3.4.21.61 Ac-(beta-cyclohexyl)alanineYKK 4-methylcoumarin 7-amide + H2O - Saccharomyces cerevisiae 7-amino-4-methylcoumarin + Ac-(beta-cyclohexyl)alanineYKK - ? 365659 3.4.21.61 Ac-Ala-Tyr-Lys-Arg 4-methylcoumarin 7-amide + H2O - Saccharomyces cerevisiae 7-amino-4-methylcoumarin + ? - ? 365674 3.4.21.61 Ac-Ala-Tyr-Lys-Lys 4-methylcoumarin 7-amide + H2O - Saccharomyces cerevisiae 7-amino-4-methylcoumarin + ? - ? 365675 3.4.21.61 Ac-alpha-aminobutyric acid-YKK 4-methylcoumarin 7-amide + H2O - Saccharomyces cerevisiae 7-amino-4-methylcoumarin + Ac-alpha-aminobutyric acid-YKK - ? 365655 3.4.21.61 Ac-Arg-Tyr-Lys-Lys 4-methylcoumarin 7-amide + H2O - Saccharomyces cerevisiae 7-amino-4-methylcoumarin + Ac-Arg-Tyr-Lys-Lys - ? 365666 3.4.21.61 Ac-AYKK 4-methylcoumarin 7-amide + H2O - Saccharomyces cerevisiae 7-amino-4-methylcoumarin + Ac-AYKK - ? 365656 3.4.21.61 Ac-AYKR 4-methylcoumarin 7-amide + H2O - Saccharomyces cerevisiae 7-amino-4-methylcoumarin + Ac-AYKR - ? 365663 3.4.21.61 Ac-Cit-Tyr-Lys-Lys 4-methylcoumarin 7-amide + H2O this substrate is cleaved poorly Saccharomyces cerevisiae 7-amino-4-methylcoumarin + Ac-Cit-Tyr-Lys-Lys 4-methylcoumarin - ? 365667 3.4.21.61 Ac-CYKK 4-methylcoumarin 7-amide + H2O - Saccharomyces cerevisiae 7-amino-4-methylcoumarin + Ac-CYKK - ? 365661 3.4.21.61 Ac-FYKK 4-methylcoumarin 7-amide + H2O - Saccharomyces cerevisiae 7-amino-4-methylcoumarin + Ac-FYKK - ? 365658 3.4.21.61 Ac-Leu-Lys-Arg-p-nitroanilide + H2O - Saccharomyces cerevisiae ? - ? 365651 3.4.21.61 Ac-Nle-Tyr-Lys-Arg 4-methylcoumarin 7-amide + H2O - Saccharomyces cerevisiae 7-amino-4-methylcoumarin + Ac-Nle-Tyr-Lys-Arg-COOH - ? 365671 3.4.21.61 Ac-Nle-Tyr-Lys-Lys 4-methylcoumarin 7-amide + H2O - Saccharomyces cerevisiae 7-amino-4-methylcoumarin + ? - ? 365672 3.4.21.61 Ac-Nle-YKK 4-methylcoumarin 7-amide + H2O - Saccharomyces cerevisiae 7-amino-4-methylcoumarin + Ac-Nle-YKK - ? 365653 3.4.21.61 Ac-Nle-YKR 4-methylcoumarin 7-amide + H2O - Saccharomyces cerevisiae 7-amino-4-methylcoumarin + Ac-Nle-YKR - ? 365662 3.4.21.61 Ac-Nle-YKR 4-methylcoumarin 7-amide + H2O - Saccharomyces cerevisiae 7-amino-4-methylcoumarin + ? - ? 365673 3.4.21.61 Ac-norvaline-YKK 4-methylcoumarin 7-amide + H2O - Saccharomyces cerevisiae 7-amino-4-methylcoumarin + Ac-norvaline-YKK - ? 365654 3.4.21.61 Ac-Pro-Met-Tyr-Lys-Arg 4-methylcoumarin 7-amide + H2O - Saccharomyces cerevisiae 7-amino-4-methylcoumarin + Ac-Pro-Met-Tyr-Lys-Arg - ? 365652 3.4.21.61 Ac-Pro-Met-Tyr-Lys-Arg 4-methylcoumarin 7-amide + H2O - Saccharomyces cerevisiae 7-amino-4-methylcoumarin + ? - ? 365678 3.4.21.61 Ac-RYKK 4-methylcoumarin 7-amide + H2O - Saccharomyces cerevisiae 7-amino-4-methylcoumarin + Ac-RYKK - ? 365660 3.4.21.61 Ac-VYKK 4-methylcoumarin 7-amide + H2O - Saccharomyces cerevisiae 7-amino-4-methylcoumarin + Ac-VYKK - ? 