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Information on EC 3.4.23.5 - cathepsin D and Organism(s) Homo sapiens

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.23 Aspartic endopeptidases
                3.4.23.5 cathepsin D
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Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Specificity similar to, but narrower than, that of pepsin A. Does not cleave the Gln4-His bond in B chain of insulin
Synonyms
cathepsin d, cath-d, cath d, cat d, cathd, pro-cathepsin d, cat-d, pro-cathepsin, cad 1, cad 2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
cath-D
-
-
cathepsin D
matCTSD
preproCatD
-
inactive zymogen
pro-cathepsin
-
pro-cathepsin D
-
-
pro-CD
proCat
-
proenzyme
proCDrec
-
-
proCTSD
-
inactive precursor
CAS REGISTRY NUMBER
COMMENTARY hide
9025-26-7
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
((7-methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly-Leu-N-3-(2,4-dinitro-phenyl)-L-2,3-diaminopropionyl-Ala-Arg-NH2) + H2O
?
show the reaction diagram
-
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly-Leu-N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-Ala-Arg-NH2 + H2O
?
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-AAKFFSRQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-AAKF + FSRQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
?
2-aminobenzoyl-AEKFFSRQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-AEKF + FSRQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
?
2-aminobenzoyl-AIAFFSRQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-AIAF + FSRQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
?
2-aminobenzoyl-AIEFFSRQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-AIEF + FSRQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
?
2-aminobenzoyl-AIFFFSRQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-AIFF + FSRQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
?
2-aminobenzoyl-AIIFFSRQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-AIIF + FSRQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
?
2-aminobenzoyl-AIKFFARQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-AIKF + FARQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
?
2-aminobenzoyl-AIKFFERQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-AIKF + FERQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
?
2-aminobenzoyl-AIKFFIRQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-AIKF + FIRQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
?
2-aminobenzoyl-AIKFFKRQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-AIKF + FKRQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
?
2-aminobenzoyl-AIKFFLRQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-AIKF + FLRQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
?
2-aminobenzoyl-AIKFFNRQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-AIKF + FNRQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
?
2-aminobenzoyl-AIKFFORQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-AIKF + FORQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
?
2-aminobenzoyl-AIKFFRRQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-AIKF + FRRQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
?
2-aminobenzoyl-AIKFFSA-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
2-aminobenzoyl-AIKF + FSA-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-AIKFFSAQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-AIKF + FSAQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
2-aminobenzoyl-AIKFFSAQTNR-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
2-aminobenzoyl-AIKF + FSAQTNR-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-AIKFFSAQTNRHILRFNR-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
2-aminobenzoyl-AIKF + FSAQTNRHILRFNR-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-AIKFFSAQTNRHILRFNRQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-AIKF + FSAQTNRHILRFNRQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
2-aminobenzoyl-AIKFFSAQTNRQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-AIKF + FSAQTNRQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
2-aminobenzoyl-AIKFFSEQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-AIKF + FSEQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
?
2-aminobenzoyl-AIKFFSIQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-AIKF + FSIQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
?
2-aminobenzoyl-AIKFFSKQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-AIKF + FSKQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
?
2-aminobenzoyl-AIKFFSLQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-AIKF + FSLQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
?
2-aminobenzoyl-AIKFFSNQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-AIKF + FSNQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
?
2-aminobenzoyl-AIKFFSOQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-AIKF + FSOQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
?
2-aminobenzoyl-AIKFFSPQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-AIKF + FSPQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
?
2-aminobenzoyl-AIKFFSRQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-AIKF + FSRQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
?
2-aminobenzoyl-AIKFFSSQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-AIKF + FSSQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
?
2-aminobenzoyl-AIKFFSTQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-AIKF + FSTQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
?
2-aminobenzoyl-AIKFFSVQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-AIKF + FSVQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
?
2-aminobenzoyl-AIKFFTRQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-AIKF + FTRQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
?
2-aminobenzoyl-AIKFFVRQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-AIKF + FVRQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
?
2-aminobenzoyl-AIKFMSRQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-AIKF + MSRQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
?
2-aminobenzoyl-AIKLFSRQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-AIKL + FSRQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
?
2-aminobenzoyl-AIKLLSRQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-AIKL + LSRQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
?
2-aminobenzoyl-AIKLMSRQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-AIKL + MSRQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
?
2-aminobenzoyl-AIKMFLRQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-AIKM + LSRQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
?
2-aminobenzoyl-AIKMFSRQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-AIKM + FSRQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
?
2-aminobenzoyl-AIKMMSRQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-AIKM + MSRQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
?
2-aminobenzoyl-AIKYYSRQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-AIKY + YSRQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
?
2-aminobenzoyl-AILFFSRQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-AILF + FSRQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
?
2-aminobenzoyl-AIMFFSRQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-AIMF + FSRQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
?
2-aminobenzoyl-AINFFSRQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-AINF + FSRQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
?
2-aminobenzoyl-AIPFFSRQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-AIPF + FSRQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
?
2-aminobenzoyl-AIQFFSRQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-AIQF + FSRQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
?
2-aminobenzoyl-AISFFSRQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-AISF + FSRQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
?
2-aminobenzoyl-AITFFSRQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-AITF + FSRQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
?
2-aminobenzoyl-AIVFFSRQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-AIVF + FSRQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
?
2-aminobenzoyl-AKKFFSRQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-AKKF + FSRQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
?
2-aminobenzoyl-ALKFFSRQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-ALKF + FSRQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
?
2-aminobenzoyl-ANKFFSRQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-ANKF + FSRQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
?
2-aminobenzoyl-APKFFSRQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-APKF + FSRQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
?
2-aminobenzoyl-AQKFFSRQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-AQKF + FSRQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
?
2-aminobenzoyl-ASKFFSRQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-ASKF + FSRQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
?
2-aminobenzoyl-ATKFFSRQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-ATKF + FSRQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
?
2-aminobenzoyl-AVKFFSRQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-AVKF + FSRQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
?
2-aminobenzoyl-KITLLSALVETRIVRFNRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
?
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-KITLLSALVETRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
?
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-KITLLSAQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
?
show the reaction diagram
-
-
-
-
?
Acid-denatured hemoglobin + H2O
?
show the reaction diagram
-
-
-
-
?
actin + H2O
?
show the reaction diagram
-
-
-
-
?
Ala-Pro-Ala-Lys-Phe-(4-nitro)Phe-Arg-Leu + H2O
Ala-Pro-Ala-Lys-Phe + (4-nitro)Phe-Arg-Leu
show the reaction diagram
-
-
-
?
Albumin + H2O
?
show the reaction diagram
alpha-synuclein + H2O
?
show the reaction diagram
alpha1-Antichymotrypsin + H2O
?
show the reaction diagram
Amca-EEKPISFFRLGK + H2O
Amca-EEKPISF + FRLGK
show the reaction diagram
-
CatD cleaves the substrate Amca-EEKPISFFRLGK specifically between the two phenylalanine residues yielding the two peptides Amca-EEKPISF and FRLGK. Only the first peptide can be detected using fluorescence detection
-
-
?
aminomethylcoumarin-hemoglobin + H2O
?
show the reaction diagram
-
-
-
-
?
aminomethylcoumarine-conjugated hemoglobin + H2O
?
show the reaction diagram
-
-
-
-
?
amyloid beta A4 protein + H2O
?
show the reaction diagram
-
-
-
-
?
amyloid precursor protein + H2O
?
show the reaction diagram
-
-
-
-
?
androgen receptor + H2O
?
show the reaction diagram
-
-
-
-
?
angiostatin + H2O
?
show the reaction diagram
-
-
-
-
?
apolipoprotein B + H2O
?
show the reaction diagram
-
-
-
-
?
apolipoprotein E + H2O
?
show the reaction diagram
-
-
-
-
?
Arg-Pro-Ala-Lys-Phe-(4-nitro)Phe-Arg-Leu + H2O
Arg-Pro-Ala-Lys-Phe + (4-nitro)Phe-Arg-Leu
show the reaction diagram
-
-
-
?
Asp-Pro-Ala-Lys-Phe-(4-nitro)Phe-Arg-Leu + H2O
Asp-Pro-Ala-Lys-Phe + (4-nitro)Phe-Arg-Leu
show the reaction diagram
-
-
-
?
Bcl-2 protein + H2O
?
show the reaction diagram
-
-
-
-
?
BID + H2O
?
show the reaction diagram
-
-
-
-
?
Bovine hemoglobin + H2O
?
show the reaction diagram
-
conjugated to the fluorochrome 6-((7-amino-4-methylcoumarin-3-acetyl) amino) hexanoic acid, succinimidyl ester
-
-
?
Bovine serum albumin + H2O
?
show the reaction diagram
-
highest cleavage activity for bovine serum albumin at pH 3.5
-
-
?
casein + H2O
?
show the reaction diagram
-
-
-
-
?
caspase-3 + ?
?
show the reaction diagram
-
-
-
-
?
cathepsin B + H2O
?
show the reaction diagram
-
-
-
-
?
cathepsin L + H2O
?
show the reaction diagram
-
-
-
-
?
collagens + H2O
?
show the reaction diagram
-
-
-
-
?
connectin + H2O
?
show the reaction diagram
-
-
-
-
?
cystatin C + H2O
?
show the reaction diagram
-
-
-
-
?
dermcidin + H2O
?
show the reaction diagram
-
-
-
-
?
EEISEVKMDAEFRG + H2O
EEISEVKM + DAEFRG
show the reaction diagram
-
beta-secretase activity assay: wild-type peptide substrate (14-mer) of the amyloid precursor protein. Cathepsin D shows only poor activity towards the wild-type beta-site sequence
-
-
?
EEISEVNLDAEFRG + H2O
EEISEVNL + DAEFRG
show the reaction diagram
-
beta-secretase activity assay: mutated Swedish family (SW) peptide subtrate (14-mer) with the two mutated residues flanking the beta-site of the amyloid precursor protein
-
-
?
endostatin + H2O
?
show the reaction diagram
-
-
-
-
?
Fibrin + H2O
?
show the reaction diagram
-
-
-
-
?
Fibrinogen + H2O
?
show the reaction diagram
-
-
-
-
?
fibrinogen + H2O
low molecular weight fragments of fibrinogen
show the reaction diagram
-
cleaves the alpha-chain, the beta-chain and the gamma-chain
-
?
fibroblast growth factor + H2O
?
show the reaction diagram
-
-
-
-
?
Fibronectin + H2O
?
show the reaction diagram
-
-
-
-
?
GKPILFFRLK(Dnp)-D-R-NH2 + H2O
?
show the reaction diagram
-
-
-
?
Glu-Glu-His-Phe-Phe-Ala-Ala + H2O
?
show the reaction diagram
-
-
-
-
?
Glu-Glu-His-Phe-Phe-Ala-Leu-methyl ester + H2O
?
show the reaction diagram
-
-
-
-
?
Glucagon + H2O
?
show the reaction diagram
-
-
-
-
?
glycated hemoglobin + H2O
LVV-hemorphin-7 + VV-hemorphin-7 + hemorphin-7 + ?
show the reaction diagram
-
-
-
-
?
Hemoglobin + H2O
?
show the reaction diagram
human apo-transferrin + H2O
?
show the reaction diagram
-
-
-
-
?
human serum albumin + H2O
?
show the reaction diagram
-
-
-
-
?
insulin + H2O
?
show the reaction diagram
insulin-like growth factor binding protein + H2O
?
show the reaction diagram
-
-
-
-
?
interleukin-1 + H2O
?
show the reaction diagram
-
-
-
-
?
kallistatin + H2O
?
show the reaction diagram
kininogen + H2O
?
show the reaction diagram
-
-
-
-
?
Leu-Pro-Ala-Lys-Phe-(4-nitro)Phe-Arg-Leu + H2O
Leu-Pro-Ala-Lys-Phe + (4-nitro)Phe-Arg-Leu
show the reaction diagram
-
-
-
?
LLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES + H2O
LLGDF + FRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES
show the reaction diagram
-
LL-37, peptide present in human sweat. Only weak cleavage is seen between Phe5 and Phe6 yielding FRK-32 and between Phe27 and Leu28 yielding LRN-10 and LLG-27
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-
?
LLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES + H2O
LLGDFFRKSKEKIGKEFKRIVQRIKDF + LRNLVPRTES
show the reaction diagram
-
LL-37, peptide present in human sweat. Only weak cleavage is seen between Phe5 and Phe6 yielding FRK-32 and between Phe27 and Leu28 yielding LRN-10 and LLG-27
-
-
?
LLVVFF + H2O
LVVFF + VVFF + LLVVF + LVVF + VVF + Leu-Leu + Phe
show the reaction diagram
-
-
-
-
?
LLVVYPWTQRFF + H2O
LVVYPWTQRFF + VVYPWTQRFF + LLVVYPWTQRF + LVVYPWTQRF + VVYPWTQRF + Leu-Leu + Phe
show the reaction diagram
-
cleavage occurs at the C-terminus (F-F) and the N-terminus (L-L, L-V and LL-V)
-
-
?
Lys-Pro-Ala-Asp-Phe-(4-nitro)Phe-Arg-Leu + H2O
Lys-Pro-Ala-Asp-Phe + (4-nitro)Phe-Arg-Leu
show the reaction diagram
-
-
-
?
Lys-Pro-Asn-Gln-Phe-(4-nitro)Phe-Arg-Leu + H2O
Lys-Pro-Asn-Gln-Phe + (4-nitro)Phe-Arg-Leu
show the reaction diagram
-
-
-
?
Lys-Pro-Ile-Glu-Phe-(4-nitro)Phe-Arg-Leu + H2O
Lys-Pro-Ile-Glu-Phe + (4-nitro)Phe-Arg-Leu
show the reaction diagram
-
-
-
?
Lys-Pro-Thr-Val-Phe-(4-nitro)Phe-Arg-Leu + H2O
Lys-Pro-Thr-Val-Phe + (4-nitro)Phe-Arg-Leu
show the reaction diagram
-
-
-
?
Lys-Pro-Val-Ser-Tyr-(4-nitro)Phe-Arg-Leu + H2O
Lys-Pro-Val-Ser-Tyr + (4-nitro)Phe-Arg-Leu
show the reaction diagram
-
-
-
?
macrophage inflammatory protein-1 alpha + H2O
?
show the reaction diagram
-
-
-
-
?
macrophage inflammatory protein-1 beta + H2O
?
show the reaction diagram
-
-
-
-
?
Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2 + H2O
?
show the reaction diagram
-
-
-
-
?
MOCAc-Gly-Lys-Pro-Ile-Leu-Phe-Phe-Arg-Leu-Lys(Dnp)gamma-NH2 + H2O
?
show the reaction diagram
-
-
-
-
?
MOCAc-Lys-Arg-Gly-Leu-Tyr-Phe-Ile-Thr-His-Lys(Dnp) + H2O
?
show the reaction diagram
-
-
-
-
?
mutant huntingtin + H2O
?
show the reaction diagram
-
-
-
-
?
myelin basic protein + H2O
?
show the reaction diagram
-
-
-
-
?
myosin + H2O
?
show the reaction diagram
-
-
-
-
?
