The current status of superoxide dismutase (SOD) is that it is an enzyme with diverse ramifications. This review attempts an understanding of SOD as a structural, functional, and biological entity. Accordingly, the review is in three parts. The first part discusses SOD in terms of protein structure, proceeding from primary to secondary and three-dimensional structure for the three forms of SOD: copper/zinc SOD, manganese SOD, and iron SOD. This is the order of structural knowledge of the enzyme. Iron SOD is an enzyme of prokaryotes and some higher plants. Manganese SOD is an enzyme of prokaryotes and eukaryotes. Copper/zinc SOD is an enzyme of eukaryotes and certain prokaryotes. The evolutionary relationships of the three forms of SOD, the status of the copper/zinc SOD gene in prokaryotes, and the cloning and sequencing of SOD genes are discussed. The second part of the review deals with the catalytic mechanism of SOD in the three forms of the enzyme. Structural and mechanistic conclusions from various spectroscopic studies are critically considered. A detailed picture is given of the active site of copper/zinc SOD. The third part is a review of SOD in the general context of oxygen toxicity. After consideration of the question of superoxide toxicity and superoxide pathology, several areas in which SOD has been investigated or used as a tool in a biochemical, pharmacological, or clinical context are discussed, including population genetics; trisomy 21; development and senescence; the nutritional copper, zinc, and manganese status; hemolysis and anemia; oxygen toxicity in the lung and nervous system; inflammation, autoimmune disease and chromosome breakage, ischemia and degenerative changes; radiation damage; and malignancy. A comprehensive picture is given of measurements of SOD activity in disease states, and the question of superoxide-related disease is considered at several points.

Aspects of the structure, function, and applications of superoxide dismutase

Microbial alkaline proteases: From a bioindustrial viewpoint

The invention is related to a non-toxic, non-toxigenic, non-pathogenic recombinant Fusarium, e.g., Fusarium graminearum host cell comprising a nucleic acid sequence encoding a heterologous protein operably linked to a promoter. The invention further relates to a method for the production of recombinant proteins using such Fusarium host cells. The invention also relates to a promoter and terminator sequence which may be used in such cells.

Non-toxic, non-toxigenic, non-pathogenic Fusarium expression system and promoters and terminators for use therein

https://www.cambridge.org/core/services/aop-cambridge-core/content/view/S0022029900024742

Proteinases of psychrotrophic bacteria: their production, properties, effects and control.

One stop mycology

A strain of Serratia, isolated from an intestinal canal of a silkworm, produced a large quantity of protease. The enzyme was extracellular and was named Serratiopeptidase, tentatively. Protease pro...

Serratia Protease:Part I. Purification and General Properties of the Enzyme

A novel superoxide dismutase is produced by cultivating a microorganism belonging to the genus Serratia. The superoxide dismutase is useful as an antiinflammatory agent. An immobilized superoxide dismutase has properties of decreased antigenicity and increased antiinflammatory activity.

Superoxide dismutase, its immobilized form, and their production and use

We have cloned a genomic DNA encoding the alkaline protease (Alp) of Fusarium sp. S-19-5 from a genomic DNA library and sequenced the nucleotides. Complementary DNA encoding Alp was also isolated from the cDNA library after amplifying the gene by PCR using partial sequences of the Alp genomic DNA as primers. The Alp gene has an open reading frame of 1137 nucleotides containing three introns. A TATA box (TAAATA) was observed 112 base pairs upstream from the translation initiation codon in the 5′-non coding region. The Alp protein has a pre region consisting of 14 amino acids and a pro region of 85 amino acids preceding the mature region, which consists of 280 amino acids. The amino acid sequence of Fusarium Alp has 52% homology with that of Aspergillus oryzae and 51% homology with that of Acremonium chrysogenum. The entire cDNA encoding Fusarium Alp was introduced into Saccharomyees cerevisiae, which then secreted enzymatically active Alp into the culture medium.

Cloning and Nucleotide Sequence of the Alkaline Protease Gene from Fusarium sp. S-19-5 and Expression in Saccharomyces cerevisiae

Superoxide dismutase was easily isolated from Serratia marcescensATCC 21074 by ammonium sulfate fractionation and Dyemātrex Gel Green A chromatography. The purified enzyme was a manganese-containing protein with a molecular weight of 4.8×104. Combination of gel electrophoresis in dodecylsulfate and gel filtration showed that it was composed of two equal molecular subunits. The dimeric protein contained 1.5 g atoms of manganese and exhibited molecular extinction coefficients of 9.4×104 M−1 cm−1 at 280 nm and 8.9×102 M−1 cm−1 at 470 nm. The enzyme showed similarities with manganese superoxide dismutases from other prokaryotes.

A Manganese Superoxide Dismutase from Serratia marcescens

Production of Alkaline Protease from n-Paraffins by a Kabicidin Resistant Mutant Strain of Fusarium sp.

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