Any feedback?
Information on EC 3.4.23.22 - Endothiapepsin and Organism(s) Cryphonectria parasitica and UniProt Accession P11838
for references in articles please use BRENDA:EC3.4.23.22Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
3.4.23.22 EndothiapepsinSpecify your search results
Word Map
- 3.4.23.22
- proteinases
-
3.4.23.6
- renin
- rhizopuspepsin
- penicillopepsin
-
scissile
-
hydroxyethylene
-
hit-to-lead
-
isostere
- cryphonectria
-
gem-diol
- medicine
- nutrition
The taxonomic range for the selected organisms is: Cryphonectria parasitica
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
hydrolysis of proteins with specificity similar to that of pepsin A; prefers hydrophobic residues at P1 and P1', but does not cleave Ala14-Leu in the B chain of insulin or Z-Glu-Tyr. Clots milk
Synonyms
endothiapepsin, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Aspartate protease
-
-
-
-
Endothia acid proteinase
-
-
-
-
Endothia aspartic proteinase
-
-
-
-
Endothia parasitica acid proteinase
-
-
-
-
Endothia parasitica aspartic proteinase
-
-
-
-
Proteinase, Endothia aspartic
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hydrolysis of proteins with specificity similar to that of pepsin A; prefers hydrophobic residues at P1 and P1', but does not cleave Ala14-Leu in the B chain of insulin or Z-Glu-Tyr. Clots milk
hydrolysis of proteins with specificity similar to that of pepsin A; prefers hydrophobic residues at P1 and P1', but does not cleave Ala14-Leu in the B chain of insulin or Z-Glu-Tyr. Clots milk
the enzyme contains a catalytic Asp dyad
-
hydrolysis of proteins with specificity similar to that of pepsin A; prefers hydrophobic residues at P1 and P1', but does not cleave Ala14-Leu in the B chain of insulin or Z-Glu-Tyr. Clots milk
catalytic mechanism, X-ray, neutron and NMR studies
-
CAS REGISTRY NUMBER
COMMENTARY
37205-60-0
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Abz-Thr-Ile-Nle-4-nitro-Phe-Gln-Arg-NH2 + H2O
Abz-Thr-Ile-Nle + 4-nitro-Phe-Gln-Arg-NH2
-
-
-
?
FVNQHLCGSHLVEALYLVCGERGFFYTPKA + H2O
FVN + Gln + HLCGSHL + VEALY + LVCGERGF + FYTPKA
-
i.e. oxidized insulin B chain, cleavage site specificity
-
-
?
kappa-casein + H2O
?
-
reaction contributes to milk-clotting activity, cleavage site specificity for Ser104-Phe105
-
-
?
Oxidized B-chain of insulin + H2O
?
-
the Phe24-Phe25 bond is hydrolyzed at a maximal rate followed by hydrolysis of the Tyr16-Leu17 and Gln4-His5 bonds. The Leu11-Val12 and Asn3-Gln4 bonds are hydrolyzed at slower rates. The Leu11-Val12 bond appears to be considerably more resistant to hydrolysis in the peptide 5-16 than in the intact oxidized B-chain. The Leu15-Tyr16 bond is very slowly hydrolyzed in the peptide 5-16, no hydrolysis in the intact oxidized B-chain. Phe25 is slowly hydrolyzed from the peptide 25-30 and the bond involving Gly20-Glu21 is slowly hydrolyzed in peptide 12-24 and/or peptide 17-24
-
-
?
additional information
?
-
-
clots milk, not: benzyloxycarbonyl-L-Glu-L-Tyr
-
-
?
additional information
?
