DB code: D00441

RLCP classification 1.13.200.966 : Hydrolysis
CATH domain 2.40.70.10 : Cathepsin D, subunit A; domain 1 Catalytic domain
2.40.70.10 : Cathepsin D, subunit A; domain 1 Catalytic domain
E.C. 3.4.23.22
CSA 1eed
M-CSA 1eed
MACiE

CATH domain Related DB codes (homologues)
2.40.70.10 : Cathepsin D, subunit A; domain 1 D00471 D00436 D00438 D00439 D00440 D00442 D00443 D00437 D00444 D00423 D00445 D00484 M00206 M00166 D00231 D00529

Uniprot Enzyme Name
UniprotKB Protein name Synonyms MEROPS Pfam
P11838 Endothiapepsin
EC 3.4.23.22
Aspartate protease
A01.017 (Aspartic)
PF00026 (Asp)
[Graphical View]

KEGG enzyme name
endothiapepsin
Endothia aspartic proteinase
Endothia acid proteinase
Endothia parasitica acid proteinase
Endothia parasitica aspartic proteinase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P11838 CARP_CRYPA Hydrolysis of proteins with specificity similar to that of pepsin A, prefers hydrophobic residues at P1 and P1'', but does not cleave 14-Ala-|-Leu-15 in the B chain of insulin or Z-Glu-Tyr. Clots milk.

KEGG Pathways
Map code Pathways E.C.

Compound table
Substrates Products Intermediates
KEGG-id C00017 C00012 C00001 C00017 C00012 I00136
E.C.
Compound Protein Peptide H2O Protein Peptide Amino-diol-tetrahedral intermediate
Type peptide/protein peptide/protein H2O peptide/protein peptide/protein
ChEBI 15377
15377
PubChem 22247451
962
22247451
962
1e5oE01 Unbound Analogue:3AI Unbound Unbound Unbound
1e80E01 Unbound Unbound Unbound Unbound Transition-state-analogue:0GQ
1e81E01 Unbound Unbound Unbound Unbound Transition-state-analogue:M91
1e82E01 Unbound Unbound Unbound Unbound Transition-state-analogue:M90
1eedP01 Unbound Unbound Unbound Unbound Transition-state-analogue:0EO
1entE01 Unbound Unbound Unbound Unbound Transition-state-analogue:0EM
1eplE01 Unbound Unbound Unbound Unbound Transition-state-analogue:PRO-LEU-GLU-PSA-ARG-LEU (chain I)
1epmE01 Unbound Unbound Unbound Unbound Transition-state-analogue:THR-PHE-GLN-ALA-PSA-LEU-ARG-GLU (chain I)
1epnE01 Unbound Unbound Unbound Unbound Transition-state-analogue:2ZS
1epoE01 Unbound Unbound Unbound Unbound Transition-state-analogue:2Z3
1eppE01 Unbound Unbound Unbound Unbound Transition-state-analogue:1Z1
1epqE01 Unbound Unbound Unbound Unbound Transition-state-analogue:0QF
1eprE01 Unbound Unbound Unbound Unbound Transition-state-analogue:0QS
1er8E01 Unbound Analogue:DHI-PRO-PHE-HIS-LEU-LEU-VAL-TYR (chain I) Unbound Unbound Unbound
1gktA01 Unbound Unbound Unbound Unbound Transition-state-analogue:BOC-HIS-PRO-PHE-HIS-LOV-ILE-HIS (chain B)
1gvtA01 Unbound Unbound Unbound Unbound Transition-state-analogue:2ZS
1gvuA01 Unbound Unbound Unbound Unbound Transition-state-analogue:PRO-PHE-HIS-STA-VAL-ILE (chain I)
1gvvA01 Unbound Unbound Unbound Unbound Transition-state-analogue:0GM
1gvwA01 Unbound Unbound Unbound Unbound Transition-state-analogue:0EM
1gvxA01 Unbound Analogue:PRO-THR-GLU-PUK-ARG-GLU (chain I) Unbound Unbound Unbound
1od1A01 Unbound Unbound Unbound Unbound Transition-state-analogue:0QS
1oewA01 Unbound Unbound Unbound Bound:SER-THR Unbound
1oexA01 Unbound Unbound Unbound Unbound Transition-state-analogue:BOC-HIS-PRO-PHE-ALA-LOV-ILE-HIS (chain B)
2er0E01 Unbound Unbound Unbound Unbound Transition-state-analogue:IVA-HIS-PRO-PHE-HIS-CHS-LEU-PHE (chain I)