365657 3.4.21.61 alpha-mating factor + H2O cleavage of dibasic sites Saccharomyces cerevisiae ? - ? 74199 3.4.21.61 Arg-Lys(DABCYL)-Nle-Tyr-Lys-Arg-Glu-Ala-Glu-Ala-Glu(EDANS)-Arg + H2O - Saccharomyces cerevisiae Arg-Lys(DABCYL)-Nle-Tyr-Lys-Arg + Glu-Ala-Glu-Ala-Glu(EDANS)-Arg - ? 365680 3.4.21.61 Arg-Lys(DABCYL)-Nle-Tyr-Lys-Lys-Glu-Ala-Glu-Ala-Glu(EDANS)-Arg + H2O - Saccharomyces cerevisiae Arg-Lys(DABCYL)-Nle-Tyr-Lys-Lys + Glu-Ala-Glu-Ala-Glu(EDANS)-Arg - ? 365681 3.4.21.61 benzyloxycarbonyl-Ala-Tyr-Lys-Lys 4-methylcoumarin 7-amide + H2O - Saccharomyces cerevisiae 7-amino-4-methylcoumarin + benzyloxycarbonyl-Ala-Tyr-Lys-Lys - ? 365669 3.4.21.61 benzyloxycarbonyl-Nle-Tyr-Lys-Arg 4-methylcoumarin 7-amide + H2O - Saccharomyces cerevisiae ? - ? 365676 3.4.21.61 benzyloxycarbonyl-Nle-Tyr-Lys-Lys 4-methylcoumarin 7-amide + H2O - Saccharomyces cerevisiae 7-amino-4-methylcoumarin + Cbz-Nle-Tyr-Lys-Lys - ? 365668 3.4.21.61 benzyloxycarbonyl-Nle-YKR 4-methylcoumarin 7-amide + H2O - Saccharomyces cerevisiae ? - ? 365677 3.4.21.61 Benzyloxycarbonyl-Tyr-Lys-Arg 4-nitroanilide + H2O - Saccharomyces cerevisiae ? - ? 15411 3.4.21.61 CLC chloride channel + H2O cleavage in first intracellular loop at residues K136/R137 Saccharomyces cerevisiae proteolytically processed CLC chloride channel - ? 383102 3.4.21.61 corin + H2O activating processing of corin by enzyme PCSK6 Homo sapiens ? - ? 448525 3.4.21.61 D-Ac-Nle-Tyr-Lys-Arg 4-methylcoumarin 7-amide + H2O - Saccharomyces cerevisiae ? - ? 365679 3.4.21.61 Dpy-5 procollagen + H2O - Caenorhabditis elegans ? - ? 397097 3.4.21.61 Killer toxin precursors + H2O cleavage of dibasic sites Saccharomyces cerevisiae ? - ? 369538 3.4.21.61 L-pyroglutamyl-Arg-Thr-Lys-Arg-4-methylcoumaryl-7-amide + H2O - Aeromonas sobria L-pyroglutamyl-Arg-Thr-Lys-Arg + 7-amino-4-methyl-coumarin - ? 397656 3.4.21.61 low density lipoprotein receptor - Homo sapiens ? - ? 412384 3.4.21.61 low density lipoprotein receptor + H2O - Mus musculus ? - ? 412383 3.4.21.61 low density lipoprotein receptor + H2O - Homo sapiens ? - ? 412383 3.4.21.61 low density lipoprotein receptor + H2O - Macaca fascicularis ? - ? 412383 3.4.21.61 low density lipoprotein receptor + H2O degradation Homo sapiens ? - ? 412383 3.4.21.61 low density lipoprotein receptor + H2O a discrete C-terminal protein fragment competes with full-length PCSK9 for binding to LDLR in vitro and attenuates PCSK9-mediated hypercholesterolemia in mice Mus musculus ? - ? 412383 3.4.21.61 low density lipoprotein receptor + H2O C-terminal domain of enzyme has a stronger affinity for substrate low density lipoprotein receptor than catalytic domain. A C-terminal deletion mutant does not mediate low density lipoprotein receptor degradation Homo sapiens ? - ? 