3.4.17.23 (7-methoxycoumarin-4-yl)-acetyl-Ala-Pro-Lys(2,4-dinitrophenyl) + H2O - Homo sapiens (7-methoxycoumarin-4-yl)-acetyl-Ala-Pro + N6-(2,4-dinitrophenyl)-L-Lys - ? 390408 3.4.17.23 (7-methoxycoumarin-4-yl)-acetyl-APK(2,4-dinitrophenyl) + H2O - Homo sapiens (7-methoxycoumarin-4-yl)-acetyl-AP + N6-(2,4-dinitrophenyl)-L-Lys - ? 390409 3.4.17.23 (7-methoxycoumarin-4-yl)-acetyl-APK(2,4-dinitrophenyl)-OH + H2O - Rattus norvegicus (7-methoxycoumarin-4-yl)-acetyl-AP + N6-(2,4-dinitrophenyl)-L-Lys - ? 390410 3.4.17.23 (7-methoxycoumarin-4-yl)-acetyl-Tyr-Val-Ala-Asp-Ala-Pro-Lys(2,4-dinitrophenyl)-OH + H2O - Homo sapiens (7-methoxycoumarin-4-yl)-acetyl-Tyr-Val-Ala-Asp-Ala-Pro + N6-(2,4-dinitrophenyl)-L-Lys - ? 390415 3.4.17.23 (7-methoxycoumarin-4-yl)-acetyl-YVADAPK-(2,4-dinitrophenyl)-OH + H2O - Mus musculus (7-methoxycoumarin-4-yl)-acetyl-YVADAP + N6-(2,4-dinitrophenyl)-L-Lys - ? 390416 3.4.17.23 (7-methoxycoumarin-4-yl)-acetyl-YVADAPK-(2,4-dinitrophenyl)-OH + H2O - Homo sapiens (7-methoxycoumarin-4-yl)-acetyl-YVADAP + N6-(2,4-dinitrophenyl)-L-Lys - ? 390416 3.4.17.23 (7-methoxycoumarin-4-yl)-YVADAPK-(2,4-dinitrophenyl)-OH + H2O - Rattus norvegicus (7-methoxycoumarin-4-yl)-YVADAP + N6-(2,4-dinitrophenyl)-L-lysine - ? 390417 3.4.17.23 (7-methoxycoumarin-4-yl)acetyl-Ala-Pro-Lys(2,4-dinitrophenyl) + H2O - Homo sapiens (7-methoxycoumarin-4-yl)acetyl-Ala-Pro + N6-(2,4-dinitrophenyl)-L-lysine - ? 383448 3.4.17.23 (7-methoxycoumarin-4-yl)acetyl-Ala-Pro-Lys(2,4-dinitrophenyl) + H2O - Mus musculus (7-methoxycoumarin-4-yl)acetyl-Ala-Pro + Lys(2,4-dinitrophenyl) - ? 449097 3.4.17.23 (7-methoxycoumarin-4-yl)acetyl-APK(2,4-dinitrophenyl) + H2O - Homo sapiens (7-methoxycoumarin-4-yl)acetyl-AP + N6-(2,4-dinitrophenyl)-L-lysine - ? 383450 3.4.17.23 (7-methoxycoumarin-4-yl)acetyl-APK(2,4-dinitrophenyl) + H2O - Rattus norvegicus (7-methoxycoumarin-4-yl)acetyl-AP + N6-(2,4-dinitrophenyl)-L-lysine - ? 383450 3.4.17.23 (7-methoxycoumarin-4-yl)acetyl-APK(2,4-dinitrophenyl)-OH + H2O synthetic fluorogenic substrate Homo sapiens (7-methoxycoumarin-4-yl)acetyl-AP + N6-(2,4-dinitrophenyl)-L-lysine - ? 375447 3.4.17.23 (7-methoxycoumarin-4-yl)acetyl-APK-(2,4-dinitrophenyl)-OH + H2O - Homo sapiens ? - ? 411089 3.4.17.23 (7-methoxycoumarin-4-yl)acetyl-APK-2,4-dinitrophenyl + H2O - Homo sapiens (7-methoxycoumarin-4-yl)acetyl-AP + N6-(2,4-dinitrophenyl)-L-lysine - ? 383451 3.4.17.23 (7-methoxycoumarin-4-yl)acetyl-YVADAPK(2,4-dinitrophenyl)-OH + H2O synthetic fluorogenic caspase-1 substrate Homo sapiens (7-methoxycoumarin-4-yl)acetyl-YVADAP + N6-(2,4-dinitrophenyl)-L-lysine - ? 375448 3.4.17.23 (des-Arg9)-bradykinin + H2O - Homo sapiens ? - ? 380804 3.4.17.23 7-methoxycoumarin-4-acetyl-Ala-Pro-Lys-(2,4-dinitrophenyl)-OH + H2O - Rattus norvegicus ? - ? 411419 3.4.17.23 7-methoxycoumarin-4-acetyl-Arg-Pro-Pro-Gly-Phe-Ser-Ala-Phe-Lys-(2,4-dinitrophenyl)-OH + H2O - Mus musculus ? - ? 411420 3.4.17.23 7-methoxycoumarin-4-acetyl-Arg-Pro-Pro-Gly-Phe-Ser-Ala-Phe-Lys-(2,4-dinitrophenyl)-OH + H2O - Rattus norvegicus ? - ? 411420 3.4.17.23 7-methoxycoumarin-4-acetyl-Tyr-Val-Ala-Asp-Ala-Pro-Lys-(2,4-dinitrophenyl)-OH + H2O - Mus musculus ? - ? 411430 3.4.17.23 7-methoxycoumarin-4-acetyl-Tyr-Val-Ala-Asp-Ala-Pro-Lys-(2,4-dinitrophenyl)-OH + H2O - Rattus norvegicus ? - ? 