2er6E01 Unbound Analogue:PRO-THR-GLU-PHE-PUK-ARG-GLU (chain I) Unbound Unbound Unbound
2er7E01 Unbound Unbound Unbound Unbound Transition-state-analogue:BOC-HIS-PRO-PHE-HIS-LOV-ILE-HIS (chain I)
2er9E01 Unbound Unbound Unbound Unbound Transition-state-analogue:BOC-HIS-PRO-PHE-HIS-STA-LEU-PHE (chain I)
3er3E01 Unbound Unbound Unbound Unbound Transition-state-analogue:0EL
3er5E01 Unbound Unbound Unbound Unbound Transition-state-analogue:PRO-HIS-PRO-PHE-HIS-STA-VAL-ILE-HIS-LYS (chain I)
4apeA01 Unbound Unbound Unbound Unbound Unbound
4er1E01 Unbound Unbound Unbound Unbound Transition-state-analogue:0ZP
4er2E01 Unbound Unbound Unbound Unbound Transition-state-analogue:IVA-VAL-VAL-STA-ALA-STA (chain I)
4er4E01 Unbound Analogue:PRO-HIS-PRO-PHE-HIS-LAV-ILE-HIS-LYS (chain I) Unbound Unbound Unbound
5er1E01 Unbound Unbound Unbound Unbound Transition-state-analogue:0HT
5er2E01 Unbound Unbound Unbound Unbound Transition-state-analogue:0EK
1e5oE02 Unbound Unbound Unbound Unbound Unbound
1e80E02 Unbound Unbound Unbound Unbound Unbound
1e81E02 Unbound Unbound Unbound Unbound Unbound
1e82E02 Unbound Unbound Unbound Unbound Unbound
1eedP02 Unbound Unbound Unbound Unbound Unbound
1entE02 Unbound Unbound Unbound Unbound Unbound
1eplE02 Unbound Unbound Unbound Unbound Unbound
1epmE02 Unbound Unbound Unbound Unbound Unbound
1epnE02 Unbound Unbound Unbound Unbound Unbound
1epoE02 Unbound Unbound Unbound Unbound Unbound
1eppE02 Unbound Unbound Unbound Unbound Unbound
1epqE02 Unbound Unbound Unbound Unbound Unbound
1eprE02 Unbound Unbound Unbound Unbound Unbound
1er8E02 Unbound Unbound Unbound Unbound Unbound
1gktA02 Unbound Unbound Unbound Unbound Unbound
1gvtA02 Unbound Unbound Unbound Unbound Unbound
1gvuA02 Unbound Unbound Unbound Unbound Unbound
1gvvA02 Unbound Unbound Unbound Unbound Unbound
1gvwA02 Unbound Unbound Unbound Unbound Unbound
1gvxA02 Unbound Unbound Unbound Unbound Unbound
1od1A02 Unbound Unbound Unbound Unbound Unbound
1oewA02 Unbound Unbound Unbound Unbound Unbound
1oexA02 Unbound Unbound Unbound Unbound Unbound
2er0E02 Unbound Unbound Unbound Unbound Unbound
2er6E02 Unbound Unbound Unbound Unbound Unbound
2er7E02 Unbound Unbound Unbound Unbound Unbound
2er9E02 Unbound Unbound Unbound Unbound Unbound
3er3E02 Unbound Unbound Unbound Unbound Unbound
3er5E02 Unbound Unbound Unbound Unbound Unbound
4apeA02 Unbound Unbound Unbound Unbound Unbound
4er1E02 Unbound Unbound Unbound Unbound Unbound
4er2E02 Unbound Unbound Unbound Unbound Unbound
4er4E02 Unbound Unbound Unbound Unbound Unbound
5er1E02 Unbound Unbound Unbound Unbound Unbound
5er2E02 Unbound Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
Swiss-prot;P11838, literature [24]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1e5oE01 ASP 32
1e80E01 ASP 32
1e81E01 ASP 32
1e82E01 ASP 32
1eedP01 ASP 32
1entE01 ASP 32
1eplE01 ASP 32
1epmE01 ASP 32
1epnE01 ASP 32
1epoE01 ASP 32
1eppE01 ASP 32
1epqE01 ASP 32
1eprE01 ASP 32
1er8E01 ASP 32
1gktA01 ASP 35
1gvtA01 ASP 35
1gvuA01 ASP 35
1gvvA01 ASP 35
1gvwA01 ASP 35
1gvxA01 ASP 35
1od1A01 ASP 35
1oewA01 ASP 35
1oexA01 ASP 35
2er0E01 ASP 32
2er6E01 ASP 32
2er7E01 ASP 32
2er9E01 ASP 32
3er3E01 ASP 32
3er5E01 ASP 32
4apeA01 ASP 32
4er1E01 ASP 32
4er2E01 ASP 32
4er4E01 ASP 32
5er1E01 ASP 32
5er2E01 ASP 32
1e5oE02 ASP 215
1e80E02 ASP 215