412383 3.4.21.61 low density lipoprotein receptor + H2O PCSK9 binding to cell surface low density lipoprotein receptor cannot be described by a simple bimolecular reaction. Data suggest the presence of two populations of binding site Homo sapiens ? - ? 412383 3.4.21.61 low density lipoprotein receptor-related protein 1 + H2O degradation Cricetulus griseus ? - ? 431055 3.4.21.61 low density lipoprotein receptor-related protein 1 + H2O degradation Homo sapiens ? - ? 431055 3.4.21.61 low density lipoprotein receptor-related protein 1 + H2O degradation Mus musculus ? - ? 431055 3.4.21.61 low density lipoprotein receptor-related protein 1 + H2O the enzyme acts on the extracellular domain of the receptor molecule Cricetulus griseus ? - ? 431055 3.4.21.61 low density lipoprotein receptor-related protein 1 + H2O the enzyme acts on the extracellular domain of the receptor molecule Homo sapiens ? - ? 431055 3.4.21.61 low density lipoprotein receptor-related protein 1 + H2O the enzyme acts on the extracellular domain of the receptor molecule Mus musculus ? - ? 431055 3.4.21.61 low-density lipoprotein receptor PCSK9 posttranslationally promotes the degradation of the low-density lipoprotein receptor Homo sapiens ? - ? 412385 3.4.21.61 additional information a variety of trypsin substrates containing only one basic amino acid Saccharomyces cerevisiae ? - ? 89 3.4.21.61 additional information cleaves peptide substrates at both Lys-Arg and Arg-Arg sites, not: benzyloxycarbonyl-Lys-Arg 4-nitroanilide, benzyloxycarbonyl-Arg-Arg 4-nitroanilide Saccharomyces cerevisiae ? - ? 89 3.4.21.61 additional information exhibits optimal activity toward substrates with Lys or Arg at P2 and Arg at P1, also recognizes P4, with dual specificity for aliphatic and basic residues Saccharomyces cerevisiae ? - ? 89 3.4.21.61 additional information generates peptide hormone by specific processing of propeptides Saccharomyces cerevisiae ? - ? 89 3.4.21.61 additional information hydrolyzes peptides and proteins with basic amino acid pairs which are cleaved at the C-ends of their peptide bonds, cleaves specifically large recombinant proteins, for example a protein consisting of a gamma-interferon fragment linked to HIV1-proteinase via a Lys-Arg-containing peptide Saccharomyces cerevisiae ? - ? 89 3.4.21.61 additional information carries out specific endoproteolytic cleavage of proprotein and prohormone precursors in the secretory pathway, hydrolyzes ester and amide substrates Saccharomyces cerevisiae ? - ? 89 3.4.21.61 additional information transforming the precursors of biologically active agents into their functional forms, processing and conversion of prohormones Saccharomyces cerevisiae ? - ? 89 3.4.21.61 additional information wild-type, preference for positively charged residues at P2 position. Mutant D176G/D210A/D211S, preference for MR- over LR- or FR-containing substrates, which cannot be cleaved by wild-type Saccharomyces cerevisiae ? - ? 