Protease
Proteases, usually divided into serine proteases, cysteine proteases, metalloproteases and aspartic proteases, are widely found in animal organs, plant stems and leaves, fruits and microorganisms.
Protease are mainly used for:
• Catalyzing the hydrolysis of proteins and peptides
• Used in protein cleavage experimental procedures
Carboxypeptidase-B rat (EC 3.4.17.2) catalyzes the hydrolysis of the basic amino acids, lysine, arginine, and ornithine from the C-terminal position of polypeptides. Carboxypeptidase-B rat (EC 3.4.17.2) may be used for sequence analysis by successive cleavage of C-terminal basic amino acids.
Proteinase, Aspergillus melleus, is an enzyme that hydrolyzes proteins, that is, it initiates protein catabolism by hydrolyzing the peptide bonds that link amino acids in a polypeptide chain.
Creatinase, Flavobacterium sp. (EC 3.5.3.3) belongs to the hydrolase family and acts on carbon-nitrogen bonds other than peptide bonds, especially in linear amidine compounds. Creatinase, Flavobacterium sp. (EC 3.5.3.3) accelerates the conversion of creatine and water molecules into sarcosine and urea. Creatinase, Flavobacterium sp. (EC 3.5.3.3) functions as a homodimer.
Trypsin Acetylated, Bovine (EC 3.4.21.4) is a serine protease from the PA clan superfamily, found in the digestive system of many vertebrates, where it hydrolyses proteins. Trypsin is produced in the pancreas as the inactive protease trypsinogen. Trypsin cleaves peptide chains mainly at the carboxyl side of the amino acids lysine or arginine, except when either is followed by proline.
Elastase, Rat (EC 3.4.21.35) is a form of elastase that is produced in the acinar cells of the pancreas, initially produced as an inactive zymogen and later activated in the duodenum by trypsin. Elastases form a subfamily of serine proteases, characterized by a distinctive structure consisting of two beta-barrel domains converging at the active site that hydrolyze amides and esters amongst many proteins in addition to elastin, a type of connective tissue that holds organs together.
Protease, Rhizopus sp. is any enzyme that performs proteolysis, that is, begins protein catabolism by hydrolysis of the peptide bonds that link amino acids together in a polypeptide chain.
Carboxypeptidase W, Wheat (EC 3.4.16.6) belongs to the serine carboxypeptidase family and can be inhibited by diisopropyl fluorophosphate.
Aminopeptidase I, Streptomyces griseus (EC 3.4.11.22), exhibits broad substrate specificity, capable of removing the N-terminal residues of most proteins, except when the penultimate residue is an imino acid. Aminopeptidase I contains two Zn2+ binding sites.
Pyroglutamate Aminopeptidase, Pyrococcus furiosus (EC 3.4.19.3), is an enzyme capable of digesting proteins. Pyroglutamate Aminopeptidase specifically acts on the N-terminal pyroglutamic acid, cleaving it from proteins and peptide chains, thereby promoting Edman degradation.
Pyroglutamate Aminopeptidase, Thermococcus thioreducens, is an enzyme capable of digesting proteins. Pyroglutamate Aminopeptidase specifically acts on the N-terminal pyroglutamic acid, cleaving it from proteins and peptide chains, thereby promoting Edman degradation.
Peptidase, Porcine is any enzyme that performs proteolysis, that is, begins protein catabolism by hydrolysis of the peptide bonds that link amino acids together in a polypeptide chain.
Aminopeptidase M, Porcine (EC 3.4.11.2), is a metalloproteinase that hydrolyzes almost all N-terminal amino acids of unsubstituted oligopeptides. It does not cleave X-Pro bonds or N-terminal blocked amino acids. Aminopeptidase M can be used for peptide sequence analysis.
Trypsin, Rat (EC 3.4.21.4) is a serine protease belonging to the PA superfamily. It is present in the digestive systems of many vertebrates and hydrolyzes proteins. Trypsin, Rat (EC 3.4.21.4) primarily cleaves peptide chains at the carboxyl terminus of lysine or arginine, but cleavage does not occur when lysine or arginine is followed by proline.
