How To Use Proenzyme In A Sentence
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Examples of important proenzymes include pepsinogen, trypsinogen and chymotrypsinogen, which give rise to the proteolytic digestive enzymes.
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TPP1 is synthesized as an inactive proenzyme (pro-TPP1) that is proteolytically processed into the active enzyme after exposure to low pH in vitro or targeting to the lysosome in vivo.
Journal of Biological Chemistry current issue
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The fibrinolytic system involves a series of enzymatic reactions that results in the conversion of the proenzyme, plasminogen, into the trypsin-like lyric enzyme, plasmin.
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All caspases, which are initially inactive proenzymes, share the same processing scheme to achieve mature forms after cleavage at specific Asp sites.
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The proenzyme structure reveals suboptimal catalytic triad geometry with its propiece linker partially blocking the substrate-binding site, which together serve to prevent premature activation of the protease.
Journal of Biological Chemistry current issue
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Caspases exist as inactive proenzymes which undergo proteolytic processing by upstream caspases (caspase-8, -9) at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme in the form of
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That in the same system one can with RIA measure both an enzyme and its proenzyme and other inactive forms has both advantages and disadvantages, depending on the problem under investigation.
Nobel Lecture Radioimmunoassay: A Probe For Fine Structure Of Biologic Systems
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Covalent modification of pre-existing pools of inactive proenzymes produces active enzymes.
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Trypsin also activates trypsinogen as well as all the other proenzymes in the pancreatic secretion, producing the active proteases and peptidases that hydrolyze dietary polypeptides.
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All of the serine proteases and the zinc peptidases of pancreatic secretions are produced in the form of their respective proenzymes.
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Protein digestion begins in the stomach, where a proenzyme called pepsinogen is secreted, autocatalytically converted to Pepsin A, and used for the first step of proteolysis.
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These death proteases are part of a proteolytic cascade activating proenzymes into active proteases.
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In the case of the serine proteases, they are synthesized as proenzymes, larger molecules that require modification before they become active.
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The next to last step in this chain is the activation of the circulating proenzyme prothrombin into its active form, thrombin.
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Degradation of fibrin clots is the function of plasmin, a serine protease that circulates as the inactive proenzyme, plasminogen.
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Examples of important proenzymes include pepsinogen, trypsinogen and chymotrypsinogen, which give rise to the proteolytic digestive enzymes.
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Caspases exist as inactive proenzymes that undergo proteolytic processing at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme.
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