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| Number | Enzyme number | Accepted name | Other names | Source | Substrate | Optimum pH | Optimum temp | Comment |
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| 1 | EC 3.4.23.8 | Yeast proteinase A | Saccharopepsin | — | — | — | — | Now EC 3.4.23.25 |
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| 2 | EC 3.4.23.9 | Rhizopus acid proteinase | Rhizopuspepsin | — | — | — | — | Now EC 3.4.23.21 |
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| 3 | EC 3.4.23.10 | Endothia acid proteinase | Endothiapepsin | — | — | — | — | Now EC 3.4.23.22 |
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| 4 | EC 3.4.23.16 | Retropepsin | HIV aspartyl protease, HIV proteinase, retroproteinase, HIV-l protease, HIV-2 protease | HIV | Viral gag and gag-pol protein precursor | 5.5–6.0 | 30 (37°C) | |
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| 5 | EC 3.4.23.18 | Aspergillopepsin I | Proteinase, Aspergillus acid protease, Aspergillus acid proteinase, Aspergillus aspartic proteinase, Aspergillus carboxyl proteinase, denapsin, proctase B, P, proteinase B, sumizyme AP, trypsinogen kinase, pepsin-type aspartic proteinase, carboxyl proteinase | Found in a variety of Aspergillus species (imperfect fungi) | Hydrolysis of proteins with broad specificity | Differs from substrate to substrate but is in the range of 1.6–6.5 | Differs but in the range of 30–50 | Formerly included in EC 3.4.23.6 |
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| 6 | EC 3.4.23.19 | Aspergillopepsin II | Proteinase A, proctase A, Aspergillus niger var. macrosporus aspartic proteinase, nonpepsin-type acid proteinase | Isolated from Aspergillus niger var. macrosporus | Preferential cleavage in B chain of insulin | — | 30°C | Formerly included in EC 3.4.23.6 |
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| 7 | EC 3.4.23.20 | Penicillopepsin | Peptidase A, Penicillium janthinellum aspartic proteinase, acid protease A, Penicillium X acid proteinase | From the imperfect fungus Penicillium janthinellum | Hydrolysis of proteins with broad specificity similar to that of pepsin A, preferring hydrophobic residues | Differs but in the range of 2.5–3.6 | Differs but in the range of 50–75 | Formerly EC 3.4.23.7; formerly included in EC 3.4.23.6 |
| 8 | EC 3.4.23.21 | Rhizopuspepsin | Rhizopus aspartic proteinase, neurase, proteinase, Rhizopus acid protease, Rhizopus acid proteinase | From the zygomycete fungus Rhizopus chinensis, R. niveus | Hydrolysis of proteins with broad specificity, prefers hydrophobic residues, clots milk, and activates trypsinogen | 3–4 (trypsinogen); 3.5–4.0 (casein) | Differs from substrate to substrate but in the range of 25 and 50 | EC 3.4.23.9 (formerly), EC 3.4.23.6 (formerly included in) |
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| 9 | EC 3.4.23.22 | Endothiapepsin | Endothia aspartic proteinase, Endothia acid proteinase, Endothia parasitica acid proteinase, Endothia parasitica aspartic proteinase | From the ascomycete Endothia parasitica | Hydrolysis of proteins with specificity similar to that of pepsin A, prefers hydrophobic residues | — | 30°C | EC 3.4.23.10 (formerly), EC 3.4.23.6 (formerly included in) |
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| 10 | EC 3.4.23.23 | Mucorpepsin | Proteinase, Mucor acid proteinase, Mucor acid protease, Mucor rennin, Mucor aspartic proteinase Mucor pusillus emporase fromase 100, Mucor pusillus rennin fromase 46TL, Mucor miehei rennin | Isolated from the zygomycete fungi Mucor pusillus and M. miehei | Hydrolysis of proteins, favouring hydrophobic residues, clots milk | Differs but in the range of 3.5–5.6 | Differs but in the range of 40–63 | EC 3.4.23.6 (formerly included in) |