1e81E02 ASP 215
1e82E02 ASP 215
1eedP02 ASP 215
1entE02 ASP 215
1eplE02 ASP 215
1epmE02 ASP 215
1epnE02 ASP 215
1epoE02 ASP 215
1eppE02 ASP 215
1epqE02 ASP 215
1eprE02 ASP 215
1er8E02 ASP 215
1gktA02 ASP 219
1gvtA02 ASP 219
1gvuA02 ASP 219
1gvvA02 ASP 219
1gvwA02 ASP 219
1gvxA02 ASP 219
1od1A02 ASP 219
1oewA02 ASP 218
1oexA02 ASP 218
2er0E02 ASP 215
2er6E02 ASP 215
2er7E02 ASP 215
2er9E02 ASP 215
3er3E02 ASP 215
3er5E02 ASP 215
4apeA02 ASP 215
4er1E02 ASP 215
4er2E02 ASP 215
4er4E02 ASP 215
5er1E02 ASP 215
5er2E02 ASP 215

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[6]
Fig.3, p.11
[20]
Fig.3, p.272
[24]
Fig.4, p.325-326
[28]
Fig.5
[29]
Fig.2, Fig.7, Fig.8
[34]
Fig.2, p.324
[39]
Fig.1
[40]
Fig.1
[41]
Fig.2
[42]
Fig.7

References
[1]
Resource
Comments X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
Medline ID 77148881
PubMed ID 322132
Journal Proc Natl Acad Sci U S A
Year 1977
Volume 74
Pages 556-9
Authors Subramanian E, Swan ID, Liu M, Davies DR, Jenkins JA, Tickle IJ, Blundell TL
Title Homology among acid proteases: comparison of crystal structures at 3A resolution of acid proteases from Rhizopus chinensis and Endothia parasitica.
Related PDB
Related UniProtKB P11838
[2]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 6381096
Journal FEBS Lett
Year 1984
Volume 174
Pages 96-101
Authors Pearl L, Blundell T
Title The active site of aspartic proteinases.
Related PDB 1er8 3er3 3er5 4ape 4er1 4er2
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 3912234
Journal Biochem Soc Trans
Year 1985
Volume 13
Pages 1036-41
Authors Hemmings AM, Foundling SI, Sibanda BL, Wood SP, Pearl LH, Blundell T
Title Energy calculations on aspartic proteinases: human renin, endothiapepsin and its complex with an angiotensinogen fragment analogue, H-142.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 3109484
Journal Biochim Biophys Acta
Year 1987
Volume 913
Pages 122-30
Authors Dunn BM, Valler MJ, Rolph CE, Foundling SI, Jimenez M, Kay J
Title The pH dependence of the hydrolysis of chromogenic substrates of the type, Lys-Pro-Xaa-Yaa-Phe-(NO2)Phe-Arg-Leu, by selected aspartic proteinases: evidence for specific interactions in subsites S3 and S2.
Related PDB
Related UniProtKB
[5]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 3119339
Journal Eur J Biochem
Year 1987
Volume 169
Pages 215-21
Authors Cooper J, Foundling S, Hemmings A, Blundell T, Jones DM, Hallett A, Szelke M
Title The structure of a synthetic pepsin inhibitor complexed with endothiapepsin.
Related PDB 2er6
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 3552727
Journal FEBS Lett
Year 1987
Volume 214
Pages 8-12
Authors Pearl LH
Title The catalytic mechanism of aspartic proteinases.
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 2485065
Journal J Cardiovasc Pharmacol
Year 1987
Volume 10 Suppl 7
Pages S59-68
Authors Foundling SI, Cooper J, Watson FE, Pearl LH, Hemmings A, Wood SP, Blundell T, Hallett A, Jones DM, Sueiras J, et al
Title Crystallographic studies of reduced bond inhibitors complexed with an aspartic proteinase.
Related PDB
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 3546346
Journal J Cell Biochem
Year 1987
Volume 33
Pages 53-63
Authors Tang J, Wong RN
Title Evolution in the structure and function of aspartic proteases.
