EzCatDB: D00441
Related links:    PDB-formatted query search system Fasta-formatted query search system Fasta-formatted query search system

DB codeD00441
RLCP classification1.13.200.966 : Hydrolysis
CATH domainDomain 12.40.70.10 : Cathepsin D, subunit A; domain 1Catalytic domain
Domain 22.40.70.10 : Cathepsin D, subunit A; domain 1Catalytic domain
E.C.3.4.23.22
CSA1eed

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

Enzyme Name
UniProtKBKEGG

P11838
Protein nameEndothiapepsinendothiapepsin
Endothia aspartic proteinase
Endothia acid proteinase
Endothia parasitica acid proteinase
Endothia parasitica aspartic proteinase
SynonymsEC 3.4.23.22
Aspartate protease
MEROPSA01.017 (Aspartic)
PfamPF00026 (Asp)
[Graphical view]


UniProtKB:Accession NumberP11838
Entry nameCARP_CRYPA
ActivityHydrolysis 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.
Subunit
Subcellular location
Cofactor

Compound table: links to PDB-related databases & PoSSuM

SubstratesProductsintermediates
KEGG-idC00017C00012C00001C00017C00012I00136
CompoundProteinPeptideH2OProteinPeptideAmino-diol-tetrahedral intermediate
Typepeptide/proteinpeptide/proteinH2Opeptide/proteinpeptide/protein
ChEBI