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| 11 | EC 3.4.23.24 | Candidapepsin | Candida albicans aspartic proteinase, Candida albicans carboxyl proteinase, Candida albicans secretory acid proteinase, Candida olea acid proteinase, Candida aspartic proteinase, Candida olea aspartic proteinase | Imperfect yeast Candida albicans | Hydrolyzed protein (preferential cleavage at the carboxyl of hydrophobic aa, activates trypsinogen, and degrades keratin | Varies between 2.5 and 5.5 | 42°C (denatured hemoglobin); 45 (at pH 3.0) | EC 3.4.23.6 (formerly included in) |
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| 12 | EC 3.4.23.25 | Saccharopepsin | Yeast endopeptidase A, Saccharomyces aspartic proteinase, aspartic proteinase yscA, proteinase A, proteinase yscA, yeast proteinase A, Saccharomyces cerevisiae aspartic proteinase A, yeast proteinase A, PRA | Saccharomyces cerevisiae | Hydrolysis of proteins with broad specificity for peptide bonds | 4–6.5 | 25°C | EC 3.4.23.8 (formerly), EC 3.4.23.6 (formerly included in) |
| 13 | EC 3.4.23.26 | Rhodotorulapepsin | Rhodotorula aspartic proteinase, Cladosporium acid protease, Paecilomyces proteinase, Rhodotorula glutinis aspartic Proteinase, Rhodotorula glutinis aspartic, Rhodotorula glutinis acid proteinase | Rhodotorula glutinis and Cladosporium sp. | Cleaves benzyloxycarbonyl-Lys- + -Ala-Ala-Ala and activates trypsinogen | 2.0–2.5 (casein), 2.5–2.7 (casein, hemoglobin), 2.5–3.0 (acid-denatured hemoglobin) | Differs between 55 and 60°C | Formerly included in EC 3.4.99.15 |
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| 14 | EC 3.4.23.28 | Acrocylindropepsin | Acrocylindricum proteinase, Acrocylindrium acid proteinase | Acrocylindrium sp. | Preference for hydrophobic residues at P1 and P10 and action on the B chain of insulin | 2.0 (casein) | — | EC 3.4.99.1 (formerly), EC 3.4.23.6 (formerly included in) |
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| 15 | EC 3.4.23.29 | Polyporopepsin | Polyporus aspartic proteinase, Irpex lacteus aspartic proteinase, Irpex lacteus carboxyl proteinase B | Basidiomycete Polyporus tulipiferae (formerly Irpex lacteus) | Milk-clotting activity, broad specificity, but fails to cleave Leu15-Tyr or Tyr16-Leu of insulin B chain | 2.8 (hemoglobin), 4.0 (Phe-Leu-Ala-Ala) | — | — |
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| 16 | EC 3.4.23.30 synonyms | Pycnoporopepsin | Proteinase ia, Pycnoporus coccineus aspartic proteinase, trametes acid proteinase | Basidiomycete Pycnoporus sanguineus, formerly known as P. coccineus and Trametes sanguinea | Cleaving only three bonds in the B chain of insulin: Ala14 + Leu, Tyr16 + Leu, and Phe24 + Phe | — | — | EC 3.4.99.25 (formerly), EC 3.4.23.6 (formerly included in) |
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| 17 | EC 3.4.23.31 | Scytalidopepsin | Scytalidium aspartic proteinase A, Scytalidium lignicolum aspartic proteinase, Scytalidium lignicolum carboxyl proteinase, Scytalidium lignicolum acid proteinase | Scytalidium lignicolum | Hydrolysis of proteins with specificity similar to that of pepsin A but also cleaves Cys (SO3H)7 Gly and Leu17 Val in the B chain of insulin | 2–3.5 (casein), 3.6 (benzyloxycarbonyl-Phe-Glu-Ala-Ala) | 50 and 55 | — |
| 18 | EC 3.4.23.32 | Scytalidopepsin B | Scytalidium aspartic proteinase B, Ganoderma lucidum carboxyl proteinase, Ganoderma lucidum aspartic proteinase, Scytalidium lignicolum aspartic proteinase B, SLB | A 2nd enzyme from Scytalidium lignicolum, Lentinus edodes (similar enzyme), Ganoderma lucidum (similar enzyme) | Hydrolysis of proteins with broad specificity, cleaving Phe24 Phe, but not Leu15-Tyr and Phe25-Tyr in the B chain of insulin | 2.0–2.7 (casein), 2.9–3.2 (hemoglobin) | 50, 52, and 65 | — |
