HIV-2 retropepsin

↑ Tözsér, J., Bláha, I., Copeland, T.D., Wondrak, E.M. and Oroszlan, S. (1991). "Comparison of the HIV-1 and HIV-2 proteinases using oligopeptide substrates representing cleavage sites in Gag and Gag-Pol polyproteins". FEBS Lett. 281: 77–80. doi:10.1016/0014-5793(91)80362-7. PMID 2015912.
↑ Chen, Z., Li, Y., Chen, E., Hall, D., Darke, P., Culberson, C., Shafer, J.A. and Kuo, L.A. (1994). "Crystal structure at 1.9-Å resolution of human immunodeficiency virus (HIV) II protease complexed with L-735,524, an orally bioavailable inhibitor of the HIV proteases". J. Biol. Chem. 269: 26344–26348. PMID 7929352.

External links

HIV-2 retropepsin at the US National Library of Medicine Medical Subject Headings (MeSH)

Proteases: aspartate proteases (EC 3.4.23)

Vertebrate	Pepsin Chymosin Renin Signal peptide peptidase Beta secretase 1 2

Pathogenic	Plasmepsin HIV-1 protease

Plant	Nepenthesin

Cathepsin	D E

Proteins: 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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