Literature summary 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 .

Cloned(Commentary)

EC Number	Cloned (Comment)	Organism
5.1.3.B12	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

EC Number	Protein Variants	Comment	Organism
5.1.3.B12	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

EC Number	Inhibitors	Comment	Organism	Structure
5.1.3.B12	Ca2+	strong inhibition at 1 mM	Agrobacterium tumefaciens
5.1.3.B12	Cu2+	almost complete inhibition at 1 mM	Agrobacterium tumefaciens
5.1.3.B12	Ni2+	almost complete inhibition at 1 mM	Agrobacterium tumefaciens
5.1.3.B12	Zn2+	almost complete inhibition at 1 mM	Agrobacterium tumefaciens

Metals/Ions

EC Number	Metals/Ions	Comment	Organism	Structure
5.1.3.B12	Co2+	activates strongly at 1 mM	Agrobacterium tumefaciens
5.1.3.B12	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
5.1.3.B12	additional information	Mg2+, Fe2+ and Ba2+ at 1 mM have no significant effct on the activity	Agrobacterium tumefaciens

Molecular Weight [Da]

EC Number	Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
5.1.3.B12	132000	-	recombinant wild-type enzyme, gel filtration	Agrobacterium tumefaciens
5.1.3.B12	180000	-	recombinant chimeric Smt3-D-psicose 3-epimerase conjugate, gel filtration	Agrobacterium tumefaciens

Natural Substrates/ Products (Substrates)

EC Number	Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
5.1.3.B12	D-psicose	Agrobacterium tumefaciens	-	D-fructose	-	r
5.1.3.B12	D-psicose	Agrobacterium tumefaciens EHA 105 / NCIM 2942	-	D-fructose	-	r

Organism

EC Number	Organism	UniProt	Comment	Textmining
5.1.3.B12	Agrobacterium tumefaciens	A9CH28	strain C58 / ATCC 33970	-
5.1.3.B12	Agrobacterium tumefaciens EHA 105 / NCIM 2942	A9CH28	strain C58 / ATCC 33970	-

Purification (Commentary)

EC Number	Purification (Comment)	Organism
5.1.3.B12	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)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
5.1.3.B12	D-psicose	-	Agrobacterium tumefaciens	D-fructose	-	r
5.1.3.B12	D-psicose	-	Agrobacterium tumefaciens EHA 105 / NCIM 2942	D-fructose	-	r

Subunits

EC Number	Subunits	Comment	Organism
5.1.3.B12	tetramer	4 * 45000, recombinant chimeric Smt3-D-psicose 3-epimerase conjugate, SDS-PAGE, 4 * 33000, recombinant wild-type enzyme, SDS-PAGE	Agrobacterium tumefaciens

Synonyms

EC Number	Synonyms	Comment	Organism
5.1.3.B12	D-psicose-3-epimerase	-	Agrobacterium tumefaciens

Temperature Optimum [°C]

EC Number	Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
5.1.3.B12	50	-	recombinant wild-type enzyme	Agrobacterium tumefaciens
5.1.3.B12	65	-	recombinant chimeric enzyme	Agrobacterium tumefaciens

Temperature Stability [°C]

EC Number	Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
5.1.3.B12	50	-	purified recombinant chimeric enzyme, retains 45% of the initial activity after 12 h	Agrobacterium tumefaciens

pH Optimum

EC Number	pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
5.1.3.B12	8	-	recombinant and native enzyme	Agrobacterium tumefaciens

pH Stability

EC Number	pH Stability	pH Stability Maximum	Comment	Organism
5.1.3.B12	5	10	purified recombinant chimeric enzyme, retains about 80% of the initial activity after 5 h, completely stable at pH 8.0	Agrobacterium tumefaciens

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)