proenzyme

(redirected from proenzymes)
Also found in: Dictionary, Thesaurus, Encyclopedia.
Related to proenzymes: Enzyme precursors

proenzyme

 [pro-en´zīm]
zymogen; an inactive precursor of an enzyme.

pro·en·zyme

(prō-en'zīm),
The precursor of an enzyme, requiring some change (usually the hydrolysis of an inhibiting fragment that masks an active grouping) to render it active; for example, pepsinogen, trypsinogen, profibrolysin.
Synonym(s): zymogen

proenzyme

/pro·en·zyme/ (pro-en´zīm) an inactive precursor that can be converted to active enzyme.

proenzyme

(prō-ĕn′zīm′)
n.
The inactive or nearly inactive precursor of an enzyme, converted into an active enzyme by proteolysis. Also called zymogen.

pro·en·zyme

(prō-en'zīm)
The precursor of an enzyme, requiring some change (usually the hydrolysis of an inhibiting fragment that masks an active grouping) to render it active, e.g., pepsinogen, trypsinogen, profibrinolysin.
Synonym(s): zymogen.

proenzyme

A protein that can give rise to an enzyme.

proenzyme

zymogen; an inactive precursor of an enzyme.
References in periodicals archive ?
The fibrinolytic (plasminogen/plasmin) system in the vasculature includes an inactive proenzyme, plasminogen (Pg), which can be converted into the active enzyme, plasmin (Pm), which degrades fibrin into soluble degradation products (2).
The protease to be measured converts a proenzyme into an active enzyme (detection enzyme), and the activity of the latter is detected (Fig.
Trypsin is produced in the exocrine pancreas as two major proenzymes, trypsinogen-1 (cationic) and trypsinogen-2 (anionic), which typically are activated in the duodenum by enterokinase to trypsin-1 and trypsin-2, respectively.
Circulating concentrations of the proenzymes of MMP-2 (gelatinase A; 72-kDa type IV collagenase) and MMP-9 (gelatinase B; 92-kDa type IV collagenase) as well as TEMP-1 and TIMP-2 in healthy controls, patients with CAH, and patients with HCV-induced Ci are shown in Fig.
There are three stages of regulation of proteolytic activity: transcription and secretion, proenzyme activation and activity inhibition by specific tissue inhibitors [22].
The C-terminal region of the heavy chain and the N terminal region of the light chain in the proenzyme resided in a 23-32 residue insert sequence which was not present in other homologs and this region was indicated by homology modeling to form a loop protruding from the remaining part of the enzyme molecule, which should permit the proteolytic cleavage to generate the two chains.