411430 3.4.17.23 amyloid-beta protein 43 + H2O ACE2 converts amyloid-beta protein 43 to amyloid-beta protein 42 in mouse brain lysates Mus musculus amyloid-beta protein 42 + ? - ? 430878 3.4.17.23 angiotensin I + H2O - Mus musculus angiotensin-(1-9) + Leu - ? 375046 3.4.17.23 angiotensin I + H2O - Homo sapiens angiotensin-(1-9) + Leu - ? 375046 3.4.17.23 angiotensin I + H2O - Rattus norvegicus angiotensin-(1-9) + Leu - ? 375046 3.4.17.23 angiotensin I + H2O - Rhipicephalus microplus angiotensin-(1-9) + Leu - ? 375046 3.4.17.23 angiotensin I + H2O C-terminal bond between His-Leu is cleaved Homo sapiens angiotensin-(1-9) + Leu - ? 375046 3.4.17.23 angiotensin I + H2O no angiotensin-converting activity, i.e. no conversion of the decapeptide angiotensin I to the octapeptide angiotensin II Homo sapiens angiotensin-(1-9) + Leu - ? 375046 3.4.17.23 angiotensin I + H2O wild-type and truncated mutant Homo sapiens angiotensin-(1-9) + Leu - ? 375046 3.4.17.23 angiotensin I + H2O ACE2 contributes to the production of angiotensin(1-7) from angiotensin I in proximal straight tubule Rattus norvegicus angiotensin-(1-9) + Leu - ? 375046 3.4.17.23 angiotensin I + H2O poor affinity Homo sapiens angiotensin-(1-9) + Leu - ? 375046 3.4.17.23 angiotensin I + H2O the affinity for Ang-I is poor in comparison with ACE, therefore the conversion of Ang-I to Ang-(1-9) is not of physiological importance, except maybe under conditions in which ACE activity is inhibited Homo sapiens angiotensin-(1-9) + Leu - ? 375046 3.4.17.23 angiotensin I + H2O - Homo sapiens DRVYIHPFH + L-Leu - ? 448447 3.4.17.23 angiotensin II + H2O - Mus musculus angiotensin-(1-7) + Phe - ? 376283 3.4.17.23 angiotensin II + H2O - Homo sapiens angiotensin-(1-7) + Phe - ? 376283 3.4.17.23 angiotensin II + H2O - Rattus norvegicus angiotensin-(1-7) + Phe - ? 376283 3.4.17.23 angiotensin II + H2O - Homo sapiens angiotensin-(1-7) + Phe - ir 376283 3.4.17.23 angiotensin II + H2O preferred substrate Homo sapiens angiotensin-(1-7) + Phe - ? 376283 3.4.17.23 angiotensin II + H2O efficient cleavage Homo sapiens angiotensin-(1-7) + Phe - ? 376283 3.4.17.23 angiotensin II + H2O 400fold higher activity than with angiotensin I Homo sapiens angiotensin-(1-7) + Phe - ? 376283 3.4.17.23 angiotensin II + H2O wild-type and truncated mutant Homo sapiens angiotensin-(1-7) + Phe - ? 376283 3.4.17.23 angiotensin II + H2O ACE2 is highly regulated at transcription. ACE2 plays a critical role in regulating the balance between vasoconstrictor and vasodilator effects within the RAS cascade. Angiotensin II may be a stimulus determining cardiac ACE2 gene expression, because either reduction in its levels or prevention of angiotensin II binding to the AT1 receptor increases ACE2 mRNA. ACE2 serves as the cellular entry point for severe acute respiratory syndrome (SARS) virus Rattus norvegicus angiotensin-(1-7) + Phe - ? 376283 3.4.17.23 angiotensin II + H2O the uteroplacental location of angiotensin (1-7) and ACE2 in pregnancy suggests an autocrine function of angiotensin(1-7) in the vasoactive regulation that characterizes placentation and establishes pregnancy Homo sapiens angiotensin-(1-7) + Phe - ? 376283 3.4.17.23 angiotensin II + H2O primary substrate Mus musculus angiotensin-(1-7) + Phe - ? 376283 3.4.17.23 angiotensin II + H2O hepatic production of Ang-(1-7) is catalysed by ACE2 Rattus norvegicus angiotensin-(1-7) + Phe - ? 