Related PDB
Related UniProtKB
[9]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 3295561
Journal Nature
Year 1987
Volume 327
Pages 349-52
Authors Foundling SI, Cooper J, Watson FE, Cleasby A, Pearl LH, Sibanda BL, Hemmings A, Wood SP, Blundell TL, Valler MJ, et al
Title High resolution X-ray analyses of renin inhibitor-aspartic proteinase complexes.
Related PDB 4er4
Related UniProtKB
[10]
Resource
Comments
Medline ID
PubMed ID 3284587
Journal Biochemistry
Year 1988
Volume 27
Pages 1653-8
Authors Goldblum A
Title Theoretical calculations on the acidity of the active site in aspartic proteinases.
Related PDB
Related UniProtKB
[11]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID
Journal Topics in Medicinal Chemistry
Year 1988
Volume (Publisher:Royal Society Of Chemistry)
Pages 308-13
Authors Cooper, J. B., Foundling, S. I., Blundell, T. L., Arrowsmith, R. J., Harris, C. J., Champness, J. N
Title A Rational Approach to the Design of Antihypertensives. X-Ray Studies of Complexes between Aspartic Proteinases and Aminoalcohol Renin Inhibitors.
Related PDB 5er1
Related UniProtKB
[12]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 2690945
Journal Biochemistry
Year 1989
Volume 28
Pages 8596-603
Authors Cooper JB, Foundling SI, Blundell TL, Boger J, Jupp RA, Kay J
Title X-ray studies of aspartic proteinase-statine inhibitor complexes.
Related PDB 2er0 2er9
Related UniProtKB
[13]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
Medline ID 90005421
PubMed ID 2676515
Journal EMBO J
Year 1989
Volume 8
Pages 2179-88
Authors Sali A, Veerapandian B, Cooper JB, Foundling SI, Hoover DJ, Blundell TL
Title 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.
Related PDB 5er2
Related UniProtKB P11838
[14]
Resource
Comments
Medline ID
PubMed ID 2548525
Journal J Protein Chem
Year 1989
Volume 8
Pages 87-100
Authors Chen J, Barber A, Pedersen J, Brandt-Rauf PW, Carucci J, Murphy RB, Carty RP, Licht D, Pincus MR
Title Comparative X-ray crystallographic evidence for a beta-bend conformation as the active structure for peptide T in T4 receptor recognition.
Related PDB
Related UniProtKB
[15]
Resource
Comments
Medline ID
PubMed ID 2107098
Journal FEBS Lett
Year 1990
Volume 261
Pages 241-4
Authors Goldblum A
Title Modulation of the affinity of aspartic proteases by the mutated residues in active site models.
Related PDB
Related UniProtKB
[16]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
Medline ID 90189152
PubMed ID 2179568
Journal J Mol Biol
Year 1990
Volume 211
Pages 919-41
Authors Blundell TL, Jenkins JA, Sewell BT, Pearl LH, Cooper JB, Tickle IJ, Veerapandian B, Wood SP
Title X-ray analyses of aspartic proteinases. The three-dimensional structure at 2.1 A resolution of endothiapepsin.
Related PDB 1ent
Related UniProtKB P11838
[17]
Resource
Comments
Medline ID
PubMed ID 2115087
Journal J Mol Biol
Year 1990
Volume 214
Pages 143-70
Authors Sielecki AR, Fedorov AA, Boodhoo A, Andreeva NS, James MN
Title Molecular and crystal structures of monoclinic porcine pepsin refined at 1.8 A resolution.
Related PDB
Related UniProtKB
[18]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 2266553
Journal J Mol Biol
Year 1990
Volume 216
Pages 1017-29
Authors Veerapandian B, Cooper JB, Sali A, Blundell TL
Title 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.
Related PDB 2er7
Related UniProtKB
[19]
Resource
Comments
Medline ID
PubMed ID 2217165
Journal Proteins
Year 1990
Volume 8
Pages 62-81
Authors Abad-Zapatero C, Rydel TJ, Erickson J
Title Revised 2.3 A structure of porcine pepsin: evidence for a flexible subdomain.
Related PDB
Related UniProtKB
[20]
Resource
Comments
Medline ID
PubMed ID 1812716
Journal Adv Exp Med Biol
Year 1991
Volume 306
Pages 269-73
Authors Hoover DJ, Veerapandian B, Cooper JB, Damon DB, Dominy BW, Rosati RL, Blundell TL
Title X-ray analysis of a difluorostatone renin inhibitor bound as the tetrahedral hydrate to the aspartic protease endothiapepsin.
