Related Research Articles
Proteolysis is the breakdown of proteins into smaller polypeptides or amino acids. Uncatalysed, the hydrolysis of peptide bonds is extremely slow, taking hundreds of years. Proteolysis is typically catalysed by cellular enzymes called proteases, but may also occur by intra-molecular digestion.
Adamalysin is an enzyme. This enzyme catalyses the following chemical reaction
Matrilysin also known as matrix metalloproteinase-7 (MMP-7), pump-1 protease (PUMP-1), or uterine metalloproteinase is an enzyme in humans that is encoded by the MMP7 gene. The enzyme has also been known as matrin, putative metalloproteinase-1, matrix metalloproteinase pump 1, PUMP-1 proteinase, PUMP, metalloproteinase pump-1, putative metalloproteinase, MMP). Human MMP-7 has a molecular weight around 30 kDa.
Triflin is a cysteine-rich secretory protein (CRISP), which is excreted by the venom gland of the Habu snake. Triflin reduces high potassium-induced smooth muscle contraction, suggesting a blocking effect on L-type calcium channels.
Latisemin is a cysteine-rich secretory protein that can be isolated from the venom of the Black-banded sea krait, a sea snake indigenous to the warmer waters of the western Pacific Ocean. It is a toxin that inhibits cyclic nucleotide-gated ion channels and blocks L-type calcium channels, thereby reducing smooth muscle contraction.
Atrolysin A is an enzyme that is one of six hemorrhagic toxins found in the venom of western diamondback rattlesnake. This endopeptidase has a length of 419 amino acid residues. The metalloproteinase disintegrin-like domain and the cysteine-rich domain of the enzyme are responsible for the enzyme's hemorrhagic effects on organisms via inhibition of platelet aggregation.
Bothropasin is an enzyme. This enzyme catalyses the following chemical reaction
Atrolysin B is an enzyme. This enzyme catalyses the following chemical reaction
Atrolysin C is an enzyme. This enzyme catalyses the following chemical reaction
Atrolysin E is an enzyme. This enzyme catalyses the following chemical reaction
Atrolysin F is an enzyme. This enzyme catalyses the following chemical reaction
Horrilysin is an enzyme. This enzyme catalyses the following chemical reaction
Ruberlysin is an enzyme. This enzyme catalyses the following chemical reaction
Bothrolysin is an enzyme. This enzyme catalyses the following chemical reaction
Ophiolysin is an enzyme. This enzyme catalyses the following chemical reaction
Trimerelysin II is an enzyme. This enzyme catalyses the following chemical reaction
Mucrolysin is an enzyme. This enzyme catalyses the following chemical reaction
Russellysin is an enzyme. This enzyme catalyses the following chemical reaction
Fibrolase is an enzyme. This enzyme catalyses the following chemical reaction
Jararhagin is an enzyme. This enzyme catalyses the following chemical reaction
References
- ↑ Omori-Satoh T, Sadahiro S (October 1979). "Resolution of the major hemorrhagic component of Trimeresurus flavoviridis venom into two parts". Biochimica et Biophysica Acta (BBA) - Protein Structure. 580 (2): 392–404. doi:10.1016/0005-2795(79)90151-x. PMID 518906.
- ↑ Yamakawa Y, Omori-Satoh T (1988). "The sites of cleavage in oxidized insulin-B chain by a hemorrhagic protease derived from the venom of the habu (Trimeresurus flavoviridis)". Toxicon. 26 (2): 227–31. doi:10.1016/0041-0101(88)90178-x. PMID 3284004.
- ↑ Takeya H, Oda K, Miyata T, Omori-Satoh T, Iwanaga S (September 1990). "The complete amino acid sequence of the high molecular mass hemorrhagic protein HR1B isolated from the venom of Trimeresurus flavoviridis". The Journal of Biological Chemistry. 265 (27): 16068–73. PMID 2398046.