376283 3.4.17.23 angiotensin II + H2O the major role of ACE2 in Ang peptides metabolism is the production of Ang-(1-7). ACE2 also participates in the metabolism of other peptides non related to the renin-angiotensin system: apelin-13, neurotensin, kinetensin, dynorphin, [des-Arg9]-bradykinin, and [Lys-des-Arg9]-bradykinin Homo sapiens angiotensin-(1-7) + Phe - ? 376283 3.4.17.23 angiotensin II + H2O ACE2 has approximately a 400fold greater affinity for Ang-II than Ang-I Homo sapiens angiotensin-(1-7) + Phe - ? 376283 3.4.17.23 angiotensin II + H2O - Homo sapiens angiotensin-(1-7) + L-Phe - ? 402428 3.4.17.23 angiotensin II + H2O the enzyme is involved in the renin angiotensin system Homo sapiens angiotensin-(1-7) + L-Phe - ? 402428 3.4.17.23 angiotensin II + H2O - Mus musculus angiotensin(1-7) + L-Phe - ? 410726 3.4.17.23 angiotensin II + H2O - Homo sapiens angiotensin(1-7) + L-Phe - ? 410726 3.4.17.23 angiotensin II + H2O - Rattus norvegicus angiotensin(1-7) + L-Phe - ? 410726 3.4.17.23 angiotensin II + H2O - Oryctolagus cuniculus angiotensin(1-7) + L-Phe - ? 410726 3.4.17.23 angiotensin II + H2O - Mus musculus angiotensin(1-7) + L-Phe Ang(1-7) is a vasodilator peptide ? 410726 3.4.17.23 angiotensin II + H2O - Homo sapiens angiotensin(1-7) + L-Phe Ang-(1–7) is a potential endogenous inhibitor of the classical renin-angiotensin system cascade ? 410726 3.4.17.23 angiotensin II + H2O i.e. Asp-Arg-Val-Tyr-Ile-His-Pro-Phe Mus musculus angiotensin(1-7) + L-Phe i.e. Asp-Arg-Val-Tyr-Ile-His-Pro ? 410726 3.4.17.23 angiotensin II + H2O i.e. Asp-Arg-Val-Tyr-Ile-His-Pro-Phe Rattus norvegicus angiotensin(1-7) + L-Phe i.e. Asp-Arg-Val-Tyr-Ile-His-Pro ? 410726 3.4.17.23 angiotensin II + H2O ACE2, a homologue of ACE, EC 3.4.15.1, converts angiotensin II into Ang(1-7). Ang(1-7) shows vasoprotective effects, serum autoantibodies to ACE2 predispose patients with connective tissue diseases to constrictive vasculopathy, pulmonary arterial hypertension, or persistent digital ischemia Homo sapiens angiotensin(1-7) + L-Phe - ? 410726 3.4.17.23 angiotensin II + H2O angiotensin II has many adverse cardiovascular effects when acting through the AT1 receptor Mus musculus angiotensin(1-7) + L-Phe - ? 410726 3.4.17.23 angiotensin II + H2O angiotensin II has many adverse cardiovascular effects when acting through the AT1 receptor Rattus norvegicus angiotensin(1-7) + L-Phe - ? 410726 3.4.17.23 angiotensin II + H2O high levels of angiotensin II induces pulmonary arterial hypertension Rattus norvegicus angiotensin(1-7) + L-Phe - ? 410726 3.4.17.23 angiotensin II + H2O i.e. Asp-Arg-Val-Tyr-Ile-His-Pro-Phe, detection of myocardial ACE2 activity by surface enhanced laser desorption lionization time of flight mass spectroscopy, SELDI-TOF-MS Rattus norvegicus angiotensin(1-7) + L-Phe i.e. Asp-Arg-Val-Tyr-Ile-His-Pro ? 410726 3.4.17.23 angiotensin II + H2O cleavage of angiotensin II analogue is minimally affected by the binding of the SARS-CoV-2 spike protein Homo sapiens angiotensin(1-7) + L-Phe - ? 410726 3.4.17.23 angiotensin II + H2O - Homo sapiens DRVYIHP + L-Phe - ? 448449 3.4.17.23 angiotensin II + H2O - Mus musculus angiotensin-(1-7) + L-phenylalanine - ? 449567 3.4.17.23 angiotensin IV + H2O - Homo sapiens VYIHP + Phe - ? 