15377



PubChem

962
22247451



              
1e5oE01UnboundAnalogue:3AI UnboundUnboundUnbound
1e80E01UnboundUnbound UnboundUnboundTransition-state-analogue:0GQ
1e81E01UnboundUnbound UnboundUnboundTransition-state-analogue:M91
1e82E01UnboundUnbound UnboundUnboundTransition-state-analogue:M90
1eedP01UnboundUnbound UnboundUnboundTransition-state-analogue:0EO
1entE01UnboundUnbound UnboundUnboundTransition-state-analogue:0EM
1eplE01UnboundUnbound UnboundUnboundTransition-state-analogue:PRO-LEU-GLU-PSA-ARG-LEU(chain I)
1epmE01UnboundUnbound UnboundUnboundTransition-state-analogue:THR-PHE-GLN-ALA-PSA-LEU-ARG-GLU(chain I)
1epnE01UnboundUnbound UnboundUnboundTransition-state-analogue:2ZS
1epoE01UnboundUnbound UnboundUnboundTransition-state-analogue:2Z3
1eppE01UnboundUnbound UnboundUnboundTransition-state-analogue:1Z1
1epqE01UnboundUnbound UnboundUnboundTransition-state-analogue:0QF
1eprE01UnboundUnbound UnboundUnboundTransition-state-analogue:0QS
1er8E01UnboundAnalogue:DHI-PRO-PHE-HIS-LEU-LEU-VAL-TYR(chain I) UnboundUnboundUnbound
1gktA01UnboundUnbound UnboundUnboundTransition-state-analogue:BOC-HIS-PRO-PHE-HIS-LOV-ILE-HIS(chain B)
1gvtA01UnboundUnbound UnboundUnboundTransition-state-analogue:2ZS
1gvuA01UnboundUnbound UnboundUnboundTransition-state-analogue:PRO-PHE-HIS-STA-VAL-ILE(chain I)
1gvvA01UnboundUnbound UnboundUnboundTransition-state-analogue:0GM
1gvwA01UnboundUnbound UnboundUnboundTransition-state-analogue:0EM
1gvxA01UnboundAnalogue:PRO-THR-GLU-PUK-ARG-GLU(chain I) UnboundUnboundUnbound
1od1A01UnboundUnbound UnboundUnboundTransition-state-analogue:0QS
1oewA01UnboundUnbound UnboundBound:SER-THRUnbound
1oexA01UnboundUnbound UnboundUnboundTransition-state-analogue:BOC-HIS-PRO-PHE-ALA-LOV-ILE-HIS(chain B)
2er0E01UnboundUnbound UnboundUnboundTransition-state-analogue:IVA-HIS-PRO-PHE-HIS-CHS-LEU-PHE(chain I)
2er6E01UnboundAnalogue:PRO-THR-GLU-PHE-PUK-ARG-GLU(chain I) UnboundUnboundUnbound
2er7E01UnboundUnbound UnboundUnboundTransition-state-analogue:BOC-HIS-PRO-PHE-HIS-LOV-ILE-HIS(chain I)
2er9E01UnboundUnbound UnboundUnboundTransition-state-analogue:BOC-HIS-PRO-PHE-HIS-STA-LEU-PHE(chain I)
3er3E01UnboundUnbound UnboundUnboundTransition-state-analogue:0EL
3er5E01UnboundUnbound UnboundUnboundTransition-state-analogue:PRO-HIS-PRO-PHE-HIS-STA-VAL-ILE-HIS-LYS(chain I)
4apeA01UnboundUnbound UnboundUnboundUnbound
4er1E01UnboundUnbound UnboundUnboundTransition-state-analogue:0ZP
4er2E01UnboundUnbound UnboundUnboundTransition-state-analogue:IVA-VAL-VAL-STA-ALA-STA(chain I)
4er4E01UnboundAnalogue:PRO-HIS-PRO-PHE-HIS-LAV-ILE-HIS-LYS(chain I) UnboundUnboundUnbound
5er1E01UnboundUnbound UnboundUnboundTransition-state-analogue:0HT
5er2E01UnboundUnbound UnboundUnboundTransition-state-analogue:0EK
1e5oE02UnboundUnbound UnboundUnboundUnbound
1e80E02UnboundUnbound UnboundUnboundUnbound
1e81E02UnboundUnbound UnboundUnboundUnbound
1e82E02UnboundUnbound UnboundUnboundUnbound
1eedP02UnboundUnbound UnboundUnboundUnbound
1entE02UnboundUnbound UnboundUnboundUnbound
1eplE02UnboundUnbound UnboundUnboundUnbound
1epmE02UnboundUnbound UnboundUnboundUnbound
1epnE02UnboundUnbound UnboundUnboundUnbound
1epoE02UnboundUnbound UnboundUnboundUnbound
1eppE02UnboundUnbound UnboundUnboundUnbound
1epqE02UnboundUnbound UnboundUnboundUnbound
1eprE02UnboundUnbound UnboundUnboundUnbound
1er8E02UnboundUnbound UnboundUnboundUnbound
1gktA02UnboundUnbound UnboundUnboundUnbound
1gvtA02UnboundUnbound UnboundUnboundUnbound
1gvuA02UnboundUnbound UnboundUnboundUnbound
1gvvA02UnboundUnbound UnboundUnboundUnbound
1gvwA02UnboundUnbound UnboundUnboundUnbound
1gvxA02UnboundUnbound UnboundUnboundUnbound
1od1A02UnboundUnbound UnboundUnboundUnbound
1oewA02UnboundUnbound UnboundUnboundUnbound
1oexA02UnboundUnbound UnboundUnboundUnbound
2er0E02UnboundUnbound UnboundUnboundUnbound
2er6E02UnboundUnbound UnboundUnboundUnbound
2er7E02UnboundUnbound UnboundUnboundUnbound
2er9E02UnboundUnbound UnboundUnboundUnbound
3er3E02UnboundUnbound UnboundUnboundUnbound
3er5E02UnboundUnbound UnboundUnboundUnbound
4apeA02UnboundUnbound UnboundUnboundUnbound
4er1E02UnboundUnbound UnboundUnboundUnbound
4er2E02UnboundUnbound UnboundUnboundUnbound
4er4E02UnboundUnbound UnboundUnboundUnbound
5er1E02UnboundUnbound UnboundUnboundUnbound
5er2E02UnboundUnbound UnboundUnboundUnbound

Active-site residues
resource
Swiss-prot;P11838, literature [24]
pdbCatalytic residues
         
