serine carboxypeptidase

ser·ine car·box·y·pep·ti·dase

a carboxypeptidase of broad specificity for terminal amino acid residues of peptides; the optimal pH is 4.5-6.0; sensitive to diisopropyl fluorophosphate; contains a seryl residue at the active site.
References in periodicals archive ?
Aspartic protease, [beta]-galactosidase, peroxidase and serine carboxypeptidase were detected in three Ephedra species.
Ephedra foeminea drops had a probable defense protein (chitinase), two carbohydrate-modifying enzymes ([beta]-xylosidase, glycosyl-hydrolase-like protein), and proteases (aspartic protease, serine carboxypeptidase).
The exceptions were extracellular proteins, such as serine carboxypeptidase, thaumatin-like protein, acid [alpha]- and [beta]-galactosidase, peroxidase, as well as [alpha]-xylosidase.
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