384198 3.4.17.23 angiotensin-(3-8) + H2O - Homo sapiens angiotensin-(3-7) + Phe - ir 376285 3.4.17.23 angiotensin-(4-8) + H2O - Homo sapiens angiotensin-(4-7) + Phe - ir 376286 3.4.17.23 angiotensin-(5-8) + H2O - Homo sapiens angiotensin-(5-7) + Phe - ir 376287 3.4.17.23 apelin 17 + H2O - Homo sapiens ? - ? 449572 3.4.17.23 apelin-13 + H2O - Homo sapiens apelin-12 + Phe - ? 376295 3.4.17.23 apelin-13 + H2O - Homo sapiens QRPRLSHKGPMP + Phe - ? 384200 3.4.17.23 apelin-13 + H2O - Rattus norvegicus QRPRLSHKGPMP + Phe - ? 384200 3.4.17.23 apelin-13 + H2O - Homo sapiens ? - ? 391294 3.4.17.23 apelin-13 + H2O high catalytic efficiency Mus musculus ? - ? 391294 3.4.17.23 apelin-13 + H2O high catalytic efficiency Rattus norvegicus ? - ? 391294 3.4.17.23 apelin-36 + H2O - Rattus norvegicus apelin-35 + Phe - ? 376296 3.4.17.23 apelin-36 + H2O - Homo sapiens apelin-35 + Phe - ? 376296 3.4.17.23 apelin-36 + H2O - Homo sapiens ? - ? 384201 3.4.17.23 apelin-36 + H2O high catalytic efficiency Mus musculus ? - ? 384201 3.4.17.23 apelin-36 + H2O high catalytic efficiency Rattus norvegicus ? - ? 384201 3.4.17.23 beta-casomorphin + H2O - Mus musculus ? - ? 36403 3.4.17.23 beta-casomorphin + H2O - Rattus norvegicus ? - ? 36403 3.4.17.23 beta-casomorphin + H2O - Homo sapiens YPFVEP + Ile - ? 384322 3.4.17.23 casomorphin + H2O - Rattus norvegicus ? - ? 36621 3.4.17.23 des-Arg10-Lys-bradykinin + H2O - Rattus norvegicus KRPPGFSP + Phe - ? 391815 3.4.17.23 des-Arg9-bradykinin + H2O - Homo sapiens RPPGFSP + Phe - ? 384587 3.4.17.23 des-Arg9-bradykinin + H2O - Mus musculus ? - ? 384588 3.4.17.23 des-Arg9-bradykinin + H2O - Rattus norvegicus ? - ? 384588 3.4.17.23 des-Arg9-bradykinin + H2O ACE2 cleavage of des-Arg9-bradykinin substrate analogue is markedly accelerated by SARS-CoV-2 infection Homo sapiens ? - ? 384588 3.4.17.23 des-Arg9-bradykinin + H2O - Rattus norvegicus bradykinin (1-7) + Phe - ? 391816 3.4.17.23 dynorphin A + H2O - Mus musculus ? - ? 15770 3.4.17.23 dynorphin A + H2O - Rattus norvegicus ? - ? 15770 3.4.17.23 dynorphin A 1-13 + H2O - Homo sapiens dynorphin A 1-12 + Lys - ir 376759 3.4.17.23 dynorphin A(1-13) + H2O - Homo sapiens YGGFLRRIRPKL + Lys - ? 384653 3.4.17.23 ghrelin + H2O - Homo sapiens ghrelin minus C-terminal amino acid + arginine - ir 376846 3.4.17.23 ghrelin + H2O - Homo sapiens ? - ? 384770 3.4.17.23 kinetensin + H2O - Rattus norvegicus ? - ? 355639 3.4.17.23 KRPPGSPF + H2O i.e. Lys-des-Arg-bradykinin Homo sapiens KRPPGSP + Phe - ir 377014 3.4.17.23 Lys-des-Arg9 bradykinin + H2O - Homo sapiens KRPPGFSP + Phe - ? 385106 3.4.17.23 Lys-des-Arg9-bradykinin + H2O - Mus musculus ? - ? 392507 3.4.17.23 Lys-des-Arg9-bradykinin + H2O - Rattus norvegicus ? - ? 392507 3.4.17.23 additional information ACE2 is a crucial SARS-CoV receptor. SARS-CoV infections and the Spike protein of the SARS-CoV reduce ACE2 expression. Injection of SARS-CoV Spike into mice worsens acute lung failure in vivo that can be attenuated by blocking the renin-angiotensin pathway Mus musculus ? - ? 89 3.4.17.23 additional information angiotensin-converting enzyme 2: a functional receptor for SARS coronavirus Chlorocebus aethiops ? - ? 89 3.4.17.23 additional information presence of ACE2 alone is not sufficient for maintaining viral infection. Other virus receptors or coreceptors may be required in different tissues Homo sapiens ? - ? 