Literature summary for 5.1.3.B12 extracted from

Patel, S.N.; Sharma, M.; Lata, K.; Singh, U.; Kumar, V.; Sangwan, R.S.; Singh, S.P.
Improved operational stability of D-psicose 3-epimerase by a novel protein engineering strategy, and D-psicose production from fruit and vegetable residues (2016), Biores. Technol., 216, 121-127 .

Search for more literature for 5.1.3.B12

Cloned(Commentary)

Cloned (Comment)	Organism
gene dpe, DNA and amino acid sequence determination and analysis, recombinant expression of the engineered chimeric Smt3-D-psicose 3-epimerase conjugate in Escherichia coli strain BL21	Agrobacterium tumefaciens

Protein Variants

Protein Variants	Comment	Organism
additional information	improved operational stability of D-psicose 3-epimerase by a protein engineering strategy by introduction of a SUMO fusion system, using Saccharomyces cerevisiae Smt3, as the N-terminal tag, which can significantly enhance operational stability and bioconversion efficiency of D-psicose 3-epimerase. The Smt3-D-psicose 3-epimerase conjugate system exhibits relatively better catalytic efficiency, and improved productivity in terms of space-time yields of about 8.5 kg/l/day, it can serve as a catalytic tool for the pilot scale production of the functional sugar, D-psicose, D-psicose production from fruit and vegetable remains and agro-industrial by-products, overview. The bioprocessing leads to achievement of D-psicose production to the extent of 25-35% conversion w/w of D-fructose contained in the sample	Agrobacterium tumefaciens

Inhibitors

Inhibitors	Comment	Organism	Structure
Ca2+	strong inhibition at 1 mM	Agrobacterium tumefaciens
Cu2+	almost complete inhibition at 1 mM	Agrobacterium tumefaciens
Ni2+	almost complete inhibition at 1 mM	Agrobacterium tumefaciens
Zn2+	almost complete inhibition at 1 mM	Agrobacterium tumefaciens

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Co2+	activates strongly at 1 mM	Agrobacterium tumefaciens
Mn2+	activates strongly at 1 mM, even low levels of Mn2+ (0.025-0.1 mM) in the assay reaction are sufficient for enhancing the enzyme's activity	Agrobacterium tumefaciens
additional information	Mg2+, Fe2+ and Ba2+ at 1 mM have no significant effct on the activity	Agrobacterium tumefaciens

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
132000	-	recombinant wild-type enzyme, gel filtration	Agrobacterium tumefaciens
180000	-	recombinant chimeric Smt3-D-psicose 3-epimerase conjugate, gel filtration	Agrobacterium tumefaciens

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
D-psicose	Agrobacterium tumefaciens	-	D-fructose	-	r
D-psicose	Agrobacterium tumefaciens EHA 105 / NCIM 2942	-	D-fructose	-	r

Organism

Organism	UniProt	Comment	Textmining
Agrobacterium tumefaciens	A9CH28	strain C58 / ATCC 33970	-
Agrobacterium tumefaciens EHA 105 / NCIM 2942	A9CH28	strain C58 / ATCC 33970	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant engineered Smt3-D-psicose 3-epimerase conjugate from Escherichia coli strain BL21 by nickel affinity and anion exchange chromatography	Agrobacterium tumefaciens

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
D-psicose	-	Agrobacterium tumefaciens	D-fructose	-	r
D-psicose	-	Agrobacterium tumefaciens EHA 105 / NCIM 2942	D-fructose	-	r

Subunits

Subunits	Comment	Organism
tetramer	4 * 45000, recombinant chimeric Smt3-D-psicose 3-epimerase conjugate, SDS-PAGE, 4 * 33000, recombinant wild-type enzyme, SDS-PAGE	Agrobacterium tumefaciens

Synonyms

Synonyms	Comment	Organism
D-psicose-3-epimerase	-	Agrobacterium tumefaciens

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
50	-	recombinant wild-type enzyme	Agrobacterium tumefaciens
65	-	recombinant chimeric enzyme	Agrobacterium tumefaciens

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
50	-	purified recombinant chimeric enzyme, retains 45% of the initial activity after 12 h	Agrobacterium tumefaciens

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
8	-	recombinant and native enzyme	Agrobacterium tumefaciens

pH Stability

pH Stability	pH Stability Maximum	Comment	Organism
5	10	purified recombinant chimeric enzyme, retains about 80% of the initial activity after 5 h, completely stable at pH 8.0	Agrobacterium tumefaciens

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Release 2023.1 (January 2023)