Tyrpsin
Tyrpsin is a serine protease found in digestive system of many vertebrates. Tyrpsin is produced in the pancreas as the inactive proenzyme trypsinogen. trypsin cleaves peptide chains mainly at the carboxyl side of the amino acid lysine or arginine,except when either is followed by proline. It is used for numerous biotechnological processes.
Molecular Description
Molecule: Chymotrypsin inhibitor 3
Classifucation: Hydrolase Inhibitor
Structure Weight: 41630.11
Polymer 1 with polypeptide (L) type, 187 in length
Chains: A and B
Molecular Function
- Endopeptidase inhibitor activity
- Serine-type endopeptidase inhibitor activity
- Peptidase inhibitor activity
DSSP secondary structure
- 3% helical (2 helices; 7 residues)
- 37% beta sheet (20 strands; 70 residues)
Subtilisin
Subtilisin a.k.a serine endopeptidase is protease (a protein-digesting enzyme) initially obtained from Bacillus subtilis. They are physically and chemically well characterized enzymes. They can obtained from soil bacteria, for example Bacillus amyloliguefaciens. Subtilisin are secreted in large amounts from many Bacillus species.
Molecular Description
Classification: Hydrolase
Structure Weight: 142388.37
Molecule: Subtilisin-like protease
Polymer 1 with polypeptide (L) type, 649 in length
Chains: A and B
Fragment: UNP residues 113-761
Molecular Function
- Serine-type endopeptidase activity
- Peptidase activity
- Serine-type peptidase activity
- Hydrolase activity
- Identical protein binding
Biological process
- Proteolysis
- Negative regulation of catalytic activity
DSSP secondary structure
- 22% helical (20 helices;146 residues)
- 29% beta sheet (44 strands; 190 residues)
Termolysin
Classification: Hydrolase
Structure Weight: 35432.25
Molecule: Termolysin
Polymer 1 with polypeptide (L) type, 316 in length
Chains: A and B
Fragment: UNP residues 233-548
Molecular Function
- Metalloendopeptidase activity
- Calcium Ion binding
- Peptidase activity
- Metallopeptidase activity
- Zinc Ion binding
- Hydrolase activity
- Metral Ion binding
Biological Process
- Proteolysis
Cellular Component
- Extracellular region
Chains: A and B
Fragment: UNP residues 113-761
Molecular Function
- Serine-type endopeptidase activity
- Peptidase activity
- Serine-type peptidase activity
- Hydrolase activity
- Identical protein binding
Biological process
- Proteolysis
- Negative regulation of catalytic activity
DSSP secondary structure
- 22% helical (20 helices;146 residues)
- 29% beta sheet (44 strands; 190 residues)
Termolysin
Structure Weight: 35432.25
Molecule: Termolysin
Polymer 1 with polypeptide (L) type, 316 in length
Chains: A and B
Fragment: UNP residues 233-548
Molecular Function
- Metalloendopeptidase activity
- Calcium Ion binding
- Peptidase activity
- Metallopeptidase activity
- Zinc Ion binding
- Hydrolase activity
- Metral Ion binding
Biological Process
- Proteolysis
Cellular Component
- Extracellular region