89 3.4.17.23 additional information the enzyme has a function in blood pressure regulation, blood flow and fluid regulation. Loss of ACE2 impairs heart function Homo sapiens ? - ? 89 3.4.17.23 additional information the enzyme is involved in diesease condition including hypertension, diabetes and cardiac function. ACE2 is the SARS virus receptor Homo sapiens ? - ? 89 3.4.17.23 additional information angiotensin I is not a good substrate for recombinant human ACE2 Homo sapiens ? - ? 89 3.4.17.23 additional information no activity with angiotensin (1-9) and angiotensin(1-7) Homo sapiens ? - ? 89 3.4.17.23 additional information no hydrolysis of angiotensin (1-9), angiotensin (1-7), bradikinin, bradykinin(1-7), neurotensin(1-13) Homo sapiens ? - ? 89 3.4.17.23 additional information ACE2 functions as a carboxymonopeptidase with a preference for C-terminal Leu or Phe, ACE2 counterbalances the enzymatic actions of ACE, ACE2 does not metabolize bradykinin Mus musculus ? - ? 89 3.4.17.23 additional information ACE2 functions as a carboxymonopeptidase with a preference for C-terminal Leu or Phe, ACE2 counterbalances the enzymatic actions of ACE, ACE2 does not metabolize bradykinin Rattus norvegicus ? - ? 89 3.4.17.23 additional information the ACE2 ectodomain can be cleaved from the cell membrane and released into the extracellular milieu by stimulation of phorbol esters and ADAM17, calmodulin inhibits shedding of the ACE2 ectodomain from the membrane Homo sapiens ? - ? 89 3.4.17.23 additional information ACE2 ectodomain shedding and/or sheddase(s) activation regulated by calmodulin is independent from the phorbol ester-induced shedding Homo sapiens ? - ? 89 3.4.17.23 additional information ACE2 is down-regulated and ACE is up-regulated in hypertensive nephropathy. Ang II, once released, can act to up-regulate ACE but down-regulate ACE2 via the AT1 receptor-mediated mechanism. Activation of the ERK1/2 and p38 MAP kinase pathway may represent a key mechanism by which Ang II down-regulates ACE2 Homo sapiens ? - ? 89 3.4.17.23 additional information ACE2 is involved in the regulation of heart function, ACE 2 is a functional receptor for the coronavirus that causes the severe acute respiratory syndrome Homo sapiens ? - ? 89 3.4.17.23 additional information ACE2 plays a crucial role in liver fibrogenesis Rattus norvegicus ? - ? 89 3.4.17.23 additional information ACE2 plays a key role in pulmonary, cardiovascular and hypertensive and diabetic kidney diseases. ACE2 plays a pivotal role in maintaining a balanced status of the RAS synergistically with ACE by exerting counter-regulatory effects Homo sapiens ? - ? 89 3.4.17.23 additional information ACE2 plays a pivotal role in the central regulation of blood pressure and volume homeostasis Mus musculus ? - ? 89 3.4.17.23 additional information ACE2 plays a protective role in organs directly related to hypertension and associated diseases Homo sapiens ? - ? 89 3.4.17.23 additional information the affinity for Ang-I is poor in comparison with ACE, therefore the conversion of Ang-I to Ang-(1-9) is not of physiological importance, except maybe under conditions in which ACE activity is inhibited Homo sapiens ? - ? 