Atrolysin C (EC 3.4.24.42, Crotalus atrox metalloendopeptidase c, hemorrhagic toxin c and d) is an enzyme.^[1]^[2]^[3]^[4]^[5]^[6] This enzyme catalyses the following chemical reaction

Cleavage of His⁵-Leu, His¹⁰-Leu, Ala¹⁴-Leu, Tyr¹⁶-Leu and Gly²³-Phe bonds in B chain of insulin. With small molecule substrates prefers hydrophobic residue at P2' and small residue such as Ala, Gly at P1

This endopeptidase is present in the venom of the western diamondback rattlesnake (Crotalus atrox).

References[edit]

^ Bjarnason JB, Tu AT (August 1978). "Hemorrhagic toxins from Western diamondback rattlesnake (Crotalus atrox) venom: isolation and characterization of five toxins and the role of zinc in hemorrhagic toxin e". Biochemistry. 17 (16): 3395–404. doi:10.1021/bi00609a033. PMID 210790.

^ Fox JW, Campbell R, Beggerly L, Bjarnason JB (April 1986). "Substrate specificities and inhibition of two hemorrhagic zinc proteases Ht-c and Ht-d from Crotalus atrox venom". European Journal of Biochemistry. 156 (1): 65–72. doi:10.1111/j.1432-1033.1986.tb09549.x. PMID 3514216.

^ Bjarnason JB, Fox JW (February 1987). "Characterization of two hemorrhagic zinc proteinases, toxin c and toxin d, from western diamondback rattlesnake (Crotalus atrox) venom". Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 911 (3): 356–63. doi:10.1016/0167-4838(87)90077-x. PMID 3101740.

^ Mori N, Nikai T, Sugihara H, Tu AT (February 1987). "Biochemical characterization of hemorrhagic toxins with fibrinogenase activity isolated from Crotalus ruber ruber venom". Archives of Biochemistry and Biophysics. 253 (1): 108–21. doi:10.1016/0003-9861(87)90643-6. PMID 2949699.

^ Shannon JD, Baramova EN, Bjarnason JB, Fox JW (July 1989). "Amino acid sequence of a Crotalus atrox venom metalloproteinase which cleaves type IV collagen and gelatin". The Journal of Biological Chemistry. 264 (20): 11575–83. PMID 2745407.

^ Takeya H, Onikura A, Nikai T, Sugihara H, Iwanaga S (November 1990). "Primary structure of a hemorrhagic metalloproteinase, HT-2, isolated from the venom of Crotalus ruber ruber". Journal of Biochemistry. 108 (5): 711–9. doi:10.1093/oxfordjournals.jbchem.a123270. PMID 2081731.

External links[edit]

Atrolysin+C at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

Proteases: metalloendopeptidases (EC 3.4.24)

ADAM proteins

Alpha secretases
- ADAM9
- ADAM10
- ADAM17
- ADAM19
ADAM2
ADAM7
ADAM8
ADAM11
ADAM12
ADAM15
ADAM18
ADAM22
ADAM23
ADAM28
ADAM33
ADAMTS1
ADAMTS2
ADAMTS3
ADAMTS4
ADAMTS5
ADAMTS8
ADAMTS9
ADAMTS10
ADAMTS12
ADAMTS13

Matrix metalloproteinases

Other

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

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