N-t-BOC-Phe-Ala-Ala-Phe(4-nitro)-Phe-Val-Leu-4-hydroxymethylpyridine ester + H2O
?
show the reaction diagram
-
-
-
-
?
neurofilaments + H2O
?
show the reaction diagram
-
-
-
-
?
osteocalcin + H2O
?
show the reaction diagram
-
-
-
-
?
osteopontin + H2O
?
show the reaction diagram
-
cathepsin D hydrolyzes the Leu38-Leu39 and Leu151-Arg152 bonds resulting in an osteopontin fragment consisting of residues Leu39-Leu151
-
-
?
Parathyroid hormone + H2O
?
show the reaction diagram
-
-
-
-
?
plasminogen + H2O
?
show the reaction diagram
-
-
-
-
?
porcine hemoglobin + H2O
?
show the reaction diagram
-
-
-
-
?
porcine serum albumin + H2O
?
show the reaction diagram
-
-
-
-
?
pro-caspase-8 + H2O
caspase-8 + ?
show the reaction diagram
-
the generation of an active caspase-8 requires both cathepsin D-mediated proteolysis and homodimerization of caspase-8
-
-
?
prolactin + H2O
?
show the reaction diagram
-
-
-
-
?
prosaposin + H2O
?
show the reaction diagram
-
-
-
-
?
proteoglycans + H2O
?
show the reaction diagram
-
-
-
-
?
R[K-2,4-dinitrophenyl]LRFFLIPK[G-7-amido-4-methylcoumarin] + H2O
R[K-2,4-dinitrophenyl]LRF + FLIPK[G-7-amido-4-methylcoumarin]
show the reaction diagram
-
-
-
-
?
secondary lymphoid-tissue chemokine + H2O
?
show the reaction diagram
-
-
-
-
?
Ser-Pro-Ala-Lys-Phe-(4-nitro)Phe-Arg-Leu + H2O
Ser-Pro-Ala-Lys-Phe + (4-nitro)Phe-Arg-Leu
show the reaction diagram
-
-
-
?
serum amyloid A protein + H2O
?
show the reaction diagram
-
-
-
-
?
SEVKMDAEFR + H2O
SEVKM + DAEFR
show the reaction diagram
-
beta-secretase activity assay: wild-type peptide substrate (10-mer) of the beta-site of the amyloid precursor protein. Cathepsin D shows only poor activity towards the wild-type beta-site sequence
-
-
?
SEVNLDAEFR + H2O
SEVNL + DAEFR
show the reaction diagram
-
beta-secretase activity assay: mutated Swedish family (SW) peptide subtrate (10-mer) with the two mutated residues flanking the beta-site of the amyloid precursor protein
-
-
?
SSLLEKGLDGAKKAVGGLGKLGKDAVEDLESVGKGAVHDVKDVLDSVL + H2O
SSLLEKGLDGAKKAVGGLGKLGKDAVEDL + ESVGKGAVHDVKDVLDSVL
show the reaction diagram
-
DCD-1L, peptide present in human sweat. DCD-1L is cleaved by CatD dominantly between Leu44 and Asp45 yielding SSL-44 and the tetrapeptide DSVL and to a lower amount between Leu29 and Glu30 leading to the peptide SSL-29 and corresponding peptides ESV-19 and ESV-15, respectively. These cleavage sites agree well with the specificity of CatD, which preferably cleaves proteins and peptides with leucine or an aromatic amino acid residue in the P1 position
-
-
?
SSLLEKGLDGAKKAVGGLGKLGKDAVEDLESVGKGAVHDVKDVLDSVL + H2O
SSLLEKGLDGAKKAVGGLGKLGKDAVEDLESVGKGAVHDVKDVL + DSVL
show the reaction diagram
-
DCD-1L, peptide present in human sweat. DCD-1L is cleaved by CatD dominantly between Leu44 and Asp45 yielding SSL-44 and the tetrapeptide DSVL and to a lower amount between Leu29 and Glu30 leading to the peptide SSL-29 and corresponding peptides ESV-19 and ESV-15, respectively. These cleavage sites agree well with the specificity of CatD, which preferably cleaves proteins and peptides with leucine or an aromatic amino acid residue in the P1 position
-
-
?
Tau + H2O
?
show the reaction diagram
-
-
-
-
?
tau protein + H2O
?
show the reaction diagram
-
-
-
-
?
thioredoxin-1 + H2O
?
show the reaction diagram
-
-
-
-
?
thyroglobulin + H2O
?
show the reaction diagram
-
-
-
-
?
transglutaminase 1 + H2O
?
show the reaction diagram
-
-
-
-
?
tropomyosin + H2O
?
show the reaction diagram
-
-
-
-
?
tubulin + H2O
?
show the reaction diagram
-
-
-
-
?
[aminooxy-acetyl-K]LLVVFF[D-PEG2] + H2O
[aminooxy-acetyl-K]LL + VVF + VVFF[D-PEG2] + F[D-PEG2]
show the reaction diagram
-
the proform of cathepsin D cleaves the substrate at pH 6.5 with the same cleavage selectivity obtained with the mature form of the protease
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
alpha-synuclein + H2O
?
show the reaction diagram
-
-
-
?
amyloid precursor protein + H2O
?
show the reaction diagram
-
-
-
-
?
angiostatin + H2O
?
show the reaction diagram
-
-
-
-
?
apolipoprotein E + H2O
?
show the reaction diagram
-
-
-
-
?
endostatin + H2O
?
show the reaction diagram
-
-
-
-
?
Hemoglobin + H2O
?
show the reaction diagram
pro-caspase-8 + H2O
caspase-8 + ?
show the reaction diagram
-
the generation of an active caspase-8 requires both cathepsin D-mediated proteolysis and homodimerization of caspase-8
-
-
?
prolactin + H2O
?
show the reaction diagram
-
-
-
-
?
tau protein + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(3S,4S)-4-(2-[4-[4-amino-3-(4-chlorophenyl)butanoyl]-1-[([1,1'-biphenyl]-4-yl)methyl]piperazin-2-yl]acetamido)-N-butyl-3-hydroxy-5-phenylpentanamide
-
-
(3S,4S)-5-(4-bromobenzyloxy)-3-hydroxy-4-(2-thiophen-2-ylacetylamino)pentanoic acid [(S)-1-((S)-1-carbamoyl-3-methylbutylcarbamoyl)ethyl]amide
-
-
(3S,4S)-5-(4-bromobenzyloxy)-4-(3,3-diphenylpropionylamino)-3-hydroxypentanoic acid [(S)-1-((S)-1-carbamoyl-3-methylbutylcarbamoyl)ethyl]amide
-
-
(3S,4S)-5-(4-bromobenzyloxy)-4-diphenylacetylamino-3-hydroxypentanoic acid [(S)-1-((S)-1-carbamoyl-3-methylbutylcarbamoyl)ethyl]amide
-
-
(3S,4S)-N-butyl-3-hydroxy-5-phenyl-4-[2-(4-[4-[(propan-2-yl)oxy]benzoyl]-1-[(3,4,5-trimethoxyphenyl)methyl]piperazin-2-yl)acetamido]pentanamide
-
-
(4'S)-3-(2-fluoropyridin-4-yl)-7-[5-(prop-1-yn-1-yl)pyridin-3-yl]-5'H-spiro[[1]benzopyrano[2,3-c]pyridine-5,4'-[1,3]oxazol]-2'-amine
-
-
(4'S)-3-(3,6-dihydro-2H-pyran-4-yl)-7-[5-(prop-1-yn-1-yl)pyridin-3-yl]-5'H-spiro[[1]benzopyrano[2,3-c]pyridine-5,4'-[1,3]oxazol]-2'-amine
-
-
(4'S)-3-(3,6-dihydro-2H-pyran-4-yl)-7-[5-[(3-methyloxetan-3-yl)ethynyl]pyridin-3-yl]-5'H-spiro[[1]benzopyrano[2,3-c]pyridine-5,4'-[1,3]oxazol]-2'-amine
-
-
(4'S)-3-(5,6-dihydro-2H-pyran-3-yl)-1-fluoro-7-(2-fluoropyridin-3-yl)-5'H-spiro[[1]benzopyrano[2,3-c]pyridine-5,4'-[1,3]oxazol]-2'-amine
-
-
(4'S)-3-(5,6-dihydro-2H-pyran-3-yl)-7-[5-(prop-1-yn-1-yl)pyridin-3-yl]-5'H-spiro[[1]benzopyrano[2,3-c]pyridine-5,4'-[1,3]oxazol]-2'-amine
-
-
(4'S)-3-chloro-7-(5-fluoropyridin-3-yl)-5'H-spiro[[1]benzopyrano[2,3-c]pyridine-5,4'-[1,3]oxazol]-2'-amine
-
-
(4'S)-3-chloro-7-[5-(prop-1-yn-1-yl)pyridin-3-yl]-5'H-spiro[[1]benzopyrano[2,3-c]pyridine-5,4'-[1,3]oxazol]-2'-amine
-
-
(4'S)-3-methoxy-5'H-spiro[[1]benzopyrano[2,3-c]pyridine-5,4'-[1,3]oxazole]-2',7-diamine
-
-
(4'S)-7-(2-fluoropyridin-3-yl)-3-(2-fluoropyridin-4-yl)-5'H-spiro[[1]benzopyrano[2,3-c]pyridine-5,4'-[1,3]oxazol]-2'-amine
-
-
(4'S)-7-[5-(cyclopropylethynyl)pyridin-3-yl]-3-(3,6-dihydro-2H-pyran-4-yl)-5'H-spiro[[1]benzopyrano[2,3-c]pyridine-5,4'-[1,3]oxazol]-2'-amine
-
-
(5S,8S,11S,12S,16S)-8-(3-amino-3-oxopropyl)-11-benzyl-12-hydroxy-7-methyl-16-(2-methylpropyl)-3,6,9,14-tetraoxo-1-phenyl-5-(propan-2-yl)-2-oxa-4,7,10,15-tetraazaheptadecan-17-oic acid
-
-
(5S,8S,11S,12S,16S,19S)-8-(3-amino-3-oxopropyl)-11-benzyl-12-hydroxy-7,19-dimethyl-16-(2-methylpropyl)-3,6,9,14,17-pentaoxo-1-phenyl-5-(propan-2-yl)-2-oxa-4,7,10,15,18-pentaazaicosan-20-oic acid
-
-
(5S,8S,11S,12S,16S,19S,22R)-8-(3-amino-3-oxopropyl)-11,22-dibenzyl-12-hydroxy-7,19,21-trimethyl-16-(2-methylpropyl)-3,6,9,14,17,20-hexaoxo-1-phenyl-5-(propan-2-yl)-2-oxa-4,7,10,15,18,21-hexaazatricosan-23-oic acid
-
-
(5Z)-5-[4-[(4-benzoyl-3-hydroxy-2-propylphenoxy)methyl]benzylidene]-2-thioxo-1,3-thiazolidin-4-one
-
(6S,9S,12S,13S,17S)-9-(3-amino-3-oxopropyl)-12-benzyl-13-hydroxy-2,2,8-trimethyl-17-(2-methylpropyl)-4,7,10,15-tetraoxo-6-(propan-2-yl)-3-oxa-5,8,11,16-tetraazaoctadecan-18-oic acid
-
-
(6S,9S,12S,13S,17S,20S)-9-(3-amino-3-oxopropyl)-12-benzyl-13-hydroxy-2,2,8,20-tetramethyl-17-(2-methylpropyl)-4,7,10,15,18-pentaoxo-6-(propan-2-yl)-3-oxa-5,8,11,16,19-pentaazahenicosan-21-oic acid
-
-
(6S,9S,12S,13S,17S,20S,23R)-9-(3-amino-3-oxopropyl)-12,23-dibenzyl-13-hydroxy-2,2,8,20,22-pentamethyl-17-(2-methylpropyl)-4,7,10,15,18,21-hexaoxo-6-(propan-2-yl)-3-oxa-5,8,11,16,19,22-hexaazatetracosan-24-oic acid
-
-
(S)-2,3-dihydro-1H-indole-2-carboxylic acid ((1S,2S)-1-(4-bromobenzyloxymethyl)-3-[(S)-1-((S)-1-carbamoyl-3-methylbutylcarbamoyl)ethylcarbamoyl]-2-hydroxypropyl)amide
-
-
1,2-epoxy-3-(4-nitrophenoxy)propane
-
-
2-(3,4-dimethoxyphenyl)-N-[N-(4-methylbenzyl)carbamimidoyl]acetamide
-
2-aminobenzoyl-AFKFFSRQ-N-(2,4-dinitrophenyl)ethylenediamine
-
-
2-aminobenzoyl-AIHFFSRQ-N-(2,4-dinitrophenyl)ethylenediamine
-
-
2-aminobenzoyl-AIKFFHRQ-N-(2,4-dinitrophenyl)ethylenediamine
-
-
2-aminobenzoyl-AIKFFPRQ-N-(2,4-dinitrophenyl)ethylenediamine
-
-
2-aminobenzoyl-AIKFFSFQ-N-(2,4-dinitrophenyl)ethylenediamine
-
-
2-aminobenzoyl-AIKIISRQ-N-(2,4-dinitrophenyl)ethylenediamine
-
-
2-aminobenzoyl-AIKQQSRQ-N-(2,4-dinitrophenyl)ethylenediamine
-
-
2-aminobenzoyl-AIKVVSRQ-N-(2,4-dinitrophenyl)ethylenediamine
-
-
2-bromo-N-[(2S,3S)-4-[[2-(2,4-dichlorophenyl)ethyl][3-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)propanoyl]amino]-3-hydroxy-1-(3-phenoxyphenyl)butan-2-yl]-4,5-dimethoxybenzamide
-
2-mercaptoethanol
-
-
3,5-dichloro-2-[[(3,5-dichloro-2-hydroxyphenyl)sulfonyl]amino]-N-[4-[(6-ethoxy-1,3-benzothiazol-2-yl)sulfanyl]phenyl]benzamide
-
3-cyclohexyl-N-(3,4-difluorobenzyl)-N2-[N-[(3,4-dimethoxyphenyl)acetyl]carbamimidoyl]-D-alaninamide
-
3-cyclohexyl-N-(3,4-dimethoxybenzyl)-N2-[N-[(3,4-dimethoxyphenyl)acetyl]carbamimidoyl]-D-alaninamide
-
3-cyclohexyl-N2-[N-[(3,4-dimethoxyphenyl)acetyl]carbamimidoyl]-N-(3-fluoro-4-methoxybenzyl)-D-alaninamide
-
3-cyclohexyl-N2-[N-[(3,4-dimethoxyphenyl)acetyl]carbamimidoyl]-N-(4-fluoro-3-methoxybenzyl)-D-alaninamide
-
3-cyclohexyl-N2-[N-[(3,4-dimethoxyphenyl)acetyl]carbamimidoyl]-N-[3-(1H-tetrazol-5-yl)benzyl]-D-alaninamide
-
3-cyclohexyl-N2-[N-[(3,4-dimethoxyphenyl)acetyl]carbamimidoyl]-N-[3-fluoro-4-(1H-tetrazol-5-yl)benzyl]-D-alaninamide
-
3-cyclohexyl-N2-[N-[(3,4-dimethoxyphenyl)acetyl]carbamimidoyl]-N-[4-(1H-tetrazol-5-yl)benzyl]-D-alaninamide
-
3-[5-[(4'S)-2'-amino-3-(3,6-dihydro-2H-pyran-4-yl)-5'H-spiro[[1]benzopyrano[2,3-c]pyridine-5,4'-[1,3]oxazol]-7-yl]pyridin-3-yl]prop-2-yn-1-ol
-
-
4-([N-[(benzyloxy)carbonyl]-L-valyl-N2-methyl-L-glutaminyl]amino)-2,4,5-trideoxy-5-phenyl-L-threo-pentonic acid
-
-
4-bromophenylacylbromide
-
-
ascorbic acid
-
-
cathepsin D inhibitor from Streptomyces sp.MBR04
-
reversible, competitive, slow-tight-binding inhibitor
-
Diazoacetyl-DL-norleucine methyl ester
-
-
Diazoacetylglycine ethyl ester
-
-
dithiothreitol
-
10 mM, 90% inhibition
EDTA
-
no significantly influenced
equistatin
-
-
-
ethanol
-
high-proof alcoholic beverages
ethyl 6-(2-[[(2S,3S)-5-(butylamino)-3-hydroxy-5-oxo-1-phenylpentan-2-yl]carbamoyl]-4-[3-(3,4,5-trimethoxyphenyl)propanoyl]piperazin-1-yl)-6-oxohexanoate
-
-
Fe2+
-
-
Fe3+
-
FeCl3
inhibitor isolated from potato
-
-
-
inhibitor isolated from potatoes
-
-
-
inhibitor isolated from tomato
-
recombinant protein, GenBank accession no. AJ289776
-
L-Cys
-
-
methyl (2S)-1-[(2R,5S,8S,12S,13S)-2,13-dibenzyl-12-hydroxy-15-(3-[(methanesulfonyl)(methyl)amino]-5-[[(1R)-1-phenylethyl]carbamoyl]phenyl)-3,5-dimethyl-8-(2-methylpropyl)-4,7,10,15-tetraoxo-3,6,9,14-tetraazapentadecanan-1-oyl]pyrrolidine-2-carboxylate
-
-
methyl (5S,8S,11S,12S,16S)-8-(3-amino-3-oxopropyl)-11-benzyl-12-hydroxy-7-methyl-16-(2-methylpropyl)-3,6,9,14-tetraoxo-1-phenyl-5-(propan-2-yl)-2-oxa-4,7,10,15-tetraazaheptadecan-17-oate
-
-
methyl (5S,8S,11S,12S,16S,19S)-8-(3-amino-3-oxopropyl)-11-benzyl-12-hydroxy-7,19-dimethyl-16-(2-methylpropyl)-3,6,9,14,17-pentaoxo-1-phenyl-5-(propan-2-yl)-2-oxa-4,7,10,15,18-pentaazaicosan-20-oate