Related PDB
Related UniProtKB
[21]
Resource
Comments
Medline ID
PubMed ID 2001389
Journal Biochim Biophys Acta
Year 1991
Volume 1076
Pages 406-15
Authors Brown ED, Yada RY
Title A kinetic and equilibrium study of the denaturation of aspartic proteinases from the fungi, Endothia parasitica and Mucor miehei.
Related PDB
Related UniProtKB
[22]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 1525155
Journal Biochemistry
Year 1992
Volume 31
Pages 8142-50
Authors Cooper J, Quail W, Frazao C, Foundling SI, Blundell TL, Humblet C, Lunney EA, Lowther WT, Dunn BM
Title X-ray crystallographic analysis of inhibition of endothiapepsin by cyclohexyl renin inhibitors.
Related PDB 1eed
Related UniProtKB
[23]
Resource
Comments
Medline ID
PubMed ID 1525154
Journal Biochemistry
Year 1992
Volume 31
Pages 8125-41
Authors Parris KD, Hoover DJ, Damon DB, Davies DR
Title Synthesis and crystallographic analysis of two rhizopuspepsin inhibitor complexes.
Related PDB
Related UniProtKB
[24]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 1304340
Journal Protein Sci
Year 1992
Volume 1
Pages 322-8
Authors Veerapandian B, Cooper JB, Sali A, Blundell TL, Rosati RL, Dominy BW, Damon DB, Hoover DJ
Title Direct observation by X-ray analysis of the tetrahedral "intermediate" of aspartic proteinases.
Related PDB 1epo
Related UniProtKB
[25]
Resource
Comments
Medline ID
PubMed ID 1603805
Journal Proteins
Year 1992
Volume 12
Pages 158-70
Authors Sali A, Veerapandian B, Cooper JB, Moss DS, Hofmann T, Blundell TL
Title Domain flexibility in aspartic proteinases.
Related PDB
Related UniProtKB
[26]
Resource
Comments
Medline ID
PubMed ID 8215428
Journal Arch Biochem Biophys
Year 1993
Volume 306
Pages 297-303
Authors Balbaa M, Cunningham A, Hofmann T
Title Secondary substrate binding in aspartic proteinases: contributions of subsites S3 and S'2 to kcat.
Related PDB
Related UniProtKB
[27]
Resource
Comments
Medline ID
PubMed ID 8424781
Journal Biochem J
Year 1993
Volume 289
Pages 363-71
Authors Bailey D, Cooper JB, Veerapandian B, Blundell TL, Atrash B, Jones DM, Szelke M
Title X-ray-crystallographic studies of complexes of pepstatin A and a statine-containing human renin inhibitor with endothiapepsin.
Related PDB
Related UniProtKB
[28]
Resource
Comments
Medline ID
PubMed ID 8461297
Journal Biochemistry
Year 1993
Volume 32
Pages 3325-33
Authors Beveridge AJ, Heywood GC
Title A quantum mechanical study of the active site of aspartic proteinases.
Related PDB
Related UniProtKB
[29]
Resource
Comments
Medline ID
PubMed ID 8391019
Journal J Chem Inf Comput Sci
Year 1993
Volume 33
Pages 270-4
Authors Goldblum A, Rayan A, Fliess A, Glick M
Title Extending crystallographic information with semiempirical quantum mechanics and molecular mechanics: a case of aspartic proteinases.
Related PDB
Related UniProtKB
[30]
Resource
Comments
Medline ID
PubMed ID 8380615
Journal J Med Chem
Year 1993
Volume 36
Pages 70-80
Authors Klebe G, Abraham U
Title On the prediction of binding properties of drug molecules by comparative molecular field analysis.
Related PDB
Related UniProtKB
[31]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 8254610
Journal J Med Chem
Year 1993
Volume 36
Pages 3809-20
Authors Lunney EA, Hamilton HW, Hodges JC, Kaltenbronn JS, Repine JT, Badasso M, Cooper JB, Dealwis C, Wallace BA, Lowther WT, et al
Title Analyses of ligand binding in five endothiapepsin crystal complexes and their use in the design and evaluation of novel renin inhibitors.
Related PDB 1epp 1epq
Related UniProtKB
[32]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 7703859
Journal Protein Sci
Year 1994
Volume 3
Pages 2129-43
Authors Bailey D, Cooper JB
Title A structural comparison of 21 inhibitor complexes of the aspartic proteinase from Endothia parasitica.
