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20657 Ensembl ENSG00000109610 ENSMUSG00000072941 UniProt P08294 O09164 RefSeq (mRNA) NM_003102 NM_011435 RefSeq (protein) NP_003093 NP_035565 Location (UCSC) Chr 4: 24.79 – 24.8 Mb Chr 5: 52.52 – 52.53 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Extracellular superoxide dismutase [Cu-Zn] is an enzyme that in humans is encoded by the SOD3 gene. This gene encodes a member of ...
SOD1 binds copper and zinc ions and is one of three superoxide dismutases responsible for destroying free superoxide radicals in the body. The encoded isozyme is a soluble cytoplasmic and mitochondrial intermembrane space protein, acting as a homodimer to convert naturally occurring, but harmful, superoxide radicals to molecular oxygen and hydrogen peroxide.
Function: Amylase is an enzyme that is responsible for the breaking of the bonds in starches, polysaccharides, and complex carbohydrates to be turned into simple sugars that will be easier to absorb. Clinical Significance: Amylase also has medical history in the use of Pancreatic Enzyme Replacement Therapy (PERT). One of the components is ...
The cytosols of virtually all eukaryotic cells contain a SOD enzyme with copper and zinc (Cu-Zn-SOD). For example, Cu-Zn-SOD available commercially is normally purified from bovine red blood cells. The bovine Cu-Zn enzyme is a homodimer of molecular weight 32,500. It was the first SOD whose atomic-detail crystal structure was solved, in 1975. [10]
Myoglobin sketch Alpha helix. 1958 – Myoglobin was the very first crystal structure of a protein molecule. [2] Myoglobin cradles an iron-containing heme group that reversibly binds oxygen for use in powering muscle fibers, and those first crystals were of myoglobin from the sperm whale, whose muscles need copious oxygen storage for deep dives.
The catalytic mechanism of enzymes within a superfamily is commonly conserved, although substrate specificity may be significantly different. [15] Catalytic residues also tend to occur in the same order in the protein sequence. [ 16 ]