-
-
methyl (5S,8S,11S,12S,16S,19S,22R)-8-(3-amino-3-oxopropyl)-11,22-dibenzyl-12-hydroxy-7,19,21-trimethyl-16-(2-methylpropyl)-3,6,9,14,17,20-hexaoxo-1-phenyl-5-(propan-2-yl)-2-oxa-4,7,10,15,18,21-hexaazatricosan-23-oate
-
-
methyl (6S,9S,12S,13S,17S)-9-(3-amino-3-oxopropyl)-12-benzyl-13-hydroxy-2,2,8-trimethyl-17-(2-methylpropyl)-4,7,10,15-tetraoxo-6-(propan-2-yl)-3-oxa-5,8,11,16-tetraazaoctadecan-18-oate
-
-
methyl (6S,9S,12S,13S,17S,20S)-9-(3-amino-3-oxopropyl)-12-benzyl-13-hydroxy-2,2,8,20-tetramethyl-17-(2-methylpropyl)-4,7,10,15,18-pentaoxo-6-(propan-2-yl)-3-oxa-5,8,11,16,19-pentaazahenicosan-21-oate
-
-
methyl (6S,9S,12S,13S,17S,20S,23R)-9-(3-amino-3-oxopropyl)-12,23-dibenzyl-13-hydroxy-2,2,8,20,22-pentamethyl-17-(2-methylpropyl)-4,7,10,15,18,21-hexaoxo-6-(propan-2-yl)-3-oxa-5,8,11,16,19,22-hexaazatetracosan-24-oate
-
-
N-((1S,2S)-1-(4-benzo[1,3]dioxol-5-yl-benzyloxymethyl)-3-[(S)-1-((S)-1-carbamoyl-3-methyl-butylcarbamoyl)-ethylcarbamoyl]-2-hydroxy-propyl)-2,4,6-trifluorobenzamide
-
-
N-((1S,2S)-1-(4-bromobenzyloxymethyl)-3-[(S)-1-((S)-1-carbamoyl-3-methylbutylcarbamoyl)ethylcarbamoyl]-2-hydroxypropyl)-3,4-dichlorobenzamide
-
-
N-((1S,2S)-1-(biphenyl-4-ylmethoxymethyl)-3-[(S)-1-((S)-1-carbamoyl-3-methyl-butylcarbamoyl)-ethylcarbamoyl]-2-hydroxy-propyl)-2,4,6-trifluorobenzamide
-
-
N-(3,4-dimethoxybenzyl)-N2-[N-[(3,4-dimethoxyphenyl)acetyl]carbamimidoyl]-D-leucinamide
-
N-(3,4-dimethoxybenzyl)-Na-[N-[(3,4-dimethoxyphenyl)acetyl]carbamimidoyl]-D-phenylalaninamide
-
N-(N-benzylcarbamimidoyl)-2-(2-chloro-5-methoxyphenyl)acetamide
-
N-(N-benzylcarbamimidoyl)-2-(4,5-dimethoxy-2-nitrophenyl)acetamide
-
N-(N-benzylcarbamimidoyl)-3-(3,4-dimethoxyphenyl)propanamide
-
N-(N-benzylcarbamimidoyl)-4-(4,5-dimethoxy-2-nitrophenyl)butanamide
-
N-[(1S,2S)-1-(biphenyl-4-ylmethoxymethyl)-3-cyclo-hexylcarbamoyl-2-hydroxypropyl]-2,4,6-trifluorobenzamide
-
-
N-[(1S,2S)-3-cyclohexylcarbamoyl-2-hydroxy-1-(4-thiophen-3-yl-benzyloxymethyl)-propyl]-2,4,6-trifluorobenzamide
-
-
N-[(1S,2S)-3-[(S)-1-((S)-1-carbamoyl-3-methyl-butyl-carbamoyl)-ethylcarbamoyl]-2-hydroxy-1-(4-thiophen-3-yl-benzyloxymethyl)-propyl]-2,4,6-trifluorobenzamide
-
-
N-[(2S,3S)-5-(butylamino)-3-hydroxy-5-oxo-1-phenylpentan-2-yl]-1-[2-(2-phenylethoxy)ethyl]-4-[3-(3,4,5-trimethoxyphenyl)propanoyl]piperazine-2-carboxamide
-
-
N-[(4'S)-2'-amino-3-(3,6-dihydro-2H-pyran-4-yl)-5'H-spiro[[1]benzopyrano[2,3-c]pyridine-5,4'-[1,3]oxazol]-7-yl]-5-chloropyridine-2-carboxamide
-
-
N-[(4'S)-2'-amino-3-(5,6-dihydro-2H-pyran-3-yl)-5'H-spiro[[1]benzopyrano[2,3-c]pyridine-5,4'-[1,3]oxazol]-7-yl]-5-chloropyridine-2-carboxamide
-
-
N-[(4'S)-2'-amino-3-chloro-5'H-spiro[[1]benzopyrano[2,3-c]pyridine-5,4'-[1,3]oxazol]-7-yl]-5-chloropyridine-2-carboxamide
-
-
N-[(4'S)-2'-amino-3-cyclopropyl-5'H-spiro[[1]benzopyrano[2,3-c]pyridine-5,4'-[1,3]oxazol]-7-yl]-5-chloropyridine-2-carboxamide
-
-
N-[(4'S)-2'-amino-3-methoxy-5'H-spiro[[1]benzopyrano[2,3-c]pyridine-5,4'-[1,3]oxazol]-7-yl]-5-chloropyridine-2-carboxamide
-
-
N-[(4'S)-2'-amino-3-methyl-5'H-spiro[[1]benzopyrano[2,3-c]pyridine-5,4'-[1,3]oxazol]-7-yl]-5-chloropyridine-2-carboxamide
-
-
N-[N-(2-chlorobenzyl)carbamimidoyl]-2-(4,5-dimethoxy-2-nitrophenyl)acetamide
-
N-[N-(3,4-dichlorobenzyl)carbamimidoyl]-2-(4,5-dimethoxy-2-nitrophenyl)acetamide
-
N-[N-(3,4-dimethoxybenzyl)carbamimidoyl]-2-(4,5-dimethoxy-2-nitrophenyl)acetamide
-
N-[N-(4-aminobenzyl)carbamimidoyl]-2-(3,4-dimethoxyphenyl)acetamide
-
N-[N-(4-chlorobenzyl)carbamimidoyl]-2-(4,5-dimethoxy-2-nitrophenyl)acetamide
-
N1-[(2S,3S)-3-hydroxy-5-([(2S)-4-methyl-1-[(2-methylpropyl)amino]-1-oxopentan-2-yl]amino)-5-oxo-1-phenylpentan-2-yl]-5-[(methanesulfonyl)(methyl)amino]-N3-[(1R)-1-phenylethyl]benzene-1,3-dicarboxamide
-
-
N1-[(2S,3S)-3-hydroxy-5-[[(2S)-1-[[(3-methoxyphenyl)methyl]amino]-4-methyl-1-oxopentan-2-yl]amino]-5-oxo-1-phenylpentan-2-yl]-5-[(methanesulfonyl)(methyl)amino]-N3-[(1R)-1-phenylethyl]benzene-1,3-dicarboxamide
-
-
N1-[(2S,3S)-5-[[(2S)-1-(cyclopropylamino)-4-methyl-1-oxopentan-2-yl]amino]-3-hydroxy-5-oxo-1-phenylpentan-2-yl]-5-[(methanesulfonyl)(methyl)amino]-N3-[(1R)-1-phenylethyl]benzene-1,3-dicarboxamide
-
-
N2-[N-[(2-bromo-4,5-dimethoxyphenyl)acetyl]carbamimidoyl]-3-cyclohexyl-N-(4-fluoro-3-methoxybenzyl)-D-alaninamide
-
N2-[N-[(2-bromo-4,5-dimethoxyphenyl)acetyl]carbamimidoyl]-3-cyclohexyl-N-[3-(1H-tetrazol-5-yl)benzyl]-D-alaninamide
-
N2-[N-[(2-bromo-4,5-dimethoxyphenyl)acetyl]carbamimidoyl]-N-[3-(1H-tetrazol-5-yl)benzyl]-D-leucinamide
-
N2-[N-[(3,4-dimethoxyphenyl)acetyl]carbamimidoyl]-N-(4-fluoro-3-methoxybenzyl)-D-leucinamide
-
N2-[N-[(3,4-dimethoxyphenyl)acetyl]carbamimidoyl]-N-[2-fluoro-3-(1H-tetrazol-5-yl)benzyl]-D-leucinamide
-
N2-[N-[(3,4-dimethoxyphenyl)acetyl]carbamimidoyl]-N-[3-(1H-tetrazol-5-yl)benzyl]-D-leucinamide
-
N2-[N-[(3,4-dimethoxyphenyl)acetyl]carbamimidoyl]-N-[3-fluoro-4-(1H-tetrazol-5-yl)benzyl]-D-leucinamide
-
N2-[N-[(3,4-dimethoxyphenyl)acetyl]carbamimidoyl]-N-[4-(1H-tetrazol-5-yl)benzyl]-D-leucinamide
-
Na-[N-[(3,4-dimethoxyphenyl)acetyl]carbamimidoyl]-N-[2-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)ethyl]-D-phenylalaninamide
-
Na-[N-[(3,4-dimethoxyphenyl)acetyl]carbamimidoyl]-N-[2-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)ethyl]-L-phenylalaninamide
-
PCMB
-
-
pepstatin
pepstatin A
pyridine-2-carboxylic acid ((R)-1-((1S,2S)-1-(4-bromobenzyloxymethyl)-3-[(S)-1-((S)-1-carbamoyl-3-methyl-butylcarbamoyl)ethylcarbamoyl]-2-hydroxypropylcarbamoyl)-2-methylpropyl)amide
-
-
pyridine-2-carboxylic acid ((S)-1-((1S,2S)-1-(3-bromobenzyloxymethyl)-3-[(S)-1-((S)-1-carbamoyl-3-methylbutylcarbamoyl)-ethylcarbamoyl]-2-hydroxypropylcarbamoyl)-2-methyl-propyl)-amide
-
-
pyridine-2-carboxylic acid ((S)-1-((1S,2S)-1-(4-benzo-[1,3]dioxol-5-yl-benzyloxymethyl)-3-[(S)-1-((S)-1-carbamoyl-3-methyl-butylcarbamoyl)-ethylcarbamoyl]-2-hydroxypropylcarbamoyl)-2-methylpropyl)-amide
-
-
pyridine-2-carboxylic acid ((S)-1-((1S,2S)-1-(4-bromobenzyloxymethyl)-2-hydroxy-3-(2-(3-methoxyphenyl)ethylcarbamoyl)propylcarbamoyl)-2-methylpropyl)amide
-
-
pyridine-2-carboxylic acid ((S)-1-((1S,2S)-1-(4-bromobenzyloxymethyl)-3-[(S)-1-((S)-1-carbamoyl-3-methyl-butylcarbamoyl)ethylcarbamoyl]-2-hydroxypropylcarbamoyl)-2-methylpropyl)amide
-
-
pyridine-2-carboxylic acid ((S)-1-((1S,2S)-1-(biphenyl-3-ylmethoxymethyl)-3-[(S)-1-((S)-1-carbamoyl-3-methyl-butylcarbamoyl)-ethylcarbamoyl]-2-hydroxy-propylcar-bamoyl)-2-methyl-propyl)-amide
-
-
pyridine-2-carboxylic acid ((S)-1-((1S,2S)-1-(biphenyl-4-ylmethoxymethyl)-3-[(S)-1-((S)-1-carbamoyl-3-methyl-butylcarbamoyl)-ethylcarbamoyl]-2-hydroxy-propylcarbamoyl)-2-methyl-propyl)-amide
-
-
pyridine-2-carboxylic acid ((S)-1-((1S,2S)-1-benzyloxymethyl-3-[(S)-1-((S)-1-carbamoyl-3-methylbutylcarbamoyl)ethylcarbamoyl]-2-hydroxypropylcarbamoyl)-2-methylpropyl)amide
-
-
pyridine-2-carboxylic acid ((S)-1-((1S,2S)-3-((S)-1-((S)-1-carbamoyl-3-methylbutylcarbamoyl)ethylcarbamoyl)-2-hydroxy-1-phenethylpropylcarbamoyl)-2-methylpropyl)amide
-
-
pyridine-2-carboxylic acid ((S)-1-[(1S,2S)-1-(4-benzo-[1,3]dioxol-5-yl-benzyloxymethyl)-3-butylcarbamoyl-2-hydroxy-propylcarbamoyl]-2-methyl-propyl)-amide
-
-
pyridine-2-carboxylic acid ((S)-1-[(1S,2S)-1-(4-bromobenzyloxymethyl)-2-hydroxy-3-(2-phenylaminoethyl-carbamoyl)propylcarbamoyl]-2-methylpropyl)amide
-
-
pyridine-2-carboxylic acid ((S)-1-[(1S,2S)-1-(4-bromobenzyloxymethyl)-2-hydroxy-3-(3-phenylpropylcarbamoyl)propylcarbamoyl]-2-methylpropyl)amide
-
-
pyridine-2-carboxylic acid ((S)-1-[(1S,2S)-1-(4-bromobenzyloxymethyl)-3-(4-cyanobenzylcarbamoyl)-2-hydroxypropylcarbamoyl]-2-methylpropyl)amide
-
-
pyridine-2-carboxylic acid ((S)-1-[(1S,2S)-1-(4-bromobenzyloxymethyl)-3-(cyclohexylmethylcarbamoyl)-2-hydroxypropylcarbamoyl]-2-methylpropyl)amide
-
-
pyridine-2-carboxylic acid ((S)-1-[(1S,2S)-1-(4-bromobenzyloxymethyl)-3-butylcarbamoyl-2-hydroxypropylcarbamoyl]-2-methylpropyl)amide
-
-
pyridine-2-carboxylic acid ((S)-1-[(1S,2S)-1-(4-bromobenzyloxymethyl)-3-cyclohexylcarbamoyl-2-hydroxypropylcarbamoyl]-2-methylpropyl)amide
-
-
pyridine-2-carboxylic acid ((S)-1-[(1S,2S)-1-(biphenyl-4-ylmethoxymethyl)-3-butylcarbamoyl-2-hydroxy-propylcarbamoyl]-2-methylpropyl)-amide
-
-
pyridine-2-carboxylic acid ((S)-1-[(1S,2S)-3-butylcarbamoyl-2-hydroxy-1-(4-thiophen-3-yl-benzyloxymethyl)-propylcarbamoyl]-2-methyl-propyl)-amide
-
-
pyridine-2-carboxylic acid ((S)-1-[(1S,2S)-3-[(S)-1-((S)-1-carbamoyl-3-methyl-butylcarbamoyl)-ethylcarbamoyl]-2-hydroxy-1-(4-thiophen-3-yl-benzyloxymethyl)-propyl-carbamoyl]-2-methyl-propyl)-amide
-
-
pyridine-2-carboxylic acid ((S)-1-[(1S,2S)-3-[(S)-1-((S)-1-carbamoyl-3-methylbutylcarbamoyl)-ethylcarbamoyl]-2-hydroxy-1-(3-thiophen-3-yl-benzyloxymethyl)-propylcarbamoyl]-2-methylpropyl)-amide
-
-
pyridine-2-carboxylic acid((S)-1-[(1S,2S)-3-[(S)-1-((S)-1-carbamoyl-3-methyl-butylcarbamoyl)-ethylcarbamoyl]-2-hydroxy-1-(4-thiophen-3-yl-benzyloxymethyl)-propyl-carbamoyl]-2-methyl-propyl)-amide
-
-
tasiamide B
-
-
TB-11
-
-
TB-13
-
-
Tb-9
-
-
Urea
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
multi-granulin domain peptide
-
-
-
progranulin
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00045
2-aminobenzoyl-AAKFFSRQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
0.00031
2-aminobenzoyl-AEKFFSRQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
0.00027
2-aminobenzoyl-AIAFFSRQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
0.00017
2-aminobenzoyl-AIEFFSRQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
0.00007
2-aminobenzoyl-AIFFFSRQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
0.00005
2-aminobenzoyl-AIIFFSRQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
0.00028
2-aminobenzoyl-AIKFFARQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
0.00034
2-aminobenzoyl-AIKFFERQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
0.00021
2-aminobenzoyl-AIKFFIRQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
0.0003
2-aminobenzoyl-AIKFFKRQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
0.0001
2-aminobenzoyl-AIKFFLRQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
0.00009
2-aminobenzoyl-AIKFFNRQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
0.00009
2-aminobenzoyl-AIKFFORQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
0.00034
2-aminobenzoyl-AIKFFRRQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
0.00037
2-aminobenzoyl-AIKFFSA-(N-(2,4-dinitrophenyl)ethylenediamine)
-
37°C, pH 4.0
-
0.00046
2-aminobenzoyl-AIKFFSAQ-N-(2,4-dinitrophenyl)ethylenediamine
0.0008
2-aminobenzoyl-AIKFFSAQTNR-(N-(2,4-dinitrophenyl)ethylenediamine)
-
37°C, pH 4.0
-
0.00008
2-aminobenzoyl-AIKFFSAQTNRHILRFNR-(N-(2,4-dinitrophenyl)ethylenediamine)
-
37°C, pH 4.0
-
0.0008
2-aminobenzoyl-AIKFFSAQTNRHILRFNRQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
0.0008
2-aminobenzoyl-AIKFFSAQTNRQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
0.00066
2-aminobenzoyl-AIKFFSEQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
0.00007
2-aminobenzoyl-AIKFFSIQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
0.00055
2-aminobenzoyl-AIKFFSKQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
0.00011
2-aminobenzoyl-AIKFFSLQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
0.0005
2-aminobenzoyl-AIKFFSNQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
0.00066
2-aminobenzoyl-AIKFFSOQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
0.00057
2-aminobenzoyl-AIKFFSPQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
