Target type: molecularfunction
Catalysis of the hydrolysis of peptide bonds in a polypeptide chain by a mechanism in which a water molecule bound by the side chains of aspartic residues at the active center acts as a nucleophile. [GOC:mah, https://www.ebi.ac.uk/merops/about/glossary.shtml#CATTYPE]
Aspartic-type peptidase activity refers to the catalytic mechanism employed by a class of enzymes known as aspartic peptidases. These enzymes cleave peptide bonds within proteins, playing a crucial role in protein degradation and processing. Their catalytic mechanism relies on two aspartic acid residues located within the active site of the enzyme. These residues, often termed Asp1 and Asp2, act in concert to facilitate the hydrolysis of the peptide bond. The mechanism involves the following steps: 1) The substrate peptide binds to the active site of the enzyme, positioning the scissile bond (the peptide bond to be cleaved) between the two aspartic acid residues. 2) Asp1 acts as a general base, abstracting a proton from a water molecule. 3) The activated water molecule then attacks the carbonyl carbon of the scissile bond, forming a tetrahedral intermediate. 4) Asp2, acting as a general acid, donates a proton to the leaving group, the amino group of the peptide bond. 5) The tetrahedral intermediate collapses, breaking the peptide bond and releasing the two peptide fragments. The two aspartic acid residues within the active site work in tandem to facilitate the hydrolysis reaction. Asp1 activates the water molecule for nucleophilic attack, while Asp2 stabilizes the transition state and facilitates the departure of the leaving group. This concerted action of the two aspartic acid residues is essential for the catalytic activity of aspartic peptidases.'
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Protein | Definition | Taxonomy |
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Cathepsin D | A cathepsin D that is encoded in the genome of human. [PRO:DNx, UniProtKB:P07339] | Homo sapiens (human) |
Compound | Definition | Classes | Roles |
---|---|---|---|
nafamostat | nafamostat: inhibitor of trypsin, plasmin, pancreatic kallikrein, plasma kallikrein & thrombin; strongly inhibits esterolytic activities of C1r & C1 esterase complement-mediated hemolysis; antineoplastic | benzoic acids; guanidines | |
1,2-diphenylhydrazine | |||
amprenavir | carbamate ester; sulfonamide; tetrahydrofuryl ester | antiviral drug; HIV protease inhibitor | |
bila 2157 bs | BILA 2157 BS: renin inhibitor; RN given for (1S-(1R*(S*),2S*,3R*))-isomer; structure in first source | ||
resveratrol | trans-resveratrol : A resveratrol in which the double bond has E configuration. | resveratrol | antioxidant; phytoalexin; plant metabolite; quorum sensing inhibitor; radical scavenger |
om99-2 | OM99-2: eight-residue memapsin 2 inhibitor; structure in first source | ||
pl 100 | PL 100: inhibits HIV-1 protease; structure in first source | ||
benzyloxycarbonyl-phe-ala-fluormethylketone | cathepsin B inhibitor : A cysteine protease inhibitor which inhibits cathepsin B (EC 3.4.22.1). | ||
pepstatin | pepstatin: inhibits the aspartic protease endothiapepsin | pentapeptide; secondary carboxamide | bacterial metabolite; EC 3.4.23.* (aspartic endopeptidase) inhibitor |
ca 074 | |||
kni 10006 | |||
balicatib | balicatib: cathepsin K inhibitor | ||
tasiamide b | tasiamide B: 4-amino-3-hydroxy-5-phenylpentanoic acid containing peptide from the marine cyanobacterium Symploca sp.; structure in first source | ||
calpain inhibitor iii | calpain inhibitor III: potential anticataract drug | ||
PF-00835231 | PF-00835231 : A primary alcohol resulting from the cleavage of the phosphate group of the prodrug PF-07304814. It is an inhibitor of SARS-CoV-1 and -2 main protease (3CLpro) and exhibits potent in vitro antiviral activity. | aromatic ether; indolecarboxamide; L-leucine derivative; primary alcohol; pyrrolidin-2-ones; secondary carboxamide | anticoronaviral agent; drug metabolite; EC 3.4.22.69 (SARS coronavirus main proteinase) inhibitor |
gsk188909 | GSK188909: a potent and selective non-peptidic BACE-1 inhibitor; structure in first source | ||
ly2811376 | |||
grassystatin a | grassystatin A: isolated from a cyanobacterium, identified as Lyngbya cf.; structure in first source | ||
ly2886721 | |||
tipranavir | tipranavir : A pyridine-2-sulfonamide substituted at C-5 by a trifluoromethyl group and at the sulfonamide nitrogen by a dihydropyrone-containing m-tolyl substituent. It is an HIV-1 protease inhibitor. tipranavir: inhibits HIV-1 protease | sulfonamide | antiviral drug; HIV protease inhibitor |