1.75% of the activity with Co2+ at 1 mM Dorea sp. CAG:317

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
D-psicose Dorea sp. CAG:317
-
 D-fructose
-
 r

Organism

Organism UniProt Comment Textmining
Dorea sp. CAG:317
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and dialysis Dorea sp. CAG:317

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
806
-
 purified recombinant enzyme, pH 6.0, 70°C, 1 mM Co2+ Dorea sp. CAG:317

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-fructose
-
 Dorea sp. CAG:317 D-psicose
-
 r
D-psicose
-
 Dorea sp. CAG:317 D-fructose
-
 r
additional information the equilibrium ratio between D-fructose and D-psicose is approximately 30:70 for the recombinant enzyme, elevated temperature does not significantly shift the equilibrium toward D-psicose. The conversion ratio of D-fructose to D-psicose is calculated to be 30.1%, 31.5%, 31.8%, 31.4%, 31.1%, 31.0%, 30.4%, 29.2%, and 28.6% when the reaction temperature is 40°C, 45°C, 50°C, 55°C, 60°C, 65°C, 70°C, 75°C, and 80°C, respectively Dorea sp. CAG:317 ?
-
 ?

Subunits

Subunits Comment Organism
homotetramer 4 * 33000, SDS-PAGE Dorea sp. CAG:317

Synonyms

Synonyms Comment Organism
DPEase
-
 Dorea sp. CAG:317

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
70
-
-
 Dorea sp. CAG:317

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
 Co2+ slightly improves the thermostability of the enzyme Dorea sp. CAG:317
40 70 the purified recombinant enzyme retains 70% and 30% of its initial activity after 4 h of incubation at 40°C and 50°C, respectively, 55% activity remaining after 0.5 h at 60°C, complete inactivation after 0.5 h at 70°C Dorea sp. CAG:317

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
-
 Dorea sp. CAG:317

pH Stability

pH Stability pH Stability Maximum Comment Organism
5.5 8.5 the purified recombinant enzyme retains more than 80% of initial activity when incubated for 2 h at pH values from pH 5.5 to pH 8.5 Dorea sp. CAG:317

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
3.32
-
 D-fructose recombinant enzyme, pH 6.0, 70°C Dorea sp. CAG:317
6.9
-
 D-psicose recombinant enzyme, pH 6.0, 70°C Dorea sp. CAG:317