0.0012
2-aminobenzoyl-AIKFFSRQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
0.00021
2-aminobenzoyl-AIKFFSSQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
0.00043
2-aminobenzoyl-AIKFFSTQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
0.0001
2-aminobenzoyl-AIKFFSVQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
0.00023
2-aminobenzoyl-AIKFFTRQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
0.00007
2-aminobenzoyl-AIKFFVRQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
0.00031
2-aminobenzoyl-AIKFMSRQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
0.00041
2-aminobenzoyl-AIKLFSRQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
0.00028
2-aminobenzoyl-AIKLLSRQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
0.00017
2-aminobenzoyl-AIKLMSRQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
0.00016
2-aminobenzoyl-AIKMFLRQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
0.001
2-aminobenzoyl-AIKMFSRQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
0.00076
2-aminobenzoyl-AIKMMSRQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
0.00009
2-aminobenzoyl-AIKYYSRQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
0.00019
2-aminobenzoyl-AILFFSRQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
0.00037
2-aminobenzoyl-AIMFFSRQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
0.00081
2-aminobenzoyl-AINFFSRQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
0.00085
2-aminobenzoyl-AIPFFSRQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
0.00043
2-aminobenzoyl-AIQFFSRQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
0.00032
2-aminobenzoyl-AISFFSRQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
0.00086
2-aminobenzoyl-AITFFSRQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
0.00017
2-aminobenzoyl-AIVFFSRQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
0.00016
2-aminobenzoyl-AKKFFSRQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
0.00054
2-aminobenzoyl-ALKFFSRQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
0.00076
2-aminobenzoyl-ANKFFSRQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
0.00052
2-aminobenzoyl-APKFFSRQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
0.00082
2-aminobenzoyl-AQKFFSRQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
0.00096
2-aminobenzoyl-ASKFFSRQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
0.0007
2-aminobenzoyl-ATKFFSRQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
0.00039
2-aminobenzoyl-AVKFFSRQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
0.00016
2-aminobenzoyl-KITLLSALVETRIVRFNRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
37°C, pH 4.0
0.00074
2-aminobenzoyl-KITLLSALVETRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
37°C, pH 4.0
0.00051 - 0.00094
2-aminobenzoyl-KITLLSAQ-(N-(2,4-dinitrophenyl)ethylenediamine)
1.1
EEISEVNLDAEFRG
-
-
0.0015
fibrinogen
-
-
-
1.6
Glu-Glu-His-Phe-Phe-Ala-Ala
-
-
1.1
Glu-Glu-His-Phe-Phe-Ala-Leu-methyl ester
-
-
0.1933
LLVVFF
-
at pH 3.7 and 37°C
0.394
LLVVYPWTQRFF
-
at pH 3.7 and 37°C
0.036 - 0.05
Lys-Pro-Ile-Glu-Phe-(4-nitro)Phe-Arg-Leu
0.0211
R[K-2,4-dinitrophenyl]LRFFLIPK[G-7-amido-4-methylcoumarin]
-
at pH 3.7 and 37°C
1.67
SEVNLDAEFR
-
-
0.0741
[aminooxy-acetyl-K]LLVVFF[D-PEG2]
-
at pH 3.7 and 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.6
2-aminobenzoyl-AAKFFSRQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
6.18
2-aminobenzoyl-AEKFFSRQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
16.3
2-aminobenzoyl-AIAFFSRQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
0.03 - 7.48
2-aminobenzoyl-AIEFFSRQ-N-(2,4-dinitrophenyl)ethylenediamine
0.47
2-aminobenzoyl-AIIFFSRQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
3.9
2-aminobenzoyl-AIKFFARQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
2.28 - 2.94
2-aminobenzoyl-AIKFFERQ-N-(2,4-dinitrophenyl)ethylenediamine
0.65
2-aminobenzoyl-AIKFFIRQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
0.65
2-aminobenzoyl-AIKFFKRQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
1.63 - 2.94
2-aminobenzoyl-AIKFFLRQ-N-(2,4-dinitrophenyl)ethylenediamine
0.98 - 6.08
2-aminobenzoyl-AIKFFNRQ-N-(2,4-dinitrophenyl)ethylenediamine
1.3
2-aminobenzoyl-AIKFFORQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
1.95
2-aminobenzoyl-AIKFFRRQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
3.13 - 4.16
2-aminobenzoyl-AIKFFSA-(N-(2,4-dinitrophenyl)ethylenediamine)
-
6.18 - 6.34
2-aminobenzoyl-AIKFFSAQ-N-(2,4-dinitrophenyl)ethylenediamine
0.99 - 2.94
2-aminobenzoyl-AIKFFSAQTNRHILRFNR-(N-(2,4-dinitrophenyl)ethylenediamine)
-
2.44 - 2.94
2-aminobenzoyl-AIKFFSAQTNRHILRFNRQ-N-(2,4-dinitrophenyl)ethylenediamine
0.99
2-aminobenzoyl-AIKFFSAQTNRQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
3.13 - 3.58
2-aminobenzoyl-AIKFFSEQ-N-(2,4-dinitrophenyl)ethylenediamine
1.63 - 2.94
2-aminobenzoyl-AIKFFSIQ-N-(2,4-dinitrophenyl)ethylenediamine
1.3
2-aminobenzoyl-AIKFFSKQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
2.6
2-aminobenzoyl-AIKFFSLQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
3.25
2-aminobenzoyl-AIKFFSNQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
3.3 - 4.88
2-aminobenzoyl-AIKFFSOQ-N-(2,4-dinitrophenyl)ethylenediamine
1.3
2-aminobenzoyl-AIKFFSPQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
3.3 - 4.88
2-aminobenzoyl-AIKFFSRQ-N-(2,4-dinitrophenyl)ethylenediamine
0.98 - 6.08
2-aminobenzoyl-AIKFFSSQ-N-(2,4-dinitrophenyl)ethylenediamine
2.6
2-aminobenzoyl-AIKFFSTQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
2.28 - 2.94
2-aminobenzoyl-AIKFFSVQ-N-(2,4-dinitrophenyl)ethylenediamine
1.63 - 2.94
2-aminobenzoyl-AIKFFTRQ-N-(2,4-dinitrophenyl)ethylenediamine
1.63 - 2.94
2-aminobenzoyl-AIKFFVRQ-N-(2,4-dinitrophenyl)ethylenediamine
1.3
2-aminobenzoyl-AIKFMSRQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
0.03 - 7.15
2-aminobenzoyl-AIKLFSRQ-N-(2,4-dinitrophenyl)ethylenediamine
0.98 - 6.08
2-aminobenzoyl-AIKLLSRQ-N-(2,4-dinitrophenyl)ethylenediamine
2.28 - 2.94
2-aminobenzoyl-AIKLMSRQ-N-(2,4-dinitrophenyl)ethylenediamine
1.3
2-aminobenzoyl-AIKMFLRQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
0.52
2-aminobenzoyl-AIKMFSRQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
1.3
2-aminobenzoyl-AIKMMSRQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
2.6
2-aminobenzoyl-AIKYYSRQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
7.8
2-aminobenzoyl-AILFFSRQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
2.47 - 2.94
2-aminobenzoyl-AIMFFSRQ-N-(2,4-dinitrophenyl)ethylenediamine
8.45
2-aminobenzoyl-AINFFSRQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
0.081
2-aminobenzoyl-AIPFFSRQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
0.41
2-aminobenzoyl-AIQFFSRQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
0.04 - 8.78
2-aminobenzoyl-AISFFSRQ-N-(2,4-dinitrophenyl)ethylenediamine
5.53
2-aminobenzoyl-AITFFSRQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
0.84 - 6.08
2-aminobenzoyl-AIVFFSRQ-N-(2,4-dinitrophenyl)ethylenediamine
1.3
2-aminobenzoyl-AKKFFSRQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
0.97
2-aminobenzoyl-ALKFFSRQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
5.85
2-aminobenzoyl-ANKFFSRQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
2.93 - 6
2-aminobenzoyl-APKFFSRQ-N-(2,4-dinitrophenyl)ethylenediamine
2.28 - 2.94
2-aminobenzoyl-AQKFFSRQ-N-(2,4-dinitrophenyl)ethylenediamine
0.65
2-aminobenzoyl-ASKFFSRQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
3.13 - 3.58
2-aminobenzoyl-ATKFFSRQ-N-(2,4-dinitrophenyl)ethylenediamine
0.04 - 8.78
2-aminobenzoyl-AVKFFSRQ-N-(2,4-dinitrophenyl)ethylenediamine
0.17
2-aminobenzoyl-KITLLSALVETRIVRFNRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
37°C, pH 4.0
2.8
2-aminobenzoyl-KITLLSALVETRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
37°C, pH 4.0
2.3 - 3.6
2-aminobenzoyl-KITLLSAQ-(N-(2,4-dinitrophenyl)ethylenediamine)
31.4
EEISEVNLDAEFRG
-
-
0.0014
fibrinogen
-
-
-
0.4
Glu-Glu-His-Phe-Phe-Ala-Ala
-
-
2.1
Glu-Glu-His-Phe-Phe-Ala-Leu-methyl ester
-
-
8.8
SEVNLDAEFR
-
-
additional information
2-aminobenzoyl-AEKFFSRQ-N-(2,4-dinitrophenyl)ethylenediamine
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.035
(3S,4S)-5-(4-bromobenzyloxy)-3-hydroxy-4-(2-thiophen-2-ylacetylamino)pentanoic acid [(S)-1-((S)-1-carbamoyl-3-methylbutylcarbamoyl)ethyl]amide
-
-
0.1
(3S,4S)-5-(4-bromobenzyloxy)-4-(3,3-diphenylpropionylamino)-3-hydroxypentanoic acid [(S)-1-((S)-1-carbamoyl-3-methylbutylcarbamoyl)ethyl]amide
-
-
0.052
(3S,4S)-5-(4-bromobenzyloxy)-4-diphenylacetylamino-3-hydroxypentanoic acid [(S)-1-((S)-1-carbamoyl-3-methylbutylcarbamoyl)ethyl]amide
-
-
0.322
(S)-2,3-dihydro-1H-indole-2-carboxylic acid ((1S,2S)-1-(4-bromobenzyloxymethyl)-3-[(S)-1-((S)-1-carbamoyl-3-methylbutylcarbamoyl)ethylcarbamoyl]-2-hydroxypropyl)amide
-
-
0.00038
2-aminobenzoyl-AFKFFSRQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
0.00015
2-aminobenzoyl-AIHFFSRQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
0.000054
2-aminobenzoyl-AIKFFHRQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
0.000068
2-aminobenzoyl-AIKFFPRQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
0.000093
2-aminobenzoyl-AIKFFSFQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
0.00019
2-aminobenzoyl-AIKIISRQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
0.000058
2-aminobenzoyl-AIKQQSRQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
0.00036
2-aminobenzoyl-AIKVVSRQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 4.0, 37°C
0.0000032
cathepsin D inhibitor from Streptomyces sp.MBR04
-
in 0.02M sodium citrate, pH 3.0, at 37°C
-
0.00003
inhibitor isolated from potato
-
37°C, pH 3.1
-
0.00058
inhibitor isolated from tomato
-
37°C, pH 3.1
-
0.002701
N-((1S,2S)-1-(4-benzo[1,3]dioxol-5-yl-benzyloxymethyl)-3-[(S)-1-((S)-1-carbamoyl-3-methyl-butylcarbamoyl)-ethylcarbamoyl]-2-hydroxy-propyl)-2,4,6-trifluorobenzamide
-
-
1.807
N-((1S,2S)-1-(4-bromobenzyloxymethyl)-3-[(S)-1-((S)-1-carbamoyl-3-methylbutylcarbamoyl)ethylcarbamoyl]-2-hydroxypropyl)-3,4-dichlorobenzamide
-
-
0.00173
N-((1S,2S)-1-(biphenyl-4-ylmethoxymethyl)-3-[(S)-1-((S)-1-carbamoyl-3-methyl-butylcarbamoyl)-ethylcarbamoyl]-2-hydroxy-propyl)-2,4,6-trifluorobenzamide
-
-
0.0036
N-[(1S,2S)-1-(biphenyl-4-ylmethoxymethyl)-3-cyclo-hexylcarbamoyl-2-hydroxypropyl]-2,4,6-trifluorobenzamide
-
-
0.00494
N-[(1S,2S)-3-cyclohexylcarbamoyl-2-hydroxy-1-(4-thiophen-3-yl-benzyloxymethyl)-propyl]-2,4,6-trifluorobenzamide
-
-
0.00144
N-[(1S,2S)-3-[(S)-1-((S)-1-carbamoyl-3-methyl-butyl-carbamoyl)-ethylcarbamoyl]-2-hydroxy-1-(4-thiophen-3-yl-benzyloxymethyl)-propyl]-2,4,6-trifluorobenzamide
-
-
0.041
pyridine-2-carboxylic acid ((R)-1-((1S,2S)-1-(4-bromobenzyloxymethyl)-3-[(S)-1-((S)-1-carbamoyl-3-methyl-butylcarbamoyl)ethylcarbamoyl]-2-hydroxypropylcarbamoyl)-2-methylpropyl)amide
-
-
0.000032
pyridine-2-carboxylic acid ((S)-1-((1S,2S)-1-(3-bromobenzyloxymethyl)-3-[(S)-1-((S)-1-carbamoyl-3-methylbutylcarbamoyl)-ethylcarbamoyl]-2-hydroxypropylcarbamoyl)-2-methyl-propyl)-amide
-
-
0.0000007
pyridine-2-carboxylic acid ((S)-1-((1S,2S)-1-(4-benzo-[1,3]dioxol-5-yl-benzyloxymethyl)-3-[(S)-1-((S)-1-carbamoyl-3-methyl-butylcarbamoyl)-ethylcarbamoyl]-2-hydroxypropylcarbamoyl)-2-methylpropyl)-amide
-
-
0.14
pyridine-2-carboxylic acid ((S)-1-((1S,2S)-1-(4-bromobenzyloxymethyl)-2-hydroxy-3-(2-(3-methoxyphenyl)ethylcarbamoyl)propylcarbamoyl)-2-methylpropyl)amide