89 3.4.21.61 additional information CT-peptide is not cleaved by enzymatically active PC1/3 Mus musculus ? - ? 89 3.4.21.61 additional information FRETS-25Xaa libraries as substrates. Best FRETS contains Lys at position Xaa (FRETS-25K). No cleavage of succinyl-Ala-Ala-Pro-Phe-4-methylylcoumaryl-7-amide, t-butyloxycarbonyl-Gly-Arg-Arg-4-methylylcoumaryl-7-amide, Z-His-Glu-Lys-4-methylylcoumaryl-7-amide, and t-butyloxycarbonyl-Phe-Ser-Arg-4-methylylcoumaryl-7-amide Aeromonas sobria ? - ? 89 3.4.21.61 additional information both furinand hepsin-cleaved enzymes are able to degrade LDL receptor on HepG2 cells resulting in elevated serum cholesterol levels Homo sapiens ? - ? 89 3.4.21.61 additional information the enzyme catalytic domain is capable of proteolysis in trans (i.e. as two separate polypeptides), and can perform intermolecular proteolysis Homo sapiens ? - ? 89 3.4.21.61 additional information a variety of trypsin substrates containing only one basic amino acid Saccharomyces cerevisiae overproducing ? - ? 89 3.4.21.61 additional information cleaves peptide substrates at both Lys-Arg and Arg-Arg sites, not: benzyloxycarbonyl-Lys-Arg 4-nitroanilide, benzyloxycarbonyl-Arg-Arg 4-nitroanilide Saccharomyces cerevisiae overproducing ? - ? 89 3.4.21.61 N-tert-butyloxycarbonyl-Gly-Lys-Arg 4-methylcoumarin 7-amide + H2O 59.2% of the activity with tert-butyloxycarbonyl-Gln-Arg-Arg 4-methylcoumarin 7-amide Saccharomyces cerevisiae N-tert-butyloxycarbonyl-Gly-Lys-Arg + 7-amino-4-methylcoumarin - ? 15415 3.4.21.61 pGlu-Arg-Thr-Lys-Arg-4-methylcoumaryl-7-amide + H2O - Mus musculus 7-amino-4-methylcoumarin - ? 398094 3.4.21.61 Precursor protein of the mating hormone alpha-factor of Saccharomyces cerevisiae + H2O processing Saccharomyces cerevisiae ? - ? 369539 3.4.21.61 Precursor protein of the mating hormone alpha-factor of Saccharomyces cerevisiae + H2O processing Saccharomyces cerevisiae overproducing ? - ? 369539 3.4.21.61 prekallikrein cleaved into four fragments by ASP, protein cleaved at specific sequences Aeromonas sobria ? - ? 398145 3.4.21.61 Prm2 - Lachancea kluyveri ? - ? 398148 3.4.21.61 pro-alpha-mating factor + H2O - Saccharomyces cerevisiae alpha-mating factor + ? - ? 365670 3.4.21.61 pro-alpha-mating factor + H2O mating pheromone precursor, physiological substrate Saccharomyces cerevisiae alpha-mating factor + ? - ? 365670 3.4.21.61 proGIP + H2O - Mus musculus GIP - ? 398168 3.4.21.61 proGIP + H2O - Rattus norvegicus GIP - ? 398168 3.4.21.61 Proinsulin + H2O cleaves human proinsulin at the peptide bond between Arg32 and Glu33 Saccharomyces cerevisiae Insulin + ? - ? 15835 3.4.21.61 proopiomelanocortin + H2O - Mus musculus beta-lipotropic hormone + adrenocorticotropic hormone + ? - ? 