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3.4.23.22: Endothiapepsin

This is an abbreviated version!
For detailed information about Endothiapepsin, go to the full flat file.

Word Map on EC 3.4.23.22

Reaction

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

Aspartate protease, Aspartic proteinase, EC 3.4.23.10, EC 3.4.23.6, EC 3.4.4.17, Endothia acid proteinase, Endothia aspartic proteinase, Endothia parasitica acid proteinase, Endothia parasitica aspartic proteinase, Proteinase, Endothia aspartic

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.23 Aspartic endopeptidases
                3.4.23.22 Endothiapepsin

Reference

topprint

Reference on EC 3.4.23.22 - Endothiapepsin

Please use the Reference Search for a specific query.
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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
Manually annotated by BRENDA team
Whitaker, J.R.
Protease of Endothia parasitica
Methods Enzymol.
19
436-445
1970
Cryphonectria parasitica
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Cooper, J.B.; Myles, D.A.
A preliminary neutron Laue diffraction study of the aspartic proteinase endothiapepsin
Acta Crystallogr. Sect. D
56
246-248
2000
Endothia sp.
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Coates, L.; Erskine, P.T.; Wood, S.P.; Myles, D.A.; Cooper, J.B.
A neutron Laue diffraction study of endothiapepsin: implications for the aspartic proteinase mechanism
Biochemistry
40
13149-13157
2001
Endothia sp.
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Stultz, C.M.; Karplus, M.
Dynamic ligand design and combinatorial optimization: designing inhibitors to endothiapepsin
Proteins
40
258-289
2000
Endothia sp.
Manually annotated by BRENDA team
Cooper, J.B.
Endothiapepsin
Handbook of Proteolytic Enzymes (Barrett, J. ; Rawlings, N. D. ; Woessner, J. F. , eds. )
1
104-107
2004
Cryphonectria parasitica
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
-
Manually annotated by BRENDA team