-
-
0.049
pyridine-2-carboxylic acid ((S)-1-((1S,2S)-1-(4-bromobenzyloxymethyl)-3-[(S)-1-((S)-1-carbamoyl-3-methyl-butylcarbamoyl)ethylcarbamoyl]-2-hydroxypropylcarbamoyl)-2-methylpropyl)amide
-
-
0.0000039
pyridine-2-carboxylic acid ((S)-1-((1S,2S)-1-(biphenyl-3-ylmethoxymethyl)-3-[(S)-1-((S)-1-carbamoyl-3-methyl-butylcarbamoyl)-ethylcarbamoyl]-2-hydroxy-propylcar-bamoyl)-2-methyl-propyl)-amide
-
-
0.0000025
pyridine-2-carboxylic acid ((S)-1-((1S,2S)-1-(biphenyl-4-ylmethoxymethyl)-3-[(S)-1-((S)-1-carbamoyl-3-methyl-butylcarbamoyl)-ethylcarbamoyl]-2-hydroxy-propylcarbamoyl)-2-methyl-propyl)-amide
-
-
0.041
pyridine-2-carboxylic acid ((S)-1-((1S,2S)-1-benzyloxymethyl-3-[(S)-1-((S)-1-carbamoyl-3-methylbutylcarbamoyl)ethylcarbamoyl]-2-hydroxypropylcarbamoyl)-2-methylpropyl)amide
-
-
0.98
pyridine-2-carboxylic acid ((S)-1-((1S,2S)-3-((S)-1-((S)-1-carbamoyl-3-methylbutylcarbamoyl)ethylcarbamoyl)-2-hydroxy-1-phenethylpropylcarbamoyl)-2-methylpropyl)amide
-
-
0.000045
pyridine-2-carboxylic acid ((S)-1-[(1S,2S)-1-(4-benzo-[1,3]dioxol-5-yl-benzyloxymethyl)-3-butylcarbamoyl-2-hydroxy-propylcarbamoyl]-2-methyl-propyl)-amide
-
-
0.265
pyridine-2-carboxylic acid ((S)-1-[(1S,2S)-1-(4-bromobenzyloxymethyl)-2-hydroxy-3-(2-phenylaminoethyl-carbamoyl)propylcarbamoyl]-2-methylpropyl)amide
-
-
0.459
pyridine-2-carboxylic acid ((S)-1-[(1S,2S)-1-(4-bromobenzyloxymethyl)-2-hydroxy-3-(3-phenylpropylcarbamoyl)propylcarbamoyl]-2-methylpropyl)amide
-
-
0.623
pyridine-2-carboxylic acid ((S)-1-[(1S,2S)-1-(4-bromobenzyloxymethyl)-3-(4-cyanobenzylcarbamoyl)-2-hydroxypropylcarbamoyl]-2-methylpropyl)amide
-
-
0.586
pyridine-2-carboxylic acid ((S)-1-[(1S,2S)-1-(4-bromobenzyloxymethyl)-3-(cyclohexylmethylcarbamoyl)-2-hydroxypropylcarbamoyl]-2-methylpropyl)amide
-
-
0.473
pyridine-2-carboxylic acid ((S)-1-[(1S,2S)-1-(4-bromobenzyloxymethyl)-3-butylcarbamoyl-2-hydroxypropylcarbamoyl]-2-methylpropyl)amide
-
-
0.217
pyridine-2-carboxylic acid ((S)-1-[(1S,2S)-1-(4-bromobenzyloxymethyl)-3-cyclohexylcarbamoyl-2-hydroxypropylcarbamoyl]-2-methylpropyl)amide
-
-
0.000481
pyridine-2-carboxylic acid ((S)-1-[(1S,2S)-1-(biphenyl-4-ylmethoxymethyl)-3-butylcarbamoyl-2-hydroxy-propylcarbamoyl]-2-methylpropyl)-amide
-
-
0.000241
pyridine-2-carboxylic acid ((S)-1-[(1S,2S)-3-butylcarbamoyl-2-hydroxy-1-(4-thiophen-3-yl-benzyloxymethyl)-propylcarbamoyl]-2-methyl-propyl)-amide
-
-
0.0000032
pyridine-2-carboxylic acid ((S)-1-[(1S,2S)-3-[(S)-1-((S)-1-carbamoyl-3-methyl-butylcarbamoyl)-ethylcarbamoyl]-2-hydroxy-1-(4-thiophen-3-yl-benzyloxymethyl)-propyl-carbamoyl]-2-methyl-propyl)-amide
-
-
0.0000016
pyridine-2-carboxylic acid ((S)-1-[(1S,2S)-3-[(S)-1-((S)-1-carbamoyl-3-methylbutylcarbamoyl)-ethylcarbamoyl]-2-hydroxy-1-(3-thiophen-3-yl-benzyloxymethyl)-propylcarbamoyl]-2-methyl-propyl)-amide
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0045
(4'S)-3-(2-fluoropyridin-4-yl)-7-[5-(prop-1-yn-1-yl)pyridin-3-yl]-5'H-spiro[[1]benzopyrano[2,3-c]pyridine-5,4'-[1,3]oxazol]-2'-amine
Homo sapiens
-
pH and temperature not specified in the publication
0.0059
(4'S)-3-(3,6-dihydro-2H-pyran-4-yl)-7-[5-(prop-1-yn-1-yl)pyridin-3-yl]-5'H-spiro[[1]benzopyrano[2,3-c]pyridine-5,4'-[1,3]oxazol]-2'-amine
Homo sapiens
-
pH and temperature not specified in the publication
0.012
(4'S)-3-(3,6-dihydro-2H-pyran-4-yl)-7-[5-[(3-methyloxetan-3-yl)ethynyl]pyridin-3-yl]-5'H-spiro[[1]benzopyrano[2,3-c]pyridine-5,4'-[1,3]oxazol]-2'-amine
Homo sapiens
-
pH and temperature not specified in the publication
0.00009
(4'S)-3-(5,6-dihydro-2H-pyran-3-yl)-1-fluoro-7-(2-fluoropyridin-3-yl)-5'H-spiro[[1]benzopyrano[2,3-c]pyridine-5,4'-[1,3]oxazol]-2'-amine
Homo sapiens
-
pH and temperature not specified in the publication
0.0027
(4'S)-3-(5,6-dihydro-2H-pyran-3-yl)-7-[5-(prop-1-yn-1-yl)pyridin-3-yl]-5'H-spiro[[1]benzopyrano[2,3-c]pyridine-5,4'-[1,3]oxazol]-2'-amine
Homo sapiens
-
pH and temperature not specified in the publication
0.13
(4'S)-3-chloro-7-(5-fluoropyridin-3-yl)-5'H-spiro[[1]benzopyrano[2,3-c]pyridine-5,4'-[1,3]oxazol]-2'-amine
Homo sapiens
-
pH and temperature not specified in the publication
0.072
(4'S)-3-chloro-7-[5-(prop-1-yn-1-yl)pyridin-3-yl]-5'H-spiro[[1]benzopyrano[2,3-c]pyridine-5,4'-[1,3]oxazol]-2'-amine
Homo sapiens
-
pH and temperature not specified in the publication
0.00066 - 0.015
(4'S)-7-(2-fluoropyridin-3-yl)-3-(2-fluoropyridin-4-yl)-5'H-spiro[[1]benzopyrano[2,3-c]pyridine-5,4'-[1,3]oxazol]-2'-amine
0.0036
(4'S)-7-[5-(cyclopropylethynyl)pyridin-3-yl]-3-(3,6-dihydro-2H-pyran-4-yl)-5'H-spiro[[1]benzopyrano[2,3-c]pyridine-5,4'-[1,3]oxazol]-2'-amine
Homo sapiens
-
pH and temperature not specified in the publication
0.006384
(5S,8S,11S,12S,16S)-8-(3-amino-3-oxopropyl)-11-benzyl-12-hydroxy-7-methyl-16-(2-methylpropyl)-3,6,9,14-tetraoxo-1-phenyl-5-(propan-2-yl)-2-oxa-4,7,10,15-tetraazaheptadecan-17-oic acid
Homo sapiens
-
at pH 3.5 and 25°C
0.000108
(5S,8S,11S,12S,16S,19S)-8-(3-amino-3-oxopropyl)-11-benzyl-12-hydroxy-7,19-dimethyl-16-(2-methylpropyl)-3,6,9,14,17-pentaoxo-1-phenyl-5-(propan-2-yl)-2-oxa-4,7,10,15,18-pentaazaicosan-20-oic acid
Homo sapiens
-
at pH 3.5 and 25°C
0.000027
(5S,8S,11S,12S,16S,19S,22R)-8-(3-amino-3-oxopropyl)-11,22-dibenzyl-12-hydroxy-7,19,21-trimethyl-16-(2-methylpropyl)-3,6,9,14,17,20-hexaoxo-1-phenyl-5-(propan-2-yl)-2-oxa-4,7,10,15,18,21-hexaazatricosan-23-oic acid
Homo sapiens
-
at pH 3.5 and 25°C
0.00021
(5Z)-5-[4-[(4-benzoyl-3-hydroxy-2-propylphenoxy)methyl]benzylidene]-2-thioxo-1,3-thiazolidin-4-one
Homo sapiens
at pH 5.5 and 37°C
0.005
(6S,9S,12S,13S,17S)-9-(3-amino-3-oxopropyl)-12-benzyl-13-hydroxy-2,2,8-trimethyl-17-(2-methylpropyl)-4,7,10,15-tetraoxo-6-(propan-2-yl)-3-oxa-5,8,11,16-tetraazaoctadecan-18-oic acid
Homo sapiens
-
IC50 above 0.005 mM, at pH 3.5 and 25°C
0.000903
(6S,9S,12S,13S,17S,20S)-9-(3-amino-3-oxopropyl)-12-benzyl-13-hydroxy-2,2,8,20-tetramethyl-17-(2-methylpropyl)-4,7,10,15,18-pentaoxo-6-(propan-2-yl)-3-oxa-5,8,11,16,19-pentaazahenicosan-21-oic acid
Homo sapiens
-
at pH 3.5 and 25°C
0.000131
(6S,9S,12S,13S,17S,20S,23R)-9-(3-amino-3-oxopropyl)-12,23-dibenzyl-13-hydroxy-2,2,8,20,22-pentamethyl-17-(2-methylpropyl)-4,7,10,15,18,21-hexaoxo-6-(propan-2-yl)-3-oxa-5,8,11,16,19,22-hexaazatetracosan-24-oic acid
Homo sapiens
-
at pH 3.5 and 25°C
0.0019
2-(3,4-dimethoxyphenyl)-N-[N-(4-methylbenzyl)carbamimidoyl]acetamide
Homo sapiens
at pH 5.5 and 37°C
0.000085
2-bromo-N-[(2S,3S)-4-[[2-(2,4-dichlorophenyl)ethyl][3-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)propanoyl]amino]-3-hydroxy-1-(3-phenoxyphenyl)butan-2-yl]-4,5-dimethoxybenzamide
Homo sapiens
at pH 5.5 and 37°C
0.00025
3,5-dichloro-2-[[(3,5-dichloro-2-hydroxyphenyl)sulfonyl]amino]-N-[4-[(6-ethoxy-1,3-benzothiazol-2-yl)sulfanyl]phenyl]benzamide
Homo sapiens
at pH 5.5 and 37°C
0.00017
3-cyclohexyl-N-(3,4-difluorobenzyl)-N2-[N-[(3,4-dimethoxyphenyl)acetyl]carbamimidoyl]-D-alaninamide
Homo sapiens
at pH 5.5 and 37°C
0.00012
3-cyclohexyl-N-(3,4-dimethoxybenzyl)-N2-[N-[(3,4-dimethoxyphenyl)acetyl]carbamimidoyl]-D-alaninamide
Homo sapiens
at pH 5.5 and 37°C
0.000098
3-cyclohexyl-N2-[N-[(3,4-dimethoxyphenyl)acetyl]carbamimidoyl]-N-(3-fluoro-4-methoxybenzyl)-D-alaninamide
Homo sapiens
at pH 5.5 and 37°C
0.00017
3-cyclohexyl-N2-[N-[(3,4-dimethoxyphenyl)acetyl]carbamimidoyl]-N-(4-fluoro-3-methoxybenzyl)-D-alaninamide
Homo sapiens
at pH 5.5 and 37°C
0.000092
3-cyclohexyl-N2-[N-[(3,4-dimethoxyphenyl)acetyl]carbamimidoyl]-N-[3-(1H-tetrazol-5-yl)benzyl]-D-alaninamide
Homo sapiens
at pH 5.5 and 37°C
0.000081
3-cyclohexyl-N2-[N-[(3,4-dimethoxyphenyl)acetyl]carbamimidoyl]-N-[3-fluoro-4-(1H-tetrazol-5-yl)benzyl]-D-alaninamide
Homo sapiens
at pH 5.5 and 37°C
0.000044
3-cyclohexyl-N2-[N-[(3,4-dimethoxyphenyl)acetyl]carbamimidoyl]-N-[4-(1H-tetrazol-5-yl)benzyl]-D-alaninamide
Homo sapiens
at pH 5.5 and 37°C
0.0044
3-[5-[(4'S)-2'-amino-3-(3,6-dihydro-2H-pyran-4-yl)-5'H-spiro[[1]benzopyrano[2,3-c]pyridine-5,4'-[1,3]oxazol]-7-yl]pyridin-3-yl]prop-2-yn-1-ol
Homo sapiens
-
pH and temperature not specified in the publication
0.01
4-([N-[(benzyloxy)carbonyl]-L-valyl-N2-methyl-L-glutaminyl]amino)-2,4,5-trideoxy-5-phenyl-L-threo-pentonic acid
Homo sapiens
-
IC50 above 0.01 mM, at pH 3.5 and 25°C
0.0000025
cathepsin D inhibitor from Streptomyces sp.MBR04
Homo sapiens
-
in 0.02M sodium citrate, pH 3.0, at 37°C
-
0.00000584
methyl (2S)-1-[(2R,5S,8S,12S,13S)-2,13-dibenzyl-12-hydroxy-15-(3-[(methanesulfonyl)(methyl)amino]-5-[[(1R)-1-phenylethyl]carbamoyl]phenyl)-3,5-dimethyl-8-(2-methylpropyl)-4,7,10,15-tetraoxo-3,6,9,14-tetraazapentadecanan-1-oyl]pyrrolidine-2-carboxylate
Homo sapiens
-
i.e. TB-13, pH and temperature not specified in the publication
0.000196
methyl (5S,8S,11S,12S,16S)-8-(3-amino-3-oxopropyl)-11-benzyl-12-hydroxy-7-methyl-16-(2-methylpropyl)-3,6,9,14-tetraoxo-1-phenyl-5-(propan-2-yl)-2-oxa-4,7,10,15-tetraazaheptadecan-17-oate
Homo sapiens
-
at pH 3.5 and 25°C
0.000102
methyl (5S,8S,11S,12S,16S,19S)-8-(3-amino-3-oxopropyl)-11-benzyl-12-hydroxy-7,19-dimethyl-16-(2-methylpropyl)-3,6,9,14,17-pentaoxo-1-phenyl-5-(propan-2-yl)-2-oxa-4,7,10,15,18-pentaazaicosan-20-oate
Homo sapiens
-
at pH 3.5 and 25°C
0.00000329
methyl (5S,8S,11S,12S,16S,19S,22R)-8-(3-amino-3-oxopropyl)-11,22-dibenzyl-12-hydroxy-7,19,21-trimethyl-16-(2-methylpropyl)-3,6,9,14,17,20-hexaoxo-1-phenyl-5-(propan-2-yl)-2-oxa-4,7,10,15,18,21-hexaazatricosan-23-oate
Homo sapiens
-
at pH 3.5 and 25°C
0.01
methyl (6S,9S,12S,13S,17S)-9-(3-amino-3-oxopropyl)-12-benzyl-13-hydroxy-2,2,8-trimethyl-17-(2-methylpropyl)-4,7,10,15-tetraoxo-6-(propan-2-yl)-3-oxa-5,8,11,16-tetraazaoctadecan-18-oate
Homo sapiens
-
IC50 above 0.01 mM, at pH 3.5 and 25°C
0.000407
methyl (6S,9S,12S,13S,17S,20S)-9-(3-amino-3-oxopropyl)-12-benzyl-13-hydroxy-2,2,8,20-tetramethyl-17-(2-methylpropyl)-4,7,10,15,18-pentaoxo-6-(propan-2-yl)-3-oxa-5,8,11,16,19-pentaazahenicosan-21-oate
Homo sapiens
-
at pH 3.5 and 25°C
0.00019
methyl (6S,9S,12S,13S,17S,20S,23R)-9-(3-amino-3-oxopropyl)-12,23-dibenzyl-13-hydroxy-2,2,8,20,22-pentamethyl-17-(2-methylpropyl)-4,7,10,15,18,21-hexaoxo-6-(propan-2-yl)-3-oxa-5,8,11,16,19,22-hexaazatetracosan-24-oate
Homo sapiens
-
at pH 3.5 and 25°C
0.000067
N-(3,4-dimethoxybenzyl)-N2-[N-[(3,4-dimethoxyphenyl)acetyl]carbamimidoyl]-D-leucinamide
Homo sapiens
at pH 5.5 and 37°C
0.000058
N-(3,4-dimethoxybenzyl)-Na-[N-[(3,4-dimethoxyphenyl)acetyl]carbamimidoyl]-D-phenylalaninamide
Homo sapiens
at pH 5.5 and 37°C
0.0061
N-(N-benzylcarbamimidoyl)-2-(2-chloro-5-methoxyphenyl)acetamide
Homo sapiens
at pH 5.5 and 37°C
0.01
N-(N-benzylcarbamimidoyl)-2-(4,5-dimethoxy-2-nitrophenyl)acetamide
Homo sapiens
at pH 5.5 and 37°C
0.025
N-(N-benzylcarbamimidoyl)-3-(3,4-dimethoxyphenyl)propanamide
Homo sapiens
at pH 5.5 and 37°C
0.018
N-(N-benzylcarbamimidoyl)-4-(4,5-dimethoxy-2-nitrophenyl)butanamide
Homo sapiens
at pH 5.5 and 37°C
1
N-[(4'S)-2'-amino-3-(3,6-dihydro-2H-pyran-4-yl)-5'H-spiro[[1]benzopyrano[2,3-c]pyridine-5,4'-[1,3]oxazol]-7-yl]-5-chloropyridine-2-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.48
N-[(4'S)-2'-amino-3-(5,6-dihydro-2H-pyran-3-yl)-5'H-spiro[[1]benzopyrano[2,3-c]pyridine-5,4'-[1,3]oxazol]-7-yl]-5-chloropyridine-2-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
1.1
N-[(4'S)-2'-amino-3-chloro-5'H-spiro[[1]benzopyrano[2,3-c]pyridine-5,4'-[1,3]oxazol]-7-yl]-5-chloropyridine-2-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.31