-
-
the enzyme prefers protein substrates with hydrophobic amino acid residues at P1 and P1' positions
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(1S)-2-(1H-indol-3-yl)-1-[5-(2,4,6-trimethylbenzyl)-1,3-thiazol-2-yl]ethanamine
-
(2R)-2-amino-N'-[(E)-(4-hydroxynaphthalen-1-yl)methylidene]-2-phenylacetohydrazide
-
(2S)-2-amino-2-[4-(trifluoromethyl)phenyl]-N'-[(E)-[3-(trifluoromethyl)phenyl]methylidene]acetohydrazide
-
(2S)-2-amino-2-[4-(trifluoromethyl)phenyl]-N'-[(E)-[4-(trifluoromethyl)phenyl]methylidene]acetohydrazide
-
(2S)-2-amino-3-(1H-indol-3-yl)-N'-[(E)-(2,4,6-trimethylphenyl)methylidene]propanehydrazide
-
(2S)-2-amino-3-(1H-indol-3-yl)-N'-[(E)-(2-methylphenyl)methylidene]propanehydrazide
-
(2S)-2-amino-3-(1H-indol-3-yl)-N'-[(E)-phenylmethylidene]propanehydrazide
-
(2S)-2-amino-3-(1H-indol-3-yl)-N'-[(E)-[3-(trifluoromethyl)phenyl]methylidene]propanehydrazide
-
(2S)-2-amino-3-(1H-indol-3-yl)-N'-[(E)-[4-(trifluoromethyl)phenyl]methylidene]propanehydrazide
-
(2S)-2-amino-N'-[(1E)-2-methylbutylidene]-2-[4-(trifluoromethyl)phenyl]acetohydrazide
-
(2S)-2-amino-N'-[(E)-(2,6-dimethylphenyl)methylidene]-3-(1H-indol-3-yl)propanehydrazide
-
(2S)-2-amino-N'-[(E)-(2-bromophenyl)methylidene]-3-(1H-indol-3-yl)propanehydrazide
-
(2S)-2-amino-N'-[(E)-(2-fluorophenyl)methylidene]-3-(1H-indol-3-yl)propanehydrazide
-
(2S)-2-amino-N'-[(E)-(2-hydroxy-3-methylphenyl)methylidene]-2-[4-(trifluoromethyl)phenyl]acetohydrazide
-
(2S)-2-amino-N'-[(E)-(2-hydroxy-3-methylphenyl)methylidene]-3-(1H-indol-3-yl)propanehydrazide
-
(2S)-2-amino-N'-[(E)-(3-methylphenyl)methylidene]-2-[4-(trifluoromethyl)phenyl]acetohydrazide
-
(2S)-2-amino-N'-[(E)-(pyridin-2-yl)methylidene]-2-[4-(trifluoromethyl)phenyl]acetohydrazide
-
(2S)-2-amino-N'-[(E)-cyclohexylmethylidene]-2-[4-(trifluoromethyl)phenyl]acetohydrazide
-
(S)-2-amino-N'-(cyclopentylmethylene)-2-(4-(trifluoromethyl)phenyl)acetohydrazide trifluoro acetic acid
-
(S)-2-amino-N'-benzylidene-2-(4-(trifluoromethyl)phenyl)acetohydrazide
-
1-(4-[1-[2-(4-chlorophenyl)ethyl]-1H-1,2,3-triazol-4-yl]phenyl)piperazine
-
2-[1-[2-(2-fluorophenyl)ethyl]-1H-1,2,3-triazol-4-yl]-1-phenylethan-1-amine
-
4-(2-[4-[4-(piperazin-1-yl)phenyl]-1H-1,2,3-triazol-1-yl]ethyl)phenol
-
N',N'''-((1E,1'E)-1,3-phenylenebis(methaneylylidene))bis(2-amino-3-(1H-indol-3-yl)propanehydrazide)
-
rac-(2R,2'R)-N',N'''-((1E,1'E)-1,3-phenylenebis(methaneylylidene))bis(2-amino-3-phenylpropanehydrazide)
-
L363564
-
statine-containing renin inhibitor, hydrogen bonding interaction witht the enzyme, e.g. via Asp32 and Asp215, overview
pepstatin
-
complex formation, structure analysis, conformation changes induced by protein-inhibitor association, proton release and uptake, overview
pepstatin A
-
strong inhibition, the inhibitor motif -CH(OH)-CH2- mimicks the tetrahedral intermdiate of the catalytic reaction
additional information
-
a structural comparison of 21 inhibitor complexes of endothiapepsin
-
additional information
-
interaction of aspartic proteinases with naturally occuring inhibitors from actinomycetes and Ascaris lumbricoides
-
additional information
-
molecular mechanism of enzyme inhibition by phosphinate and phosphonate inhibitors, molecular dynamic simulations for investigation of the hydrogen bonding pattern, structure, overview
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0016
Abz-Thr-Ile-Nle-4-nitro-Phe-Gln-Arg-NH2