1e5oE01ASP 32
1e80E01ASP 32
1e81E01ASP 32
1e82E01ASP 32
1eedP01ASP 32
1entE01ASP 32
1eplE01ASP 32
1epmE01ASP 32
1epnE01ASP 32
1epoE01ASP 32
1eppE01ASP 32
1epqE01ASP 32
1eprE01ASP 32
1er8E01ASP 32
1gktA01ASP 35
1gvtA01ASP 35
1gvuA01ASP 35
1gvvA01ASP 35
1gvwA01ASP 35
1gvxA01ASP 35
1od1A01ASP 35
1oewA01ASP 35
1oexA01ASP 35
2er0E01ASP 32
2er6E01ASP 32
2er7E01ASP 32
2er9E01ASP 32
3er3E01ASP 32
3er5E01ASP 32
4apeA01ASP 32
4er1E01ASP 32
4er2E01ASP 32
4er4E01ASP 32
5er1E01ASP 32
5er2E01ASP 32
1e5oE02ASP 215
1e80E02ASP 215
1e81E02ASP 215
1e82E02ASP 215
1eedP02ASP 215
1entE02ASP 215
1eplE02ASP 215
1epmE02ASP 215
1epnE02ASP 215
1epoE02ASP 215
1eppE02ASP 215
1epqE02ASP 215
1eprE02ASP 215
1er8E02ASP 215
1gktA02ASP 219
1gvtA02ASP 219
1gvuA02ASP 219
1gvvA02ASP 219
1gvwA02ASP 219
1gvxA02ASP 219
1od1A02ASP 219
1oewA02ASP 218
1oexA02ASP 218
2er0E02ASP 215
2er6E02ASP 215
2er7E02ASP 215
2er9E02ASP 215
3er3E02ASP 215
3er5E02ASP 215
4apeA02ASP 215
4er1E02ASP 215
4er2E02ASP 215
4er4E02ASP 215
5er1E02ASP 215
5er2E02ASP 215