N-[(4'S)-2'-amino-3-cyclopropyl-5'H-spiro[[1]benzopyrano[2,3-c]pyridine-5,4'-[1,3]oxazol]-7-yl]-5-chloropyridine-2-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
1.2
N-[(4'S)-2'-amino-3-methoxy-5'H-spiro[[1]benzopyrano[2,3-c]pyridine-5,4'-[1,3]oxazol]-7-yl]-5-chloropyridine-2-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.64
N-[(4'S)-2'-amino-3-methyl-5'H-spiro[[1]benzopyrano[2,3-c]pyridine-5,4'-[1,3]oxazol]-7-yl]-5-chloropyridine-2-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.003
N-[N-(2-chlorobenzyl)carbamimidoyl]-2-(4,5-dimethoxy-2-nitrophenyl)acetamide
Homo sapiens
at pH 5.5 and 37°C
0.00044
N-[N-(3,4-dichlorobenzyl)carbamimidoyl]-2-(4,5-dimethoxy-2-nitrophenyl)acetamide
Homo sapiens
at pH 5.5 and 37°C
0.0027
N-[N-(3,4-dimethoxybenzyl)carbamimidoyl]-2-(4,5-dimethoxy-2-nitrophenyl)acetamide
Homo sapiens
at pH 5.5 and 37°C
0.029
N-[N-(4-aminobenzyl)carbamimidoyl]-2-(3,4-dimethoxyphenyl)acetamide
Homo sapiens
at pH 5.5 and 37°C
0.0015
N-[N-(4-chlorobenzyl)carbamimidoyl]-2-(4,5-dimethoxy-2-nitrophenyl)acetamide
Homo sapiens
at pH 5.5 and 37°C
0.000015
N1-[(2S,3S)-3-hydroxy-5-([(2S)-4-methyl-1-[(2-methylpropyl)amino]-1-oxopentan-2-yl]amino)-5-oxo-1-phenylpentan-2-yl]-5-[(methanesulfonyl)(methyl)amino]-N3-[(1R)-1-phenylethyl]benzene-1,3-dicarboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000353
N1-[(2S,3S)-3-hydroxy-5-[[(2S)-1-[[(3-methoxyphenyl)methyl]amino]-4-methyl-1-oxopentan-2-yl]amino]-5-oxo-1-phenylpentan-2-yl]-5-[(methanesulfonyl)(methyl)amino]-N3-[(1R)-1-phenylethyl]benzene-1,3-dicarboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000884
N1-[(2S,3S)-5-[[(2S)-1-(cyclopropylamino)-4-methyl-1-oxopentan-2-yl]amino]-3-hydroxy-5-oxo-1-phenylpentan-2-yl]-5-[(methanesulfonyl)(methyl)amino]-N3-[(1R)-1-phenylethyl]benzene-1,3-dicarboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000086
N2-[N-[(2-bromo-4,5-dimethoxyphenyl)acetyl]carbamimidoyl]-3-cyclohexyl-N-(4-fluoro-3-methoxybenzyl)-D-alaninamide
Homo sapiens
at pH 5.5 and 37°C
0.00014
N2-[N-[(2-bromo-4,5-dimethoxyphenyl)acetyl]carbamimidoyl]-3-cyclohexyl-N-[3-(1H-tetrazol-5-yl)benzyl]-D-alaninamide
Homo sapiens
at pH 5.5 and 37°C
0.00024
N2-[N-[(2-bromo-4,5-dimethoxyphenyl)acetyl]carbamimidoyl]-N-[3-(1H-tetrazol-5-yl)benzyl]-D-leucinamide
Homo sapiens
at pH 5.5 and 37°C
0.000024
N2-[N-[(3,4-dimethoxyphenyl)acetyl]carbamimidoyl]-N-(4-fluoro-3-methoxybenzyl)-D-leucinamide
Homo sapiens
at pH 5.5 and 37°C
0.00028
N2-[N-[(3,4-dimethoxyphenyl)acetyl]carbamimidoyl]-N-[2-fluoro-3-(1H-tetrazol-5-yl)benzyl]-D-leucinamide
Homo sapiens
at pH 5.5 and 37°C
0.00037
N2-[N-[(3,4-dimethoxyphenyl)acetyl]carbamimidoyl]-N-[3-(1H-tetrazol-5-yl)benzyl]-D-leucinamide
Homo sapiens
at pH 5.5 and 37°C
0.00069
N2-[N-[(3,4-dimethoxyphenyl)acetyl]carbamimidoyl]-N-[3-fluoro-4-(1H-tetrazol-5-yl)benzyl]-D-leucinamide
Homo sapiens
at pH 5.5 and 37°C
0.00051
N2-[N-[(3,4-dimethoxyphenyl)acetyl]carbamimidoyl]-N-[4-(1H-tetrazol-5-yl)benzyl]-D-leucinamide
Homo sapiens
at pH 5.5 and 37°C
0.00032
Na-[N-[(3,4-dimethoxyphenyl)acetyl]carbamimidoyl]-N-[2-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)ethyl]-D-phenylalaninamide
Homo sapiens
at pH 5.5 and 37°C
0.0083
Na-[N-[(3,4-dimethoxyphenyl)acetyl]carbamimidoyl]-N-[2-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)ethyl]-L-phenylalaninamide
Homo sapiens
at pH 5.5 and 37°C
0.00000059 - 0.000001
pepstatin A
0.000000182
tasiamide B
Homo sapiens
-
at pH 3.5 and 25°C
0.000000126
TB-11
Homo sapiens
-
at pH 3.5 and 25°C
0.00000584
TB-13
Homo sapiens
-
pH and temperature not specified in the publication
0.0000000783
Tb-9
Homo sapiens
-
at pH 3.5 and 25°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.2 - 3.6
-
hemoglobin
3.4
-
broad optimum around
3.6 - 5
-
assay at
additional information
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 4.3
-
about 55% of maximal activity at pH 3.0 and at pH 4.3
3 - 8
-
-
3.5 - 5
-
pH 3.5: maximal activity, pH 5.0: about 50% of maximal activity, fibrinogen as substrate
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35
-
assay at
37
-
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0 - 50
-
-
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
derived from human neuroblastoma cell line BE2-M17D
Manually annotated by BRENDA team
CP-A hTRT, CP-C hTRT, CP-D hTRT
Manually annotated by BRENDA team
-
cathepsin D is overexpressed and hyper-secreted by epithelial breast cancer cells
Manually annotated by BRENDA team
-
in M-BE, a SV40T-transformed human bronchial epithelial cell line with phenotypic features of early tumorigenesis, it is shown by 2-DE/MALDI-TOF that cathepsin D among 23 other proteins is up-regulated
Manually annotated by BRENDA team
-
prostate carcinoma, breast carcinoma
Manually annotated by BRENDA team
-
human colorectal cancer cell line DLD1 and HT29 are used
Manually annotated by BRENDA team
-
hippocampal CA1 neurons, parahippocampal glial cells
Manually annotated by BRENDA team
-
studies are carried out using peripheral blood neutrophils which are purified from healthy normal individuals and patients suffering from septic shock by Ficoll-Hypaque centrifugation
Manually annotated by BRENDA team
-
cathepsin D protein is over-expressed in plasma of 36 (out of 104) patients with lung squamous cell carcinoma
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
CatD is expressed in human eccrine sweat. Both forms, the active beta-chain of CatD (31 kDa) as well as the proform (56 kDa) can be detected in eccrine sweat, the latter in lower amounts
Manually annotated by BRENDA team
additional information
-
using a tissue microarray it is shown that the cathepsin D expression levels in squamous cell carcinoma tissues is significantly higher than those in normal donors
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
cathepsin D is released from azurophilic granules in neutrophils in a caspase-independent but reactive oxygen species-dependent manner. Under inflammatory conditions the translocation of cathepsin D in the cytosol is blocked
Manually annotated by BRENDA team
-
significant correlation between age and enzyme immunoreactivity in cytoplasm of parahippocampal glial cells, no correlation between the potmortem intervall between death and autopsy and enzyme immunoreaction in CA1 neurons
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CATD_HUMAN
412
0
44552
Swiss-Prot
Secretory Pathway (Reliability: 2)
V9HWI3_HUMAN
412
0
44552
TrEMBL
Secretory Pathway (Reliability: 2)
A0A1B0GVD5_HUMAN
409
0
44238
TrEMBL
Secretory Pathway (Reliability: 2)
F8W787_HUMAN
377
0
40784
TrEMBL
other Location (Reliability: 1)
A0A1B0GWE8_HUMAN
410
0
44353
TrEMBL
Secretory Pathway (Reliability: 2)
A0A1B0GW44_HUMAN
405
0
43688
TrEMBL
Secretory Pathway (Reliability: 2)
A0A1B0GV23_HUMAN
406
0
43831
TrEMBL
Secretory Pathway (Reliability: 2)
C9JH19_HUMAN
451
0
48614
TrEMBL
Secretory Pathway (Reliability: 2)
A0A1B0GVP3_HUMAN
405
0
43687
TrEMBL
Secretory Pathway (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
13000
-
double chain form
14000
18000
-
1 * 18000 + 1 * 33000, SDS-PAGE
26229
x * 26229
27000
x * 27000, x * 35000, SDS-PAGE
29000
30000
-
x * 30000, SDS-PAGE
31000
33000
-
1 * 18000 + 1 * 33000, SDS-PAGE
34000
35000
x * 27000, x * 35000, SDS-PAGE
42000
-
gel filtration
45000
-
gel filtration
48000
49000
-
gel filtration
50000
-
x * 50000, SDS-PAGE
52000
53000
55000
-
gel filtration
56000
-
proform of CatD
additional information
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
1 * 18000 + 1 * 33000, SDS-PAGE
heterodimer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
proteolytic modification
-
intracellular proCDrec is processed into the 48 kDa intermediate single-chain and the 31 plus 13 kDa double-chain form. Processing is slower than in normal cells
side-chain modification
additional information
-
human cathepsin D is synthesized as a di-glycosylated precursor of approximately 53 kDa that is processed by proteolysis first into an intermediate single-chain of 48 kDa and eventually into the mature double-chain form
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
cathepsin D and a complex with pepstatin at 2.5 A resolution
-
cathepsin D complexed with the 6-peptide inhibitor pepstatin A
-
in complex with inhibitors, hanging drop vapor diffusion method, using 35% (w/v) PEG2000, 0.1 M Na-acetat (pH 5.5)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A38V
-
the mutation is linked with Alzheimer’s disease
D231N
S100F
-
mutant, activity affected, causative of congenital neuronal ceroid lipofuscinose
additional information
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2
-
inactivation at
677422
8 - 10
-
inactivation at
677422
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
complete inactivation within 10 days
50 - 60
-
inactivation at the temperature of 50-60°C
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the addition of progranulin to the proenzyme at a 3:1 molar ratio causes a significant destabilizing effect on the melting temperature of the proenzyme
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, stable
-
4°C or -17°C, stable for at least 3 weeks
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
3 major forms of enzyme: alpha, beta, gamma
-
pepstatin-A affinity chromatography
using Pepstatin A-affinity purification
-
using pepstatin A-chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
a vaccinia virus expression system is used for the production of recombinant human cathepsin D in human cell lines MCF7 (breast cancer), HepG2 (hepatocarcinoma) and HeLa (cervix cancer) and non-human cell line BSC1 (simian kidney epithelial). For generation of a recombinant vaccinia virus the full-length cathepsin D cDNA comprising the ATG codon is inserted downstream of a synthetic vaccinia late promoter into the vector pMJ601 which also contains the Escherichia coli LacZ gene. This expression cassette is flanked by segments of the vaccinia thymidine kinase (TK) gene that allows homologous recombination with the wild-type virus
-
expressed in Escherichia coli
-
expressed in HEK-293FT cells
-
expressed in SH-SY5Y cells and PAC-2 cells
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
cathepsin D decreases in chronic photodamaged skin
-
cathepsin D expression and activity increases during epidermal differentiation
-
cathepsin D is elevated in the frontal cortex, in pyramidal and granule cells of the hippocampus, and in cerebellar neurons of autistic subjects
-
cathepsin D is not upregulated during apoptosis induced by 300 nM taxol or 0.01 mg doxorubicin or autophagy induced by 0.01 mM tamoxifen
-
cathepsin D is overexpressed and hyper-secreted by epithelial breast cancer cells
-
epidermal growth factor rapidly induces enzyme mRNA by 2-4fold. Cathepsin D is overexpressed in breast cancer
expression in mesenchymal stem cells is increased following co-culture with breast and colon cancer cells
-
senescence induced by ionizing radiation (6 Gy), 0.3 mM hydrogen peroxide or anticancer drugs (40 nM camptothecin, 0.03 mM etoposide, or 50 ng doxorubicin) is associated with up-regulation of cathepsin D
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
molecular biology
-
insights on the amino acid region involved in the terminal processing of human cathepsin D and on the function of the processing beta-hairpin loop are provided
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
von Clausbruch, U.C.; Tschesche, H.