in 0.1 M acetate buffer, pH 4.6, containing 0.01% (v/v) Tween 20, temperature not specified in the publication
0.0016
Abz-Thr-Ile-Nle-4-nitro-Phe-Gln-Arg-NH2
at pH 4.6, temperature not specified in the publication
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0912
(1S)-2-(1H-indol-3-yl)-1-[5-(2,4,6-trimethylbenzyl)-1,3-thiazol-2-yl]ethanamine
pH and temperature not specified in the publication
0.007
(2R)-2-amino-N'-[(E)-(4-hydroxynaphthalen-1-yl)methylidene]-2-phenylacetohydrazide
pH and temperature not specified in the publication
0.006
(2S)-2-amino-3-(1H-indol-3-yl)-N'-[(E)-(2,4,6-trimethylphenyl)methylidene]propanehydrazide
pH and temperature not specified in the publication
0.0135
2-(2,4,6-trimethylphenyl)ethyl L-tryptophanate
pH and temperature not specified in the publication
0.0000254
N',N'''-((1E,1'E)-1,3-phenylenebis(methaneylylidene))bis(2-amino-3-(1H-indol-3-yl)propanehydrazide)
pH and temperature not specified in the publication
0.0061
N-[2-(2,4,6-trimethylphenyl)ethyl]-L-tryptophanamide
pH and temperature not specified in the publication
0.00098
rac-(2R,2'R)-N',N'''-((1E,1'E)-1,3-phenylenebis(methaneylylidene))bis(2-amino-3-phenylpropanehydrazide)
pH and temperature not specified in the publication
additional information
additional information
-
pepstatin inhibition kinetics and thermodynamics, overview
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.1937
(1S)-2-(1H-indol-3-yl)-1-[5-(2,4,6-trimethylbenzyl)-1,3-thiazol-2-yl]ethanamine
Cryphonectria parasitica
pH and temperature not specified in the publication
0.0145
(2R)-2-amino-N'-[(E)-(4-hydroxynaphthalen-1-yl)methylidene]-2-phenylacetohydrazide
Cryphonectria parasitica
pH and temperature not specified in the publication
0.0128
(2S)-2-amino-3-(1H-indol-3-yl)-N'-[(E)-(2,4,6-trimethylphenyl)methylidene]propanehydrazide
Cryphonectria parasitica
pH and temperature not specified in the publication
0.059
(2S)-2-amino-3-(1H-indol-3-yl)-N'-[(E)-(2-methylphenyl)methylidene]propanehydrazide
Cryphonectria parasitica
pH and temperature not specified in the publication
0.049
(2S)-2-amino-3-(1H-indol-3-yl)-N'-[(E)-phenylmethylidene]propanehydrazide
Cryphonectria parasitica
pH and temperature not specified in the publication
0.244
(2S)-2-amino-3-(1H-indol-3-yl)-N'-[(E)-[3-(trifluoromethyl)phenyl]methylidene]propanehydrazide
Cryphonectria parasitica
pH and temperature not specified in the publication
0.007
(2S)-2-amino-3-(1H-indol-3-yl)-N'-[(E)-[4-(trifluoromethyl)phenyl]methylidene]propanehydrazide
Cryphonectria parasitica
pH and temperature not specified in the publication
0.03
(2S)-2-amino-N'-[(E)-(2,6-dimethylphenyl)methylidene]-3-(1H-indol-3-yl)propanehydrazide
Cryphonectria parasitica
pH and temperature not specified in the publication
0.0545
(2S)-2-amino-N'-[(E)-(2-bromophenyl)methylidene]-3-(1H-indol-3-yl)propanehydrazide
Cryphonectria parasitica
pH and temperature not specified in the publication
0.038
(2S)-2-amino-N'-[(E)-(2-fluorophenyl)methylidene]-3-(1H-indol-3-yl)propanehydrazide
Cryphonectria parasitica
pH and temperature not specified in the publication
0.036
(2S)-2-amino-N'-[(E)-(2-hydroxy-3-methylphenyl)methylidene]-3-(1H-indol-3-yl)propanehydrazide
Cryphonectria parasitica
pH and temperature not specified in the publication
0.085
(S)-2-amino-N'-(cyclopentylmethylene)-2-(4-(trifluoromethyl)phenyl)acetohydrazide trifluoro acetic acid
