Literature summary for 1.15.1.1 extracted from

Umasuthan, N.; Bathige, S.D.; Thulasitha, W.S.; Qiang, W.; Lim, B.S.; Lee, J.
Characterization of rock bream (Oplegnathus fasciatus) cytosolic Cu/Zn superoxide dismutase in terms of molecular structure, genomic arrangement, stress-induced mRNA expression and antioxidant function (2014), Comp. Biochem. Physiol. B, 176, 18-33 .

Cloned(Commentary)

Cloned (Comment)	Organism
cDNA library construction, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, genetic structure, the primary transcript is represented by five exons and encodes a peptide of 154 amino acids, quantitative PCR expression analysis. Screening of Of-cCu/ZnSOD 5'-flanking region reveal the presence of several important transcription factor binding sites that potentially govern the Cu/ZnSOD expression. Recombinant overexpression of MBP-tagged enzyme in Escherichia coli strain BL21(DE3)	Oplegnathus fasciatus

Cloned (Comment)

Organism

cDNA library construction, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, genetic structure, the primary transcript is represented by five exons and encodes a peptide of 154 amino acids, quantitative PCR expression analysis. Screening of Of-cCu/ZnSOD 5'-flanking region reveal the presence of several important transcription factor binding sites that potentially govern the Cu/ZnSOD expression. Recombinant overexpression of MBP-tagged enzyme in Escherichia coli strain BL21(DE3)

Oplegnathus fasciatus

Inhibitors

Inhibitors	Comment	Organism
Dithiocarbamate	strongly inhibits the activity of the rOf-cCu/ZnSOD	Oplegnathus fasciatus
H2O2	-	Oplegnathus fasciatus
KCN	strongly inhibits the activity of the rOf-cCu/ZnSOD	Oplegnathus fasciatus
additional information	no inhibition by EDTA and poor inhibition by NaN3	Oplegnathus fasciatus

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
cytosol	enzyme Of-cCu/ZnSOD possesses no signal peptide at the N-terminus suggesting that it is an intracellular protein belonging to the cytoplasmic Cu/ZnSOD family	Oplegnathus fasciatus	5829	-

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Cu2+	a Cu/ZnSOD, the enzyme sequence harbors two Cu/ZnSOD signatures and seven metal liganding residues	Oplegnathus fasciatus
Zn2+	a Cu/ZnSOD, the enzyme sequence harbors two Cu/ZnSOD signatures and seven metal liganding residues	Oplegnathus fasciatus

Natural Substrates/ Products (Substrates)

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

Organism

Organism	UniProt	Comment	Textmining
Oplegnathus fasciatus	Q6IYF2	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
glycoprotein	a potential N-glycosylation site (87NVTA90) is identified indicating that Of-cCu/ZnSOD is a glycoprotein	Oplegnathus fasciatus

Purification (Commentary)

Purification (Comment)	Organism
recombinant MBP-tagged enzyme from Escherichia coli strain BL21(DE3) by amylose affinity chromatography	Oplegnathus fasciatus

Source Tissue

Source Tissue	Comment	Organism	Textmining
blood	-	Oplegnathus fasciatus	-
brain	-	Oplegnathus fasciatus	-
gill	low expression level	Oplegnathus fasciatus	-
head kidney	low expression level	Oplegnathus fasciatus	-
heart	-	Oplegnathus fasciatus	-
intestine	low expression level	Oplegnathus fasciatus	-
kidney	low expression level	Oplegnathus fasciatus	-
liver	-	Oplegnathus fasciatus	-
additional information	a constitutive mRNA expression of Of-cCu/ZnSOD with higher levels in blood, liver, heart, and brain is observed, no expresion in muscle	Oplegnathus fasciatus	-
skin	low expression level	Oplegnathus fasciatus	-
spleen	low expression level	Oplegnathus fasciatus	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
2 superoxide + 2 H+	-	Oplegnathus fasciatus	O2 + H2O2	-	?

Subunits

Subunits	Comment	Organism
More	the enzyme sequence comprises eight beta-sheets forming a beta-barrel topology, alignment and modeling studies confirmed the conservation of Cu/ZnSOD at primary and tertiary levels. Structure homology modeling and three-dimensional structure, overview	Oplegnathus fasciatus

Synonyms

Synonyms	Comment	Organism
Cu/ZnSOD	-	Oplegnathus fasciatus
cytosolic Cu/Zn superoxide dismutase	-	Oplegnathus fasciatus
Of-cCu/ZnSOD	-	Oplegnathus fasciatus

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
25	-	-	Oplegnathus fasciatus

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
25	-	purified recombinant enzyme, 120 min, completely stable	Oplegnathus fasciatus
60	-	purified recombinant enzyme, loss of 50% activity after 20 min, of about 85% activity after 100 min, and inactivation after 120 min	Oplegnathus fasciatus

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
10	-	-	Oplegnathus fasciatus

pH Range

pH Minimum	pH Maximum	Comment	Organism
6	10	activity range, rapid loss of activity above pH 10.0, inactive at pH 5.0 and pH 11.0, profile overview	Oplegnathus fasciatus

Expression

Organism	Comment	Expression
Oplegnathus fasciatus	screening of Of-cCu/ZnSOD 5'-flanking region reveal the presence of several important transcription factor binding sites that potentially govern the Cu/ZnSOD expression	additional information
Oplegnathus fasciatus	the transcriptional profile and temporal assessment of Of-cCu/ZnSOD transcripts in animals under pathological (bacteriaor viral-induced) and physiological (H2O2-induced oxidative) stress conditions using quantitative PCR expression analysis, in which the enzyme expression exhibits significantly upregulated levels. Lipopolysaccharide induces the enzyme expression, and H2O2 causes a transient increase in Of-cCu/ZnSOD transcription	up

General Information

General Information	Comment	Organism
evolution	while invertebrate Cu/ZnSOD members mainly demonstrate a tetraexonic structure, the vertebrate members have acquired an additional intron in the third exon resulting in a quinquepartite arrangement with class-specific exon lengths. Although, teleost Cu/ZnSOD members resemble the mammalian orthologues in their genomic organization, they share a proximal position with molluscan members in the phylogeny	Oplegnathus fasciatus
additional information	structure homology modeling	Oplegnathus fasciatus
physiological function	the enzyme shws antioxidant action	Oplegnathus fasciatus