Cathepsin D from human leukocytes. Purification by affinity chromatography and properties of the enzyme
Biol. Chem. Hoppe-Seyler
369
683-691
1988
Homo sapiens
Manually annotated by BRENDA team
Simon, D.I.; Ezratty, A.M.; Loscalzo, J.
The fibrin(ogen)olytic properties of cathepsin D
Biochemistry
33
6555-6563
1994
Homo sapiens
Manually annotated by BRENDA team
Barrett, A.J.
Cathepsin D and other carboxyl proteinases
Proteinases in Mammalian Cells and Tissues (Barrett, A. J. , ed. )
2
209-248
1977
Bos taurus, Gallus gallus, Oryctolagus cuniculus, Homo sapiens, Rattus norvegicus, Sus scrofa
-
Manually annotated by BRENDA team
Ishikawa, I.; Cimasoni, G.
Isolation of cathepsin D from human leucocytes
Biochim. Biophys. Acta
480
228-240
1977
Homo sapiens
Manually annotated by BRENDA team
Reichelt, D.; Jacobsohn, E.; Haschen, R.J.
Purification and properties of cathepsin D from human erythrocytes
Biochim. Biophys. Acta
341
15-26
1974
Homo sapiens
Manually annotated by BRENDA team
Scarborough, P.E.; Richo, G.R.; Kay, J.; Conner, G.E.; Dunn, B.M.
Comparison of kinetic properties of native and recombinant human cathepsin D
Struct. Funct. Asp. Proteinases (Dunn, Ben M. ; ed. ) Plenum Press, New York
306
343-347
1991
Homo sapiens
Manually annotated by BRENDA team
Chen, H.C.; Zall, R.R.
Partial purification and characterization of cathepsin D-like and B-like acid proteases from surf clam viscera
J. Food Sci.
51
71-78
1986
Homo sapiens, Spisula solidissima
-
Manually annotated by BRENDA team
Gulnik, S.; Baldwin, E.T.; Trasova, N.; Erickson, J.
Human liver cathepsin D. Purification, crystallization and preliminary X-ray diffraction analysis of a lysosomal enzyme
J. Mol. Biol.
227
265-270
1992
Homo sapiens
Manually annotated by BRENDA team
Pohl, J.; Bures, L.; Slavik, K.
Isolation and characterization of cathepsin D from human gasttric mucosa
Collect. Czech. Chem. Commun.
46
3302-3313
1981
Homo sapiens
-
Manually annotated by BRENDA team
Barrett, A.J.
Purification of isoenzymes from human and chicken liver
Biochem. J.
117
601-607
1970
Gallus gallus, Homo sapiens
Manually annotated by BRENDA team
Majer, P.; Collins, J.R.; Gulnik, S.V.; Erickson, J.W.
Structure-based subsite specificity mapping of human cathepsin D using statine-based inhibitors
Protein Sci.
6
1458-1466
1997
Homo sapiens
Manually annotated by BRENDA team
Baldwin, E.T.; Bhat, T.N.; Gulnik, S.; Hosur, M.V.; Sowder, R.C.; Cachau, R.E.; Collins, J.; Silva, A.M.; Erickson, J.W.
Crystal structures of native and inhibited forms of human cathepsin D: implications for lysosomal targeting and drug design
Proc. Natl. Acad. Sci. USA
90
6796-6800
1993
Homo sapiens
Manually annotated by BRENDA team
Metcalf, P.; Fusek, M.
Two crystal structures for cathepsin D: the lysosomal targeting signal and active site
EMBO J.
12
1293-1302
1993
Bos taurus, Homo sapiens
Manually annotated by BRENDA team
Bazel, S.; Alhadeff, J.A.
Characterization of purified cathepsin D from malignmant human breast tissue
Int. J. Oncol.
14
315-319
1999
Homo sapiens
Manually annotated by BRENDA team
Beyer, B.M.; Dunn, B.M.
Prime region subsite specificity characterization of human cathepsin D: the dominant role of position 128
Protein Sci.
7
88-95
1998
Homo sapiens
Manually annotated by BRENDA team
Pimenta, D.C.; Oliveira, A.; Juliano, M.A.; Juliano, L.
Substrate specificity of human cathepsin D using internally quenched fluorescent peptides derived from reactive site loop of kallistatin
Biochim. Biophys. Acta
1544
113-122
2001
Homo sapiens
Manually annotated by BRENDA team
Cater, S.A.; Lees, W.E.; Hill, J.; Brzin, J.; Kay, J.; Phylip, L.H.
Aspartic proteinase inhibitors from tomato and potato are more potent against yeast proteinase A than cathepsin D
Biochim. Biophys. Acta
1596
76-82
2002
Homo sapiens
Manually annotated by BRENDA team
Johansson, A.C.; Steen, H.; Ollinger, K.; Roberg, K.
Cathepsin D mediates cytochrome c release and caspase activation in human fibroblast apoptosis induced by staurosporine
Cell Death Differ.
10
1253-1259
2003
Homo sapiens
Manually annotated by BRENDA team
Nogami, M.; Takatsu, A.; Endo, N.; Ishiyama, I.
An immunohistochemical study on cathepsin D in human hippocampus
Histochem. J.
32
505-508
2000
Homo sapiens
Manually annotated by BRENDA team
Bidere, N.; Lorenzo, H.K.; Carmona, S.; Laforge, M.; Harper, F.; Dumont, C.; Senik, A.
Cathepsin D triggers Bax activation, resulting in selective apoptosis-inducing factor (AIF) relocation in T lymphocytes entering the early commitment phase to apoptosis
J. Biol. Chem.
278
31401-31411
2003
Homo sapiens
Manually annotated by BRENDA team
Pimenta, D.C.; Chen, V.C.; Chao, J.; Juliano, M.A.; Juliano, L.
alpha1-antichymotrypsin and kallistatin hydrolysis by human cathepsin D
J. Protein Chem.
19
411-418
2000
Homo sapiens
Manually annotated by BRENDA team
Tsukuba, T.; Okamoto, K.; Yasuda, Y.; Morikawa, W.; Nakanishi, H.; Yamamoto, K.
New functional aspects of cathepsin D and cathepsin E
Mol. Cells
10
601-611
2000
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Johansson, P.O.; Chen, Y.; Belfrage, A.K.; Blackman, M.J.; Kvarnstroem, I.; Jansson, K.; Vrang, L.; Hamelink, E.; Hallberg, A.; Rosenquist, A.; Samuelsson, B.
Design and synthesis of potent inhibitors of the malaria aspartyl proteases plasmepsin I and II. Use of solid-phase synthesis to explore novel statine motifs
J. Med. Chem.
47
3353-3366
2004
Homo sapiens
Manually annotated by BRENDA team
Johansson, P.O.; Lindberg, J.; Blackman, M.J.; Kvarnstroem, I.; Vrang, L.; Hamelink, E.; Hallberg, A.; Rosenquist, A.; Samuelsson, B.
Design and synthesis of potent inhibitors of plasmepsin I and II: X-ray crystal structure of inhibitor in complex with plasmepsin II
J. Med. Chem.
48
4400-4409
2005
Homo sapiens
Manually annotated by BRENDA team
Karwowska, A.; Roszkowska-Jakimiec, W.; Dabrowska, E.; Gacko, M.; Chlabicz, M.
The effect of temperature, acidification, and alkalization changes as well as ethanol on salivary cathepsin D activity
Adv. Med. Sci.
51 Suppl 1
59-61
2006
Homo sapiens
Manually annotated by BRENDA team
Schechter, I.; Ziv, E.
Kinetic properties of cathepsin D and BACE 1 indicate the need to search for additional beta-secretase candidate(s)
Biol. Chem.
389
313-320
2008
Homo sapiens, Sus scrofa
Manually annotated by BRENDA team
Trincheri, N.F.; Nicotra, G.; Follo, C.; Castino, R.; Isidoro, C.
Resveratrol induces cell death in colorectal cancer cells by a novel pathway involving lysosomal cathepsin D
Carcinogenesis
28
922-931
2007
Homo sapiens
Manually annotated by BRENDA team
Minarowska, A.; Minarowski, L.; Karwowska, A.; Sands, D.; Dabrowska, E.
The activity of cathepsin D in saliva of cystic fibrosis patients
Folia Histochem. Cytobiol.
45
165-168
2007
Homo sapiens
Manually annotated by BRENDA team
Follo, C.; Castino, R.; Nicotra, G.; Trincheri, N.F.; Isidoro, C.
Folding, activity and targeting of mutated human cathepsin D that cannot be processed into the double-chain form
Int. J. Biochem. Cell Biol.
39
638-649
2007
Homo sapiens
Manually annotated by BRENDA team
Haidar, B.; Kiss, R.S.; Sarov-Blat, L.; Brunet, R.; Harder, C.; McPherson, R.; Marcel, Y.L.
Cathepsin D, a lysosomal protease, regulates ABCA1-mediated lipid efflux
J. Biol. Chem.
281
39971-39981
2006
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Baechle, D.; Flad, T.; Cansier, A.; Steffen, H.; Schittek, B.; Tolson, J.; Herrmann, T.; Dihazi, H.; Beck, A.; Mueller, G.A.; Mueller, M.; Stevanovic, S.; Garbe, C.; Mueller, C.A.; Kalbacher, H.
Cathepsin D is present in human eccrine sweat and involved in the postsecretory processing of the antimicrobial peptide DCD-1L
J. Biol. Chem.
281
5406-5415
2006
Homo sapiens
Manually annotated by BRENDA team
Conus, S.; Perozzo, R.; Reinheckel, T.; Peters, C.; Scapozza, L.; Yousefi, S.; Simon, H.U.
Caspase-8 is activated by cathepsin D initiating neutrophil apoptosis during the resolution of inflammation
J. Exp. Med.
205
685-698
2008
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Lou, X.; Xiao, T.; Zhao, K.; Wang, H.; Zheng, H.; Lin, D.; Lu, Y.; Gao, Y.; Cheng, S.; Liu, S.; Xu, N.
Cathepsin D is secreted from M-BE cells: its potential role as a biomarker of lung cancer
J. Proteome Res.
6
1083-1092
2007
Homo sapiens
Manually annotated by BRENDA team
Demoz, M.; Castino, R.; Follo, C.; Hasilik, A.; Sloane, B.F.; Isidoro, C.
High yield synthesis and characterization of phosphorylated recombinant human procathepsin D expressed in mammalian cells
Protein Expr. Purif.
45
157-167
2006
Homo sapiens
Manually annotated by BRENDA team
Fritchie, K.; Siintola, E.; Armao, D.; Lehesjoki, A.E.; Marino, T.; Powell, C.; Tennison, M.; Booker, J.M.; Koch, S.; Partanen, S.; Suzuki, K.; Tyynelae, J.; Thorne, L.B.
Novel mutation and the first prenatal screening of cathepsin D deficiency (CLN10)
Acta Neuropathol.
117
201-208
2009
Homo sapiens
Manually annotated by BRENDA team
Markicevic, M.; Petrovic, A.; Kanjer, K.; Neskovic-Konstantinovic, Z.; Nikolic-Vukosavujevic, D.
Estrogen-regulated cut-off values of pS2 and cathepsin D expression in breast carcinomas
Adv. Exp. Med. Biol.
617
341-348
2008
Homo sapiens
Manually annotated by BRENDA team
Beaujouin, M.; Liaudet-Coopman, E.
Cathepsin D overexpressed by cancer cells can enhance apoptosis-dependent chemo-sensitivity independently of its catalytic activity
Adv. Exp. Med. Biol.
617
453-461
2008
Homo sapiens
Manually annotated by BRENDA team
Fernandez-Aguilar, S.; Noel, J.C.
