We are analyzing https://link.springer.com/article/10.1007/bf02906155.

Title:
The complete amino acid sequence of copper, zinc superoxide dismutase from Saccharomyces cerevisiae | Carlsberg Research Communications
Description:
The amino acid sequence of the copper zinc superoxide dismutase from Saccharomyces cerevisiae has been determined by automated Edman degradation. Peptides were obtained from cyanogen bromide cleavage, Staphylococcus aureus V8 protease digestion, tryptic and chymotryptic digests of the citraconylated reduced and carboxymethylated enzyme, and by further fragmentation of selected peptides with trypsin. From the alignment of these peptides and the previously published sequence of the first 54 amino terminal residues (24) the complete sequence was deduced by direct sequence identification of all 153 amino acid residues and of all peptide overlaps. The amino acid sequence corresponds to a molecular weight of 15,950 for each of the two identical subunits in the native enzyme. The primary structure of yeast copper, zinc superoxide dismutase is 55% identical with the sequence of the copper, zinc enzyme from bovine erythrocytes. Importantly, all the copper and zinc ligands, six histidine residues and one aspartate residue from the bovine enzyme, are conserved in the yeast enzyme. The high overall sequence homology and conservation of important metal binding active site amino acid residues suggest that the three-dimensional structure and in particular the active site geometry is virtually the same for the bovine and yeast enzyme. In contrast no sequence homology is apparent by comparison with the manganese or iron class of superoxide dismutases indicating that the two classes have not evolved from a common ancestor.
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Keywords {🔍}

google, scholar, article, sequence, cas, superoxide, amino, pubmed, dismutase, acid, copper, enzyme, protein, biochem, carlsberg, zinc, saccharomyces, cerevisiae, structure, dismutases, research, bovine, privacy, cookies, johansen, hasemann, peptides, content, publish, search, complete, download, martin, edman, residues, yeast, determination, proteins, chromatography, enzymol, bannister, res, proc, nat, sci, usa, hill, biochemistry, york, fridovich,

Topics {✒️}

automated protein sequencing performic acid-oxidized ribonuclease micropolyamide thin-layer chromatography protein sequence determination human γ-g-immunoglobulin active site geometry amino acid sequence protein sequence privacy choices/manage cookies related subjects performic acid oxidation amino terminal sequence polyamide layer chromatography automated edman degradation automated edman degradations previously published sequence direct sequence identification assigning metal ligands zinc superoxide dismutase saccharomyces cerevisiae published saccharomyces cerevisiae cells zn superoxide dismutase mangano superoxide dismutase main content log dansyl amino acids protein sequenator european economic area cyanogen bromide cleavage high catalytic efficiency simultaneous multisample identification cyanogen bromide fragments phenylthiohydantoin amino acids conditions privacy policy phenylmethane sulfonyl fluoride histidine c2 protons carsten overballe-petersen mitochondrial superoxide dismutases superoxide dismutases indicating proteolytic enzyme specific accepting optional cookies search search sequence determination complete sequence article number 201 journal finder publish sequence homologies metal ligands article cite histidine residues saccharomyces cerevisiae

Schema {🗺️}

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         description:The amino acid sequence of the copper zinc superoxide dismutase from Saccharomyces cerevisiae has been determined by automated Edman degradation. Peptides were obtained from cyanogen bromide cleavage, Staphylococcus aureus V8 protease digestion, tryptic and chymotryptic digests of the citraconylated reduced and carboxymethylated enzyme, and by further fragmentation of selected peptides with trypsin. From the alignment of these peptides and the previously published sequence of the first 54 amino terminal residues (24) the complete sequence was deduced by direct sequence identification of all 153 amino acid residues and of all peptide overlaps. The amino acid sequence corresponds to a molecular weight of 15,950 for each of the two identical subunits in the native enzyme. The primary structure of yeast copper, zinc superoxide dismutase is 55% identical with the sequence of the copper, zinc enzyme from bovine erythrocytes. Importantly, all the copper and zinc ligands, six histidine residues and one aspartate residue from the bovine enzyme, are conserved in the yeast enzyme. The high overall sequence homology and conservation of important metal binding active site amino acid residues suggest that the three-dimensional structure and in particular the active site geometry is virtually the same for the bovine and yeast enzyme. In contrast no sequence homology is apparent by comparison with the manganese or iron class of superoxide dismutases indicating that the two classes have not evolved from a common ancestor.
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      headline:The complete amino acid sequence of copper, zinc superoxide dismutase from Saccharomyces cerevisiae
      description:The amino acid sequence of the copper zinc superoxide dismutase from Saccharomyces cerevisiae has been determined by automated Edman degradation. Peptides were obtained from cyanogen bromide cleavage, Staphylococcus aureus V8 protease digestion, tryptic and chymotryptic digests of the citraconylated reduced and carboxymethylated enzyme, and by further fragmentation of selected peptides with trypsin. From the alignment of these peptides and the previously published sequence of the first 54 amino terminal residues (24) the complete sequence was deduced by direct sequence identification of all 153 amino acid residues and of all peptide overlaps. The amino acid sequence corresponds to a molecular weight of 15,950 for each of the two identical subunits in the native enzyme. The primary structure of yeast copper, zinc superoxide dismutase is 55% identical with the sequence of the copper, zinc enzyme from bovine erythrocytes. Importantly, all the copper and zinc ligands, six histidine residues and one aspartate residue from the bovine enzyme, are conserved in the yeast enzyme. The high overall sequence homology and conservation of important metal binding active site amino acid residues suggest that the three-dimensional structure and in particular the active site geometry is virtually the same for the bovine and yeast enzyme. In contrast no sequence homology is apparent by comparison with the manganese or iron class of superoxide dismutases indicating that the two classes have not evolved from a common ancestor.
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