References for Catalytic Mechanism
ReferencesSectionsNo. 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]
CommentsX-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
Medline ID77148881
PubMed ID322132
JournalProc Natl Acad Sci U S A
Year1977
Volume74
Pages556-9
AuthorsSubramanian E, Swan ID, Liu M, Davies DR, Jenkins JA, Tickle IJ, Blundell TL
TitleHomology among acid proteases: comparison of crystal structures at 3A resolution of acid proteases from Rhizopus chinensis and Endothia parasitica.
Related UniProtKBP11838
[2]
CommentsX-ray crystallography
PubMed ID6381096
JournalFEBS Lett
Year1984
Volume174
Pages96-101
AuthorsPearl L, Blundell T
TitleThe active site of aspartic proteinases.
Related PDB1er8,3er3,3er5,4ape,4er1,4er2
[3]
PubMed ID3912234
JournalBiochem Soc Trans
Year1985
Volume13
Pages1036-41
AuthorsHemmings AM, Foundling SI, Sibanda BL, Wood SP, Pearl LH, Blundell T
TitleEnergy calculations on aspartic proteinases: human renin, endothiapepsin and its complex with an angiotensinogen fragment analogue, H-142.
[4]
PubMed ID3109484
JournalBiochim Biophys Acta
Year1987
Volume913
Pages122-30
AuthorsDunn BM, Valler MJ, Rolph CE, Foundling SI, Jimenez M, Kay J
TitleThe 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.
[5]
CommentsX-ray crystallography
PubMed ID3119339
JournalEur J Biochem
Year1987
Volume169
Pages215-21
AuthorsCooper J, Foundling S, Hemmings A, Blundell T, Jones DM, Hallett A, Szelke M
TitleThe structure of a synthetic pepsin inhibitor complexed with endothiapepsin.
Related PDB2er6
[6]
PubMed ID3552727
JournalFEBS Lett
Year1987
Volume214
Pages8-12
AuthorsPearl LH
TitleThe catalytic mechanism of aspartic proteinases.
[7]
PubMed ID2485065
JournalJ Cardiovasc Pharmacol
Year1987
Volume10 Suppl 7
PagesS59-68
AuthorsFoundling SI, Cooper J, Watson FE, Pearl LH, Hemmings A, Wood SP, Blundell T, Hallett A, Jones DM, Sueiras J, et al
TitleCrystallographic studies of reduced bond inhibitors complexed with an aspartic proteinase.
[8]
PubMed ID3546346
JournalJ Cell Biochem
Year1987
Volume33
Pages53-63
AuthorsTang J, Wong RN
TitleEvolution in the structure and function of aspartic proteases.
[9]
CommentsX-ray crystallography
PubMed ID3295561
JournalNature
Year1987
Volume327
Pages349-52
AuthorsFoundling SI, Cooper J, Watson FE, Cleasby A, Pearl LH, Sibanda BL, Hemmings A, Wood SP, Blundell TL, Valler MJ, et al
TitleHigh resolution X-ray analyses of renin inhibitor-aspartic proteinase complexes.
Related PDB4er4
[10]
PubMed ID3284587
JournalBiochemistry
Year1988
Volume27
Pages1653-8
AuthorsGoldblum A
TitleTheoretical calculations on the acidity of the active site in aspartic proteinases.
[11]
CommentsX-ray crystallography
JournalTopics in Medicinal Chemistry
Year1988
Volume(Publisher:Royal Society Of Chemistry)
Pages308-13
AuthorsCooper, J. B., Foundling, S. I., Blundell, T. L., Arrowsmith, R. J., Harris, C. J., Champness, J. N
TitleA Rational Approach to the Design of Antihypertensives. X-Ray Studies of Complexes between Aspartic Proteinases and Aminoalcohol Renin Inhibitors.
Related PDB5er1
[12]
CommentsX-ray crystallography
PubMed ID2690945
JournalBiochemistry
Year1989
Volume28
Pages8596-603
AuthorsCooper JB, Foundling SI, Blundell TL, Boger J, Jupp RA, Kay J
TitleX-ray studies of aspartic proteinase-statine inhibitor complexes.
Related PDB2er0,2er9
[13]
CommentsX-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
Medline ID90005421
PubMed ID2676515
JournalEMBO J
Year1989
Volume8
Pages2179-88
AuthorsSali A, Veerapandian B, Cooper JB, Foundling SI, Hoover DJ, Blundell TL
TitleHigh-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 PDB5er2
Related UniProtKBP11838
[14]
PubMed ID2548525
JournalJ Protein Chem
Year1989
Volume8
Pages87-100
AuthorsChen J, Barber A, Pedersen J, Brandt-Rauf PW, Carucci J, Murphy RB, Carty RP, Licht D, Pincus MR
TitleComparative X-ray crystallographic evidence for a beta-bend conformation as the active structure for peptide T in T4 receptor recognition.
[15]
PubMed ID2107098
JournalFEBS Lett
Year1990
Volume261
Pages241-4
AuthorsGoldblum A
TitleModulation of the affinity of aspartic proteases by the mutated residues in active site models.
[16]
CommentsX-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
Medline ID90189152
PubMed ID2179568
JournalJ Mol Biol
Year1990
Volume211
Pages919-41
AuthorsBlundell TL, Jenkins JA, Sewell BT, Pearl LH, Cooper JB, Tickle IJ, Veerapandian B, Wood SP
TitleX-ray analyses of aspartic proteinases. The three-dimensional structure at 2.1 A resolution of endothiapepsin.
Related PDB1ent
Related UniProtKBP11838
[17]
PubMed ID2115087
JournalJ Mol Biol
Year1990
Volume214
Pages143-70
AuthorsSielecki AR, Fedorov AA, Boodhoo A, Andreeva NS, James MN
TitleMolecular and crystal structures of monoclinic porcine pepsin refined at 1.8 A resolution.