Expression of cathepsin D and galectin 3 in tubular carcinomas of the breast
APMIS
116
33-40
2008
Homo sapiens
Manually annotated by BRENDA team
Zaidi, N.; Maurer, A.; Nieke, S.; Kalbacher, H.
Cathepsin D: a cellular roadmap
Biochem. Biophys. Res. Commun.
376
5-9
2008
Homo sapiens, Clupea harengus (Q9DEX3)
Manually annotated by BRENDA team
Sevlever, D.; Jiang, P.; Yen, S.H.
Cathepsin D is the main lysosomal enzyme involved in the degradation of alpha-synuclein and generation of its carboxy-terminally truncated species
Biochemistry
47
9678-9687
2008
Homo sapiens (P07339), Mus musculus (P10605)
Manually annotated by BRENDA team
Salvioli, R.; Ricci-Vitiani, L.; Tatti, M.; Scarpa, S.; De Maria, R.; Vaccaro, A.M.
The secretion and maturation of prosaposin and procathepsin D are blocked in embryonic neural progenitor cells
Biochim. Biophys. Acta
1783
1480-1489
2008
Homo sapiens
Manually annotated by BRENDA team
Zheng, X.; Chu, F.; Mirkin, B.L.; Sudha, T.; Mousa, S.A.; Rebbaa, A.
Role of the proteolytic hierarchy between cathepsin L, cathepsin D and caspase-3 in regulation of cellular susceptibility to apoptosis and autophagy
Biochim. Biophys. Acta
1783
2294-2300
2008
Homo sapiens
Manually annotated by BRENDA team
Bishop, M.T.; Kovacs, G.G.; Sanchez-Juan, P.; Knight, R.S.
Cathepsin D SNP associated with increased risk of variant Creutzfeldt-Jakob disease
BMC Med. genet.
9
31
2008
Homo sapiens (P07339), Homo sapiens
Manually annotated by BRENDA team
Hu, L.; Roth, J.M.; Brooks, P.; Luty, J.; Karpatkin, S.
Thrombin up-regulates cathepsin D which enhances angiogenesis, growth, and metastasis
Cancer Res.
68
4666-4673
2008
Homo sapiens (P07339), Homo sapiens
Manually annotated by BRENDA team
Sagulenko, V.; Muth, D.; Sagulenko, E.; Paffhausen, T.; Schwab, M.; Westermann, F.
Cathepsin D protects human neuroblastoma cells from doxorubicin-induced cell death
Carcinogenesis
29
1869-1877
2008
Homo sapiens
Manually annotated by BRENDA team
Benes, P.; Vetvicka, V.; Fusek, M.
Cathepsin D - many functions of one aspartic protease
Crit. Rev. Oncol. Hematol.
68
12-28
2008
Homo sapiens
Manually annotated by BRENDA team
Wozniak, B.; Mila-Kierzenkowska, C.; Wozniak, A.; Drewa, G.; Soponska, M.; Drewa, T.; Krzyzynska-Malinowska, E.; Makarewicz, R.; Kowalski, T.; Szmytkowska, K.
The effect of combined therapy on activity of cathepsin D and alpha-1-antitrypsin in the blood serum of women with cervical cancer
Eur. J. Gynaecol. Oncol.
29
617-619
2008
Homo sapiens
Manually annotated by BRENDA team
Szajda, S.D.; Snarska, J.; Jankowska, A.; Roszkowska-Jakimiec, W.; Puchalski, Z.; Zwierz, K.
Cathepsin D and carcino-embryonic antigen in serum, urine and tissues of colon adenocarcinoma patients
Hepatogastroenterology
55
388-393
2008
Homo sapiens
Manually annotated by BRENDA team
Khalkhali-Ellis, Z.; Abbott, D.E.; Bailey, C.M.; Goossens, W.; Margaryan, N.V.; Gluck, S.L.; Reuveni, M.; Hendrix, M.J.
IFN-gamma regulation of vacuolar pH, cathepsin D processing and autophagy in mammary epithelial cells
J. Cell. Biochem.
105
208-218
2008
Homo sapiens
Manually annotated by BRENDA team
Castino, R.; Peracchio, C.; Salini, A.; Nicotra, G.; Trincheri, N.F.; Demoz, M.; Valente, G.; Isidoro, C.
Chemotherapy drug response in ovarian cancer cells strictly depends on a cathepsin D - bax activation loop
J. Cell. Mol. Med.
13
1096-1109
2009
Homo sapiens
Manually annotated by BRENDA team
Breton, J.; Gage, M.C.; Hay, A.W.; Keen, J.N.; Wild, C.P.; Donnellan, C.; Findlay, J.B.; Hardie, L.J.
Proteomic screening of a cell line model of esophageal carcinogenesis identifies cathepsin D and aldo-keto reductase 1C2 and 1B10 dysregulation in Barretts esophagus and esophageal adenocarcinoma
J. Proteome Res.
7
1953-1962
2008
Homo sapiens (P07339), Homo sapiens
Manually annotated by BRENDA team
Cheng, A.L.; Huang, W.G.; Chen, Z.C.; Zhang, P.F.; Li, M.Y.; Li, F.; Li, J.L.; Li, C.; Yi, H.; Peng, F.; Duan, C.J.; Xiao, Z.Q.
Identificating cathepsin D as a biomarker for differentiation and prognosis of nasopharyngeal carcinoma by laser capture microdissection and proteomic analysis
J. Proteome Res.
7
2415-2426
2008
Homo sapiens (P07339), Homo sapiens
Manually annotated by BRENDA team
Perez-Victoria, F.J.; Mardones, G.A.; Bonifacino, J.S.
Requirement of the human GARP complex for mannose 6-phosphate-receptor-dependent sorting of cathepsin D to lysosomes
Mol. Biol. Cell
19
2350-2362
2008
Homo sapiens
Manually annotated by BRENDA team
Capurso, C.; Solfrizzi, V.; DIntrono, A.; Colacicco, A.M.; Capurso, S.A.; Bifaro, L.; Menga, R.; Santamato, A.; Seripa, D.; Pilotto, A.; Capurso, A.; Panza, F.
Short arm of chromosome 11 and sporadic Alzheimers disease: catalase and cathepsin D gene polymorphisms
Neurosci. Lett.
432
237-242
2008
Homo sapiens (P07339), Homo sapiens
Manually annotated by BRENDA team
Feron, D.; Begu-Le Corroller, A.; Piot, J.M.; Frelicot, C.; Vialettes, B.; Fruitier-Arnaudin, I.
Significant lower VVH7-like immunoreactivity serum level in diabetic patients: evidence for independence from metabolic control and three key enzymes in hemorphin metabolism, cathepsin D, ACE and DPP-IV
Peptides
30
256-261
2009
Homo sapiens
Manually annotated by BRENDA team
Masson, O.; Bach, A.S.; Derocq, D.; Prebois, C.; Laurent-Matha, V.; Pattingre, S.; Liaudet-Coopman, E.
Pathophysiological functions of cathepsin D: Targeting its catalytic activity versus its protein binding activity?
Biochimie
92
1635-1643
2010
Homo sapiens
Manually annotated by BRENDA team
Byun, H.O.; Han, N.K.; Lee, H.J.; Kim, K.B.; Ko, Y.G.; Yoon, G.; Lee, Y.S.; Hong, S.I.; Lee, J.S.
Cathepsin D and eukaryotic translation elongation factor 1 as promising markers of cellular senescence
Cancer Res.
69
4638-4647
2009
Homo sapiens
Manually annotated by BRENDA team
Vashishta, A.; Ohri, S.; Vetvicka, V.
Pleiotropic effects of cathepsin D
Endocr. Metab. Immune Disord. Drug Targets
9
385-391
2009
Homo sapiens
Manually annotated by BRENDA team
van der Hilst, J.C.; Kluve-Beckerman, B.; van der Meer, J.W.; Simon, A.
Cathepsin D activity protects against development of type AA amyloid fibrils
Eur. J. Clin. Invest.
39
412-416
2009
Homo sapiens
Manually annotated by BRENDA team
Christensen, B.; Schack, L.; Klaening, E.; Sorensen, E.S.
Osteopontin is cleaved at multiple sites close to its integrin-binding motifs in milk and is a novel substrate for plasmin and cathepsin D
J. Biol. Chem.
285
7929-7937
2010
Homo sapiens
Manually annotated by BRENDA team
Sheikh, A.M.; Li, X.; Wen, G.; Tauqeer, Z.; Brown, W.T.; Malik, M.
Cathepsin D and apoptosis related proteins are elevated in the brain of autistic subjects
Neuroscience
165
363-370
2010
Homo sapiens
Manually annotated by BRENDA team
Feron, D.; Piot, J.M.; Fruitier-Arnaudin, I.
Proteolytic degradation by cathepsin D of glycated hemoglobin from diabetes patients gives rise to hemorphin-7 peptides
Peptides
31
956-961
2010
Homo sapiens
Manually annotated by BRENDA team
Bewley, M.A.; Marriott, H.M.; Tulone, C.; Francis, S.E.; Mitchell, T.J.; Read, R.C.; Chain, B.; Kroemer, G.; Whyte, M.K.; Dockrell, D.H.
A cardinal role for cathepsin D in co-ordinating the host-mediated apoptosis of macrophages and killing of pneumococci
PLoS Pathog.
7
e1001262
2011
Homo sapiens
Manually annotated by BRENDA team
Menon, V.; Rao, M.
Interactions of a low molecular weight inhibitor from Streptomyces sp. MBR04 with human cathepsin D: implications in mechanism of inactivation
Appl. Biochem. Biotechnol.
174
1705-1723
2014
Homo sapiens
Manually annotated by BRENDA team
Achour, O.; Bridiau, N.; Kacem, M.; Delatouche, R.; Bordenave-Juchereau, S.; Sannier, F.; Thiery, V.; Piot, J.M.; Maugard, T.; Arnaudin, I.
Cathepsin D activity and selectivity in the acidic conditions of a tumor microenvironment: Utilization in the development of a novel cathepsin D substrate for simultaneous cancer diagnosis and therapy
Biochimie
95
2010-2017
2013
Homo sapiens
Manually annotated by BRENDA team
Khalkhali-Ellis, Z.; Hendrix, M.J.
Two faces of cathepsin D: physiological guardian angel and pathological demon
Biol. Med. (Aligarh)
6
1000206
2014
Homo sapiens (P07339), Homo sapiens
Manually annotated by BRENDA team
Graedler, U.; Czodrowski, P.; Tsaklakidis, C.; Klein, M.; Werkmann, D.; Lindemann, S.; Maskos, K.; Leuthner, B.
Structure-based optimization of non-peptidic Cathepsin D inhibitors
Bioorg. Med. Chem. Lett.
24
4141-4150
2014
Homo sapiens (P07339)
Manually annotated by BRENDA team
Oliveira, C.S.; Pereira, H.; Alves, S.; Castro, L.; Baltazar, F.; Chaves, S.R.; Preto, A.; Corte-Real, M.
Cathepsin D protects colorectal cancer cells from acetate-induced apoptosis through autophagy-independent degradation of damaged mitochondria
Cell Death Dis.
6
e1788
2015
Saccharomyces cerevisiae, Homo sapiens
Manually annotated by BRENDA team
Follo, C.; Ozzano, M.; Montalenti, C.; Ekkapongpisit, M.; Isidoro, C.
Similarities and differences in the biogenesis, processing and lysosomal targeting between zebrafish and human pro-Cathepsin D: functional implications
Int. J. Biochem. Cell Biol.
45
273-282
2013
Homo sapiens (P07339), Homo sapiens, Danio rerio (Q8JH28), Danio rerio
Manually annotated by BRENDA team
Conus, S.; Pop, C.; Snipas, S.J.; Salvesen, G.S.; Simon, H.U.
Cathepsin D primes caspase-8 activation by multiple intra-chain proteolysis
J. Biol. Chem.
287
21142-21151
2012
Homo sapiens
Manually annotated by BRENDA team
Sun, H.; Lou, X.; Shan, Q.; Zhang, J.; Zhu, X.; Zhang, J.; Wang, Y.; Xie, Y.; Xu, N.; Liu, S.
Proteolytic characteristics of cathepsin D related to the recognition and cleavage of its target proteins
PLoS ONE
8
e65733
2013
Homo sapiens
Manually annotated by BRENDA team
Zheng, Y.; Chen, H.; Lai, W.; Xu, Q.; Liu, C.; Wu, L.; Maibach, H.I.
Cathepsin D repairing role in photodamaged skin barrier
Skin Pharmacol. Physiol.
28
97-102
2015
Homo sapiens
Manually annotated by BRENDA team
Butler, V.J.; Cortopassi, W.A.; Gururaj, S.; Wang, A.L.; Pierce, O.M.; Jacobson, M.P.; Kao, A.W.
Multi-granulin domain peptides bind to pro-cathepsin D and stimulate its enzymatic activity more effectively than progranulin in vitro
Biochemistry
58
2670-2674
2019
Homo sapiens
Manually annotated by BRENDA team
Vangala, G.; Imhoff, F.M.; Squires, C.M.L.; Cridge, A.G.; Baird, S.K.
Mesenchymal stem cell homing towards cancer cells is increased by enzyme activity of cathepsin D
Exp. Cell Res.
383
111494
2019
Homo sapiens
Manually annotated by BRENDA team
Monickaraj, F.; McGuire, P.; Das, A.
Cathepsin D plays a role in endothelial-pericyte interactions during alteration of the blood-retinal barrier in diabetic retinopathy
FASEB J.
32
2539-2548
2018
Homo sapiens
Manually annotated by BRENDA team
Butler, V.J.; Cortopassi, W.A.; Argouarch, A.R.; Ivry, S.L.; Craik, C.S.; Jacobson, M.P.; Kao, A.W.
Progranulin stimulates the in vitro maturation of pro-cathepsin D at acidic pH
J. Mol. Biol.
431
1038-1047
2019
Homo sapiens
Manually annotated by BRENDA team
Xu, H.; Bao, K.; Tang, S.; Ai, J.; Hu, H.; Zhang, W.
Cyanobacterial peptides as a prototype for the design of cathepsin D inhibitors
J. Pept. Sci.
23
701-706
2017
Homo sapiens
Manually annotated by BRENDA team
Li, Z.; Bao, K.; Xu, H.; Wu, P.; Li, W.; Liu, J.; Zhang, W.
Design, synthesis, and bioactivities of tasiamide B derivatives as cathepsin D inhibitors
J. Pept. Sci.
25
e3154
2019
Homo sapiens
Manually annotated by BRENDA team
Low, J.D.; Bartberger, M.D.; Chen, K.; Cheng, Y.; Fielden, M.R.; Gore, V.; Hickman, D.; Liu, Q.; Allen Sickmier, E.; Vargas, H.M.; Werner, J.; White, R.D.; Whittington, D.A.; Wood, S.; Minatti, A.E.
Development of 2-aminooxazoline 3-azaxanthene beta-amyloid cleaving enzyme (BACE) inhibitors with improved selectivity against cathepsin D
MedChemComm
8
1196-1206
2017
Homo sapiens
Manually annotated by BRENDA team
Pereira, H.; Oliveira, C.S.; Castro, L.; Preto, A.; Chaves, S.R.; Corte-Real, M.
Yeast as a tool to explore cathepsin D function
Microb. Cell
2
225-234
2015
Saccharomyces cerevisiae, Homo sapiens
Manually annotated by BRENDA team
Jancekova, B.; Ondrouskova, E.; Knopfova, L.; Smarda, J.; Benes, P.
Enzymatically active cathepsin D sensitizes breast carcinoma cells to TRAIL
Tumour Biol.
37
10685-10696
2016
Homo sapiens
Manually annotated by BRENDA team