89 3.4.17.23 additional information ACE2 functions predominantly as a carboxymonopeptidase with a substrate preference for hydrolysis between proline and a hydrophobic or basic C-terminal residue Homo sapiens ? - ? 89 3.4.17.23 additional information hydrolyses its substrates by removing a single amino acid from their respective C-terminal Homo sapiens ? - ? 89 3.4.17.23 additional information ACE2 activation promotes antithrombotic activity. ACE2 is an ACE, EC 3.4.15.1, homologue Mus musculus ? - ? 89 3.4.17.23 additional information ACE2 activation promotes antithrombotic activity. ACE2 is an ACE, EC 3.4.15.1, homologue Rattus norvegicus ? - ? 89 3.4.17.23 additional information ACE2 is a terminal carboxypeptidase and the receptor for the SARS and NL63 coronaviruses. Soluble sACE2 acts as receptor binding SARS-CoV glycoprotein S pseudotyped FIV virus and blocks virus infection of target cells Homo sapiens ? - ? 89 3.4.17.23 additional information a combination of ACE2 and ACE convert amyloid-beta protein 43 to amyloid-beta protein 40 Mus musculus ? - ? 89 3.4.17.23 additional information the requirements for ACE2 binding at the first position of a tetrapeptide substrate, i.e. fourth position from the Ang II C-terminus XHPF, are a preference for non-polar, hydrophobic or cyclic residues, with Val and Pro substitutions showing enhanced binding. No strict preference is observed at position two of the tetrapeptide IXPF. Apolar cyclic residues Phe and Pro are not tolerated at the position. Substitution of position three results in moderate increases in binding for Val, 77% and decreases for Ile. The only other functional group tolerated at this position is naphthalene. Peptides PYPF/PHVF/PYVF show almost equivalent ACE2 binding compared to full-length angiotensin II Homo sapiens ? - ? 89 3.4.17.23 neocasomorphin + H2O - Homo sapiens neocasomorphin minus C-terminal amino acid + isoleucine - ir 377349 3.4.17.23 neurotensin + H2O - Mus musculus ? - ? 15385 3.4.17.23 neurotensin + H2O - Rattus norvegicus ? - ? 15385 3.4.17.23 neurotensin 1-13 + H2O - Rattus norvegicus ? - ? 392886 3.4.17.23 neurotensin(1-11) + H2O - Homo sapiens pELYENKPRRP + Tyr - ? 385402 3.4.17.23 neurotensin(1-8) + H2O - Homo sapiens pELYENKP + Arg - ? 385403 3.4.17.23 neurotensin-(1-8) + H2O - Homo sapiens neurotensin-(1-7) + arginine - ir 377355 3.4.17.23 pyr-apelin 13 + H2O - Homo sapiens ? - ? 450528 3.4.17.23 QRPRLSHKGPMPF + H2O i.e. apein(1-13) Homo sapiens QRPRLSHKGPMP + L-Phe - ? 460236 3.4.17.23 RPPGSPF + H2O i.e. des-Arg-bradykinin Homo sapiens RPPGSP + Phe i.e. des-Arg-bradykinin-(1-7) ir 377609 3.4.17.23 SARS-coronavirus S1 protein + H2O - Homo sapiens ? - ? 393467 3.4.17.23 SARS-coronavirus S1 protein + H2O - Mus musculus ? - ? 393467 3.4.17.23 SARS-coronavirus S1 protein + H2O - Felis silvestris ? - ? 393467 3.4.17.23 SARS-coronavirus S1 protein + H2O - Rattus norvegicus ? - ? 393467 3.4.17.23 TBC5046 + H2O synthetic fluorogenic peptide, i.e. des-Arg-bradykinin with N-terminal o-aminobenzoic acid and a 3-nitrophenylalanine instead of Phe at the C-terminus Homo sapiens o-aminobenzoic acid-des-Arg-bradykinin-(1-7) + 3-nitrophenylalanine - ir 377849 3.4.17.23 YGGFLRRIRPKLK + H2O i.e. dynorphin A 1-13 Homo sapiens YGGFLRRIRPKL + L-Lys - ? 460254 3.4.17.23 YPVEPFI + H2O i.e. beta-casomorphin Homo sapiens YPVEPF + Ile - ir 378333