Proenzyme

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Related to proenzymes: Enzyme precursors

proenzyme

[prō′en‚zīm]
(biochemistry)

Proenzyme

 

(also proferment, zymogen, preenzyme), an inactive precursor of enzymes. Proenzymes form during the biosynthesis of enzymes. They are converted into active enzymes following limited proteolysis. The fission of usually one of the peptide bonds of the proenzyme molecule, which results in a partial structural change in the molecule, leads to the formation of the enzyme’s active center. Many proteolytics that are present in animals and bacteria, as well as phospholipase, are synthesized as proenzymes. Typical proenzymes include pepsinogen, trypsinogen, and prothrombin. Proenzymes are biologically important because they inhibit premature enzymatic activity in those cells and tissues where there is enzyme biosynthesis.

References in periodicals archive ?
Within the phenoloxidase system (factor 2), four proenzymes (A1, A2, A3, and PHOX) are involved (Seybold et al.
The proenzymes from dogs and rabbits require high concentrations of streptokinase for activation.
Modified proenzymes as artificial substrates for proteolytic enzymes: colorimetric assay of bacterial collagenase and matrix metal loproteinase activity using modified pro-urokinase.
UCB gelatinases are MMPs circulating as latent proenzymes in zymogenic activatable isoforms.
2+] dependence, and p-aminophenyl-mercuric acetate activation (data not shown) identified the plasma gelatinases as fibroblast-derived proMMP-2 and neutrophil-derived proMMP-9, circulating as latent activatable proenzymes.
Modified proenzymes as artificial substrates for proteolytic enzymes: a colorimetric assay of bacterial collagenase and matrix metal loproteinase activity using modified pro-urokinase.