Cryphonectria parasitica
pH and temperature not specified in the publication
0.21
(S)-2-amino-N'-benzylidene-2-(4-(trifluoromethyl)phenyl)acetohydrazide
Cryphonectria parasitica
pH and temperature not specified in the publication
0.142
1-(4-ethynylphenyl)piperazine
Cryphonectria parasitica
pH and temperature not specified in the publication
0.121
1-(4-[1-[2-(4-chlorophenyl)ethyl]-1H-1,2,3-triazol-4-yl]phenyl)piperazine
Cryphonectria parasitica
pH and temperature not specified in the publication
0.0287
2-(2,4,6-trimethylphenyl)ethyl L-tryptophanate
Cryphonectria parasitica
pH and temperature not specified in the publication
0.094
2-[1-[2-(2-fluorophenyl)ethyl]-1H-1,2,3-triazol-4-yl]-1-phenylethan-1-amine
Cryphonectria parasitica
pH and temperature not specified in the publication
0.043
4-(2-[4-[4-(piperazin-1-yl)phenyl]-1H-1,2,3-triazol-1-yl]ethyl)phenol
Cryphonectria parasitica
pH and temperature not specified in the publication
0.0000545
N',N'''-((1E,1'E)-1,3-phenylenebis(methaneylylidene))bis(2-amino-3-(1H-indol-3-yl)propanehydrazide)
Cryphonectria parasitica
pH and temperature not specified in the publication
0.0129
N-[2-(2,4,6-trimethylphenyl)ethyl]-L-tryptophanamide
Cryphonectria parasitica
pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). CARP_CRYPA
419
0
43255
Swiss-Prot
Secretory Pathway (Reliability: 3)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method, using 0.1 M NH4Ac, 0.1 M acetate buffer, pH 4.6, and 26% (w/v) PEG 4000
complexes of pepstatin A and a statine-containing human renin inhibitor with endothiapepsin
-
crystal structure of enzyme bound to inhibitor Pd130328, inhibitor binding structure and analysis
-
in complex with gem-diol inhibitor PD-135,040, hanging-drop vapour-diffusion method, space group P2(1), unit-cell parameters a : 53.20, b : 73.25, c : 46.00
-
of the complex between endothiapepsin and an oligopeptide inhibitor
-
space group P2(1), in complex with H189 unit cell parameters a : 42.48, b : 75.78, c : 42.99, in complex with CP-80,794 unit cell parameters a : 42.55, b : 74.62, c : 44.43, in complex with CP-129,541 unit cell parameters a : 42.47, b : 74.31, c : 42.81, in complex with PD-130,328 unit cell parameters a : 43.88, b : 75.44, c : 43.23, in complex with H256 unit cell parameters a : 43.88, b : 75.44, c : 43.23
-
three-dimensional structure of endothiapepsin complexed with a transition-state isostere inhibitor of renin
-
using ammonium sulfate as precipitant at pH 4.6, X-ray diffraction structure determination and analysis at 2.1 A resolution, multiple isomorphous replacement
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.8 - 4.5
-
50°C, maximal stability, 30% loss of activity after 30 min
30629
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Enzyme solution equilibrated against 0.01 M acetate buffer, pH 4.6, and frozen at -25°C to -30°C, may be lyophilized with no loss of activity
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
aspartic proteinases play major roles in amyloid disease and malaria, implicated in tumourigenesis, design of inhibitors to this class of enzymes as potential therapeutic agents
nutrition
-
the enzyme can be used as a fungal rennet in cheese production
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Subramanian, E.; Swan, I.D.A.; Liu, M.; Davies, D.R.; Jenkins, J.A.; Tickle, I.J.; Blundell, T.L.