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| 19 | EC 3.4.23.33 | Xanthomonapepsin | Xanthomonas aspartic proteinase proteinase, Xanthomonas aspartic PCP, pseudomonas carboxyl proteinase | Pseudomonas sp., expression in E. coli, Xanthomonas sp | — | 2.7 (casein, acid-denatured hemoglobin), 3 (acid-denatured hemoglobin, casein) | 50 and 55 | Now transferred to EC 3.4.21.101, xanthomonalisin |
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| 20 | EC 3.4.23.35 | Barrierpepsin | Barrier proteinase, bar proteinase | Saccharomyces cerevisiae | Selective cleavage of -Leu6+ Lys− bond in the mating pheromone a-factor | 5–5.3 | — | — |
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| 21 | EC 3.4.23.36 | Signal peptidase II | Premurein-leader peptidase, prolipoprotein signal peptidase, leader peptidase II, leader peptidase II | E. coli, Enterobacter aerogenes, Staphylococcus aureus | Hydrolyzes -Xaa-Yaa-Zaa+ (S,diacylglyceryl)Cys−, in which Xaa is hydrophobic (preferably Leu) and Yaa (Ala or Ser) and Zaa (Gly or Ala) have Small, neutral side chains | 6 | 37 | — |
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| 22 | EC 3.4.23.37 | Pseudomonapepsin | Pseudomonas sp. pepstatin-insensitive carboxyl proteinase, pepstatin-insensitive carboxyl proteinase | Pseudomonas sp., Xanthomonas sp. | Hydrolysis of the B-chain of insulin at Glu13-Ala-, Leu1S-Tyr-, Phe2S-Tyr-, and angiotensin I at Tyr4-lle. A good synthetic substrate is Lys-Pro-Ile-Glu-Phe-(4-nitro) Phe-Arg-Leu) | 3 (acid-denatured hemoglobin, casein) | 50 | Now EC 3.4.21.100, pseudomonalisin |
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| 23 | EC 3.4.23.41 | Yapsin 1 | Yeast aspartic protease 3, Yap3 | Saccharomyces cerevisiae | Hydrolyzes various precursor proteins with Arg or Lys in P1, and commonly Arg or Lys also in P2 | — | — | — |
| 24 | EC 3.4.23.42 | Thermopsin | — | Thermophilic archeaon Sulfolobus acidocaldarius | Similar in specificity to pepsin A preferring bulky hydrophobic amino acids in P1 and P10 | — | — | — |
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| 25 | EC 3.4.23.43 | Prepilin peptidase | — | Many species of bacteria carry pili | Typically cleaves a –Gly+ Phe− | — | — | — |
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| 26 | EC 3.4.23.44 | Nodavirus endopeptidase | Black Beetle virus endopeptidase, flock house virus endopeptidase | From several nodaviruses that are pathogens of insects | Hydrolysis of an asparaginyl bond, typically –Asn+ Ala− or –Asn+ Phe− | — | — | — |
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| 27 | EC 3.4.23.47 | HIV-2 retropepsin | — | HIV-2 | — | — | — | — |
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| 28 | EC 3.4.23.48 | Plasminogen activator Pla | — | Yersinia pestis that causes plague | Converts human Glu-plasminogen to plasmin by cleaving the Arg560 + Val peptide bond, also cleaves arginyl bonds in other proteins | — | — | — |
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| 29 | EC 3.4.23.49 | Omptin | Protease VII, protease A, ompT protease, protein a, protease VII, OmpT | A product of the ompT gene of Escherichia coli | Has a virtual requirement for Arg in the P1 position | — | — | — |
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| 30 | EC 3.4.23.50 | Human endogenous retrovirus K endopeptidase | Human endogenous retrovirus K10 endopeptidase, endogenous retrovirus HERV-K10 putative protease, human endogenous retrovirus K retropepsin | HIV-1 | Cleavage of the –SQNY+ PIVQ− cleavage site | — | — | — |
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| 31 | EC 3.4.23.51 | HycI peptidase | HycI, HycE processing protein | Escherichia coli | Removes a 32-aa acid peptide from the C-terminus of the precursor of the hydrogenase 3 | — | — | — |
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