Atrolysin C

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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

↑ Bjarnason, J.B. and Tu, A.T. (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: 3395–3404. doi:10.1021/bi00609a033. PMID 210790.
↑ Fox, J.W., Campbell, R., Beggerly, L. and Bjarnason, J.B. (1986). "Substrate specificities and inhibition of two hemorrhagic zinc proteases Ht-c and Ht-d from Crotalus atrox venom". Eur. J. Biochem. 156 (1): 65–72. doi:10.1111/j.1432-1033.1986.tb09549.x. PMID 3514216.
↑ Bjarnason, J.B. and Fox, J.W. (1987). "Characterization of two hemorrhagic zinc proteinases, toxin c and toxin d, from western diamondback rattlesnake (Crotalus atrox) venom". Biochim. Biophys. Acta 911 (3): 356–363. doi:10.1016/0167-4838(87)90077-x. PMID 3101740.
↑ Mori, N., Nikai, T., Sugihara, H. and Tu, A.T. (1987). "Biochemical characterization of hemorrhagic toxins with fibrinogenase activity isolated from 'Crotalus ruber ruber venom". Arch. Biochem. Biophys. 253 (1): 108–121. doi:10.1016/0003-9861(87)90643-6. PMID 2949699.
↑ Shannon, J.D., Baramova, E.N., Bjarnason, J.B. and Fox, F.W. (1989). "Amino acid sequence of a Crotalus atrox venom metalloproteinase which cleaves type IV collagen and gelatin". J. Biol. Chem. 264 (20): 11575–11583. PMID 2745407.
↑ Takeya, H., Onikura, A., Nikai, T., Sugihara, H. and Iwanaga, S. Primary structure of a hemorrhagic metalloproteinase, HT- (1990). "2, isolated from the venom of Crotalus ruber ruber". J. Biochem. (Tokyo) 108 (5): 711–719. PMID 2081731.

External links

Atrolysin C at the US 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	Collagenases MMP1 MMP8 Gelatinases MMP2 MMP9 MMP3 MMP7 MMP10 MMP11 MMP12 MMP13 MMP14 MMP15 MMP16 MMP17 MMP19 MMP20 MMP21 MMP23A MMP23B MMP24 MMP25 MMP26 MMP27 MMP28

Other	Neprilysin Procollagen peptidase Thermolysin Pregnancy-associated plasma protein A Bone morphogenetic protein 1 Lysostaphin Insulin-degrading enzyme ZMPSTE24

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases(list) EC2 Transferases(list) EC3 Hydrolases(list) EC4 Lyases(list) EC5 Isomerases(list) EC6 Ligases(list)

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