Literature summary for 1.15.1.1 extracted from

Tuteja, N.; Mishra, P.; Yadav, S.; Tajrishi, M.; Baral, S.; Sabat, S.C.
Heterologous expression and biochemical characterization of a highly active and stable chloroplastic CuZn-superoxide dismutase from Pisum sativum (2015), BMC Biotechnol., 15, 3-3 .

Search for more literature for 1.15.1.1

Cloned(Commentary)

Cloned (Comment)	Organism
recombinant expression of His-tagged soluble chloroplastic isoform CuZn-SOD in its enzymatically active and stable form in Escherichia coli, and optimization of culture conditions, best at 18°C and upon isopropyl beta-D-1-thiogalactopyranoside induction, recombinant enzyme production process optimization	Pisum sativum

Protein Variants

Protein Variants	Comment	Organism
additional information	the recombinant pea chloroplastic SOD possesses nearly 6fold higher superoxide dismutase activity and 5fold higher peroxidase activity as compared to commercially available CuZn-superoxide dismutase from Bos taurus. The recombinant protein harbors all the characteristics features of this class of enzyme. The recombinant enzyme is exceptionally stable concerning pH and temperature and maintains its activity upon prolonged storage	Pisum sativum

General Stability

General Stability	Organism
the purified recombinant enzyme is stable to proteolytic digestion	Pisum sativum

Inhibitors

Inhibitors	Comment	Organism	Structure
diethyldithiocarbamate	complete inhibition at 1.4 mM, a specific inhibitor for CuZn-SODs	Pisum sativum
H2O2	addition of 5 mM of hydrogen peroxide (H2O2) completely inhibits of the enzyme	Pisum sativum
KCN	complete inhibition at 0.16 mM, a specific inhibitor for CuZn-SODs	Pisum sativum
NaN3	low inhibition by sodium azide, 40% inhibition at 50 mM	Pisum sativum

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
chloroplast	-	Pisum sativum	9507	-

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Cu2+	a CuZn-superoxide dismutase, the prosthetic copper and zinc are essential component of CuZn-SODs, 1.80-1.84 Cu2+ per enzyme dimer	Pisum sativum
additional information	measurement of Cu and Zn content of PschSOD by ICP-MS, zincon, and bathocuproeine protocols	Pisum sativum
Zn2+	a CuZn-superoxide dismutase, the prosthetic copper and zinc are essential component of CuZn-SODs, 1.6 Zn2+ per enzyme dimer	Pisum sativum

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
36000	38000	recombinant His-tagged enzyme, gel filtration	Pisum sativum

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
2 superoxide + 2 H+	Pisum sativum	-	O2 + H2O2	-	?

Organism

Organism	UniProt	Comment	Textmining
Pisum sativum	P11964	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant His-tagged soluble chloroplastic isoform CuZn-SOD from Escherichia coli by nickel affinity chromatography	Pisum sativum

Storage Stability

Storage Stability	Organism
25°C, the purified recombinant enzyme retains 50% of its original activity after storing for 180 days at room temperature	Pisum sativum

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
2 superoxide + 2 H+	-	Pisum sativum	O2 + H2O2	-	?
additional information	enzyme PschSOD exhibits superoxide dismutase and peroxidase activities. The enzyme utilizes its own dismutation product, the H2O2 in presence of bicarbonate	Pisum sativum	?	-	?

Subunits

Subunits	Comment	Organism
homodimer	2 * 18000, recombinant His-tagged enzyme, SDS-PAGE	Pisum sativum
More	circular dichroism spectral analysis of the enzyme's secondary structure. The enzyme conserves the beta-barrel structure of the CuZn-SODs in its recombinant form	Pisum sativum

Synonyms

Synonyms	Comment	Organism
CuZn-SOD	-	Pisum sativum
CuZn-superoxide dismutase	-	Pisum sativum
PschSOD	-	Pisum sativum

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
37	-	assay at	Pisum sativum

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
45	-	purified recombinant His-tagged enzyme, completely stable at, 60 min	Pisum sativum
62	-	t1/2, purified recombinant His-tagged enzyme, 20-60 min	Pisum sativum
75	-	purified recombinant His-tagged enzyme, 20 min, inactivation	Pisum sativum

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
6	8	recombinant His-tagged enzyme	Pisum sativum

pH Range

pH Minimum	pH Maximum	Comment	Organism
additional information	-	the decrease of the enzyme activity at acidic pH might be due to the dissociation of dimer into monomer, as the acidic pH favors the monomer formation, whereas the alkaline pH favors the dimer formation. Charge interaction between the subunits are postulated to be a major determinant of CuZn-SOD activity at varying pHs	Pisum sativum
5	10	about 70% of maximal activity within this range, 10% at pH 4.0, 40% at pH 11.0	Pisum sativum

pH Stability

pH Stability	pH Stability Maximum	Comment	Organism
additional information	-	the purified recombinant His-tagged enzyme's activity shows a broad range of pH sustainability	Pisum sativum

General Information

General Information	Comment	Organism
additional information	circular dichroism spectral analysis of the enzyme's secondary structure	Pisum sativum

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Release 2023.1 (January 2023)