Related PDB 1epl 1epm 1epn 1epr
Related UniProtKB
[33]
Resource
Comments
Medline ID
PubMed ID 7563055
Journal J Mol Biol
Year 1995
Volume 252
Pages 337-50
Authors Gomez J, Freire E
Title Thermodynamic mapping of the inhibitor site of the aspartic protease endothiapepsin.
Related PDB
Related UniProtKB
[34]
Resource
Comments
Medline ID
PubMed ID 8778779
Journal Proteins
Year 1996
Volume 24
Pages 322-34
Authors Beveridge A
Title A theoretical study of torsional flexibility in the active site of aspartic proteinases: implications for catalysis.
Related PDB
Related UniProtKB
[35]
Resource
Comments
Medline ID
PubMed ID 9135120
Journal J Mol Biol
Year 1997
Volume 267
Pages 899-915
Authors Aguilar CF, Cronin NB, Badasso M, Dreyer T, Newman MP, Cooper JB, Hoover DJ, Wood SP, Johnson MS, Blundell TL
Title The three-dimensional structure at 2.4 A resolution of glycosylated proteinase A from the lysosome-like vacuole of Saccharomyces cerevisiae.
Related PDB
Related UniProtKB
[36]
Resource
Comments
Medline ID
PubMed ID 9542997
Journal Protein Eng
Year 1997
Volume 10
Pages 1363-72
Authors Muegge I, Tao H, Warshel A
Title A fast estimate of electrostatic group contributions to the free energy of protein-inhibitor binding.
Related PDB
Related UniProtKB
[37]
Resource
Comments X-ray crystallography (Ph D Thesis 1999 London University Birkbeck College)
Medline ID
PubMed ID
Journal Crystallographic Studies
Year 1999
Volume
Pages 237 leaves
Authors Read JA
Title Refinement of Four Endothiapepsin Inhibitor Complexes. Crystallographic Studies of Cytochrome Ch from Methylobacterium Extorquens and Inhibitor Complexes of Aspartic Proteinases.
Related PDB 1e5o 1e80 1e81 1e82
Related UniProtKB
[38]
Resource
Comments
Medline ID
PubMed ID 10842341
Journal Proteins
Year 2000
Volume 40
Pages 258-89
Authors Stultz CM, Karplus M
Title Dynamic ligand design and combinatorial optimization: designing inhibitors to endothiapepsin.
Related PDB
Related UniProtKB
[39]
Resource
Comments Neutron diffraction
Medline ID
PubMed ID 11683623
Journal Biochemistry
Year 2001
Volume 40
Pages 13149-57
Authors Coates L, Erskine PT, Wood SP, Myles DA, Cooper JB
Title A neutron Laue diffraction study of endothiapepsin: implications for the aspartic proteinase mechanism.
Related PDB 1gkt
Related UniProtKB
[40]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 12083527
Journal J Mol Biol
Year 2002
Volume 318
Pages 1405-15
Authors Coates L, Erskine PT, Crump MP, Wood SP, Cooper JB
Title Five atomic resolution structures of endothiapepsin inhibitor complexes: implications for the aspartic proteinase mechanism.
Related PDB 1gvt 1gvu 1gvv 1gvw 1gvx
Related UniProtKB
[41]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 12777758
Journal Acta Crystallogr D Biol Crystallogr
Year 2003
Volume 59
Pages 978-81
Authors Coates L, Erskine PT, Mall S, Williams PA, Gill RS, Wood SP, Cooper JB
Title The structure of endothiapepsin complexed with the gem-diol inhibitor PD-135,040 at 1.37 A.
Related PDB 1od1
Related UniProtKB
[42]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 12876323
Journal Protein Sci
Year 2003
Volume 12
Pages 1741-9
Authors Erskine PT, Coates L, Mall S, Gill RS, Wood SP, Myles DA, Cooper JB
Title Atomic resolution analysis of the catalytic site of an aspartic proteinase and an unexpected mode of binding by short peptides.
Related PDB 1oew 1oex
Related UniProtKB
[43]
Resource
Comments
Medline ID
PubMed ID 15229889
Journal Proteins
Year 2004
Volume 56
Pages 572-84
Authors Alexov E
Title 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.
Related PDB
Related UniProtKB

Comments
This enzyme belongs to the peptidase family-A1.
As it has a catalytic dyad, composed of two aspartic acid residues, it must have a similar mechanism to that of pepsin (D00436 in EzCatDB).

Created Updated
2005-02-15 2012-07-03