Homology among acid proteases: comparison of crystal structures at 3A resolution of acid proteases from Rhizopus chinensis and Endothia parasitica
Proc. Natl. Acad. Sci. USA
74
556-559
1977
Cryphonectria parasitica
Whitaker, J.R.
Protease of Endothia parasitica
Methods Enzymol.
19
436-445
1970
Cryphonectria parasitica
-
Williams, D.C.; Whitaker, J.R.; Caldwell, P.V.
Hydrolysis of peptide bonds of the oxidized B-chain of insulin by Endothia parasitica protease
Arch. Biochem. Biophys.
149
52-61
1972
Cryphonectria parasitica
Barkholt, V.
Amino acid sequence of endothiapepsin. Complete primary structure of the aspartic protease from Endothia parasitica
Eur. J. Biochem.
167
327-338
1987
Cryphonectria parasitica
Cooper, J.; Foundling, S.; Hemmings, A.; Blundell, T.; Jones, D.M.; Hallett, A.; Szelke, M.
The structure of a synthetic pepsin inhibitor complexed with endothiapepsin
Eur. J. Biochem.
169
215-221
1987
Cryphonectria parasitica
Brown, E.D.; Wynne, M.G.; Clarke, A.J.; Yada, R.Y.
Purification of two fungal aspartic proteinases using fast protein liquid chromatography
Agric. Biol. Chem.
54
1563-1565
1990
Cryphonectria parasitica
-
Cooper, J.; Quail, W.; Frazao, C.; Foundling, S.I.; Blundell, T.L.; Humblet, C.; Lunney, E.A.; Lowther, W.T.; Dunn, B.M.
X-ray crystallographic analysis of inhibition of endothiapepsin by cyclohexyl renin inhibitors
Biochemistry
31
8142-8150
1992
Cryphonectria parasitica
Bailey, D.; Cooper, J.B.; Veerapandian, B.; Blundell, T.L.; Atrash, B.; Jones, D.M.; Szelke, M.
X-ray-crystallographic studies of complexes of pepstatin A and a statine-containing human renin inhibitor with endothiapepsin
Biochem. J.
289
363-371
1993
Cryphonectria parasitica
Veerapandian, B.; Cooper, J.B.; Sali, A.; Blundell, T.L.
X-ray analyses of aspartic proteinases. III. Three-dimensional structure of endothiapepsin complexed with a transition-state isostere inhibitor of renin at 1.6 A resolution
J. Mol. Biol.
216
1017-1029
1990
Cryphonectria parasitica
Sali, A.; Veerapandian, B.; Cooper, J.B.; Foundling, S.I.; Hoover, D.J.; Blundell, T.L.
High-resolution X-ray diffraction study of the complex between endothiapepsin and an oligopeptide inhibitor: the analysis of the inhibitor binding and description of the rigid body shift in the enzyme
EMBO J.
8
2179-2188
1989
Cryphonectria parasitica
Bailey, D.; Cooper, J.B.
A structural comparison of 21 inhibitor complexes of the aspartic proteinase from Endothia parasitica
Protein Sci.
3
2129-2143
1994
Cryphonectria parasitica
Valler, M.J.; Kay, J.; Aoyagi, T.; Dunn, B.M.
The interaction of aspartic proteinases with naturally-occurring inhibitors from actinomycetes and Ascaris lumbricoides
J. Enzyme Inhib.
1
77-82
1985
Cryphonectria parasitica
Coates, L.; Erskine, P.T.; Mall, S.; Williams, P.A.; Gill, R.S.; Wood, S.P.; Cooper, J.B.
The structure of endothiapepsin complexed with the gem-diol inhibitor PD-135,040 at 1.37 A
Acta Crystallogr. Sect. D
59
978-981
2003
Cryphonectria parasitica
Coates, L.; Erskine, P.T.; Crump, M.P.; Wood, S.P.; Cooper, J.B.
Five atomic resolution structures of endothiapepsin inhibitor complexes: implications for the aspartic proteinase mechanism
J. Mol. Biol.
318
1405-1415
2002
Cryphonectria parasitica
Cooper, J.B.
Endothiapepsin
Handbook of Proteolytic Enzymes (Barrett, J. ; Rawlings, N. D. ; Woessner, J. F. , eds. )
1
104-107
2004
Cryphonectria parasitica
-
Vidossich, P.; Carloni, P.