419015 3.4.21.61 Protein + H2O - Saccharomyces cerevisiae ? - ? 15410 3.4.21.61 Protein + H2O specificity: preference for Lys-Arg, while Arg-Arg, Pro-Arg, Ala-Arg, and Thr-Arg are equally rapidly cleaved but with higher Km Saccharomyces cerevisiae ? - ? 15410 3.4.21.61 Protein + H2O autocatalytic activation at an internal Lys108-Arg109 Saccharomyces cerevisiae ? - ? 15410 3.4.21.61 Protein + H2O precursor protein of the mating hormone alpha-factor of Saccharomyces cerevisiae Saccharomyces cerevisiae ? - ? 15410 3.4.21.61 Protein + H2O specificity towards the carbonyl side of Lys-Arg, Arg-Arg and Pro-Arg sequences Saccharomyces cerevisiae ? - ? 15410 3.4.21.61 Protein + H2O cleaves a wide variety of precursors from higher eukaryotes including prohormones, such as proinsulin and proopiomelanocortin, as well as precursors of constitutively secreteted proteins, such as proalbumin Saccharomyces cerevisiae ? - ? 15410 3.4.21.61 Protein + H2O - Saccharomyces cerevisiae overproducing ? - ? 15410 3.4.21.61 t-butyloxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumaryl-7-amide + H2O - Aeromonas sobria t-butyloxycarbonyl-Arg-Val-Arg-Arg + 7-amino-4-methyl-coumarin - ? 398391 3.4.21.61 t-butyloxycarbonyl-EKK 4-methylcoumarin 7-amide + H2O - Saccharomyces cerevisiae 7-amino-4-methylcoumarin + t-butyloxycarbonyl-EKK - ? 365664 3.4.21.61 t-butyloxycarbonyl-Glu-Lys-Lys-4-methylcoumaryl-7-amide + H2O best substrate Aeromonas sobria t-butyloxycarbonyl-Glu-Lys-Lys + 7-amino-4-methyl-coumarin - ? 398394 3.4.21.61 t-butyloxycarbonyl-Gly-Lys-Arg-4-methylcoumaryl-7-amide + H2O - Aeromonas sobria t-butyloxycarbonyl-Gly-Lys-Arg + 7-amino-4-methyl-coumarin - ? 398395 3.4.21.61 t-butyloxycarbonyl-QGR 4-methylcoumarin 7-amide + H2O - Saccharomyces cerevisiae 7-amino-4-methylcoumarin + t-butyloxycarbonyl-QGR - ? 365665 3.4.21.61 tert-Butyloxycarbonyl-Ala-Pro-Arg 4-methylcoumarin 7-amide + H2O 17% of the activity with tert-butyloxycarbonyl-Gln-Arg-Arg 4-methylcoumarin 7-amide Saccharomyces cerevisiae ? - ? 15417 3.4.21.61 tert-butyloxycarbonyl-Gln-Arg-Arg 4-methylcoumarin 7-amide + H2O - Saccharomyces cerevisiae tert-butyloxycarbonyl-Gln-Arg-Arg + 7-amino-4-methylcoumarin - ? 15412 3.4.21.61 tert-Butyloxycarbonyl-Leu-Arg-Arg 4-methylcoumarin 7-amide + H2O 116% of the activity with tert-butyloxycarbonyl-Gln-Arg-Arg 4-methylcoumarin 7-amide Saccharomyces cerevisiae ? - ? 15413 3.4.21.61 tert-Butyloxycarbonyl-Leu-Lys-Arg 4-methylcoumarin 7-amide + H2O 92.8% of the activity with tert-butyloxycarbonyl-Gln-Arg-Arg 4-methylcoumarin 7-amide Saccharomyces cerevisiae ? - ? 15414 3.4.21.61 tert-Butyloxycarbonyl-Val-Pro-Arg 4-methylcoumarin 7-amide + H2O 38% of the activity with tert-butyloxycarbonyl-Gln-Arg-Arg 4-methylcoumarin 7-amide Saccharomyces cerevisiae ? - ? 15416 3.4.21.61 Ykl077w - Lachancea kluyveri ? - ? 398579