Binding of phosphinate and phosphonate inhibitors to aspartic proteases: a first-principles study
J. Phys. Chem. B
110
1437-1442
2006
Cryphonectria parasitica
Alexov, E.
Calculating proton uptake/release and binding free energy taking into account ionization and conformation changes induced by protein-inhibitor association: application to plasmepsin, cathepsin D and endothiapepsin-pepstatin complexes
Proteins
56
572-584
2004
Cryphonectria parasitica
Coates, L.; Erskine, P.T.; Mall, S.; Gill, R.; Wood, S.P.; Myles, D.A.; Cooper, J.B.
X-ray, neutron and NMR studies of the catalytic mechanism of aspartic proteinases
Eur. Biophys. J.
35
559-566
2006
Cryphonectria parasitica
Koester, H.; Craan, T.; Brass, S.; Herhaus, C.; Zentgraf, M.; Neumann, L.; Heine, A.; Klebe, G.
A small nonrule of 3 compatible fragment library provides high hit rate of endothiapepsin crystal structures with various fragment chemotypes
J. Med. Chem.
54
7784-7796
2011
Cryphonectria parasitica (P11838)
Mondal, M.; Radeva, N.; Fanlo-Virgos, H.; Otto, S.; Klebe, G.; Hirsch, A.K.
Fragment linking and optimization of inhibitors of the aspartic protease endothiapepsin fragment-based drug design facilitated by dynamic combinatorial chemistry
Angew. Chem. Int. Ed. Engl.
55
9422-9426
2016
Cryphonectria parasitica (P11838)
Mondal, M.; Unver, M.Y.; Pal, A.; Bakker, M.; Berrier, S.P.; Hirsch, A.K.
Fragment-based drug design facilitated by protein-templated click chemistry fragment linking and optimization of inhibitors of the aspartic protease endothiapepsin
Chemistry
22
14826-14830
2016
Cryphonectria parasitica (P11838)
Jumde, V.R.; Mondal, M.; Gierse, R.M.; Unver, M.Y.; Magari, F.; van Lier, R.C.W.; Heine, A.; Klebe, G.; Hirsch, A.K.H.
Design and synthesis of bioisosteres of acylhydrazones as stable inhibitors of the aspartic protease endothiapepsin
ChemMedChem
13
2266-2270
2018
Cryphonectria parasitica (P11838)
Hartman, A.M.; Mondal, M.; Radeva, N.; Klebe, G.; Hirsch, A.K.
Structure-based optimization of inhibitors of the aspartic protease endothiapepsin
Int. J. Mol. Sci.
16
19184-19194
2015
Cryphonectria parasitica (P11838)
Radeva, N.; Krimmer, S.G.; Stieler, M.; Fu, K.; Wang, X.; Ehrmann, F.R.; Metz, A.; Huschmann, F.U.; Weiss, M.S.; Mueller, U.; Schiebel, J.; Heine, A.; Klebe, G.
Experimental active-site mapping by fragments hot spots remote from the catalytic center of endothiapepsin
J. Med. Chem.
59
7561-7575
2016
Cryphonectria parasitica (P11838)
Radeva, N.; Schiebel, J.; Wang, X.; Krimmer, S.G.; Fu, K.; Stieler, M.; Ehrmann, F.R.; Metz, A.; Rickmeyer, T.; Betz, M.; Winquist, J.; Park, A.Y.; Huschmann, F.U.; Weiss, M.S.; Mueller, U.; Heine, A.; Klebe, G.
Active site mapping of an aspartic protease by multiple fragment crystal structures versatile warheads to address a catalytic dyad
J. Med. Chem.
59
9743-9759
2016
Cryphonectria parasitica (P11838)
Mondal, M.; Groothuis, D.; Hirsch, A.
Fragment growing exploiting dynamic combinatorial chemistry of inhibitors of the aspartic protease endothiapepsin
MedChemComm
6
1267-1271
2015
Cryphonectria parasitica (P11838)
-
EXTERNAL LINKS (specific for EC-Number 3.4.23.22)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