[18]
CommentsX-ray crystallography
PubMed ID2266553
JournalJ Mol Biol
Year1990
Volume216
Pages1017-29
AuthorsVeerapandian B, Cooper JB, Sali A, Blundell TL
TitleX-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 PDB2er7
[19]
PubMed ID2217165
JournalProteins
Year1990
Volume8
Pages62-81
AuthorsAbad-Zapatero C, Rydel TJ, Erickson J
TitleRevised 2.3 A structure of porcine pepsin: evidence for a flexible subdomain.
[20]
PubMed ID1812716
JournalAdv Exp Med Biol
Year1991
Volume306
Pages269-73
AuthorsHoover DJ, Veerapandian B, Cooper JB, Damon DB, Dominy BW, Rosati RL, Blundell TL
TitleX-ray analysis of a difluorostatone renin inhibitor bound as the tetrahedral hydrate to the aspartic protease endothiapepsin.
[21]
PubMed ID2001389
JournalBiochim Biophys Acta
Year1991
Volume1076
Pages406-15
AuthorsBrown ED, Yada RY
TitleA kinetic and equilibrium study of the denaturation of aspartic proteinases from the fungi, Endothia parasitica and Mucor miehei.
[22]
CommentsX-ray crystallography
PubMed ID1525155
JournalBiochemistry
Year1992
Volume31
Pages8142-50
AuthorsCooper J, Quail W, Frazao C, Foundling SI, Blundell TL, Humblet C, Lunney EA, Lowther WT, Dunn BM
TitleX-ray crystallographic analysis of inhibition of endothiapepsin by cyclohexyl renin inhibitors.
Related PDB1eed
[23]
PubMed ID1525154
JournalBiochemistry
Year1992
Volume31
Pages8125-41
AuthorsParris KD, Hoover DJ, Damon DB, Davies DR
TitleSynthesis and crystallographic analysis of two rhizopuspepsin inhibitor complexes.
[24]
CommentsX-ray crystallography
PubMed ID1304340
JournalProtein Sci
Year1992
Volume1
Pages322-8
AuthorsVeerapandian B, Cooper JB, Sali A, Blundell TL, Rosati RL, Dominy BW, Damon DB, Hoover DJ
TitleDirect observation by X-ray analysis of the tetrahedral "intermediate" of aspartic proteinases.
Related PDB1epo
[25]
PubMed ID1603805
JournalProteins
Year1992
Volume12
Pages158-70
AuthorsSali A, Veerapandian B, Cooper JB, Moss DS, Hofmann T, Blundell TL
TitleDomain flexibility in aspartic proteinases.
[26]
PubMed ID8215428
JournalArch Biochem Biophys
Year1993
Volume306
Pages297-303
AuthorsBalbaa M, Cunningham A, Hofmann T
TitleSecondary substrate binding in aspartic proteinases: contributions of subsites S3 and S'2 to kcat.
[27]
PubMed ID8424781
JournalBiochem J
Year1993
Volume289
Pages363-71
AuthorsBailey D, Cooper JB, Veerapandian B, Blundell TL, Atrash B, Jones DM, Szelke M
TitleX-ray-crystallographic studies of complexes of pepstatin A and a statine-containing human renin inhibitor with endothiapepsin.
[28]
PubMed ID8461297
JournalBiochemistry
Year1993
Volume32
Pages3325-33
AuthorsBeveridge AJ, Heywood GC
TitleA quantum mechanical study of the active site of aspartic proteinases.
[29]
PubMed ID8391019
JournalJ Chem Inf Comput Sci
Year1993
Volume33
Pages270-4
AuthorsGoldblum A, Rayan A, Fliess A, Glick M
TitleExtending crystallographic information with semiempirical quantum mechanics and molecular mechanics: a case of aspartic proteinases.
[30]
PubMed ID8380615
JournalJ Med Chem
Year1993
Volume36
Pages70-80
AuthorsKlebe G, Abraham U
TitleOn the prediction of binding properties of drug molecules by comparative molecular field analysis.
[31]
CommentsX-ray crystallography
PubMed ID8254610
JournalJ Med Chem
Year1993
Volume36
Pages3809-20
AuthorsLunney EA, Hamilton HW, Hodges JC, Kaltenbronn JS, Repine JT, Badasso M, Cooper JB, Dealwis C, Wallace BA, Lowther WT, et al
TitleAnalyses of ligand binding in five endothiapepsin crystal complexes and their use in the design and evaluation of novel renin inhibitors.
Related PDB1epp,1epq
[32]
CommentsX-ray crystallography
PubMed ID7703859
JournalProtein Sci
Year1994
Volume3
Pages2129-43
AuthorsBailey D, Cooper JB
TitleA structural comparison of 21 inhibitor complexes of the aspartic proteinase from Endothia parasitica.
Related PDB1epl,1epm,1epn,1epr
[33]
PubMed ID7563055
JournalJ Mol Biol
Year1995
Volume252
Pages337-50
AuthorsGomez J, Freire E
TitleThermodynamic mapping of the inhibitor site of the aspartic protease endothiapepsin.
[34]
PubMed ID8778779
JournalProteins
Year1996
Volume24
Pages322-34
AuthorsBeveridge A
TitleA theoretical study of torsional flexibility in the active site of aspartic proteinases: implications for catalysis.
[35]
PubMed ID9135120
JournalJ Mol Biol
Year1997
Volume267
Pages899-915
AuthorsAguilar CF, Cronin NB, Badasso M, Dreyer T, Newman MP, Cooper JB, Hoover DJ, Wood SP, Johnson MS, Blundell TL
TitleThe three-dimensional structure at 2.4 A resolution of glycosylated proteinase A from the lysosome-like vacuole of Saccharomyces cerevisiae.
[36]
PubMed ID9542997
JournalProtein Eng
Year1997
Volume10
Pages1363-72
AuthorsMuegge I, Tao H, Warshel A
TitleA fast estimate of electrostatic group contributions to the free energy of protein-inhibitor binding.
[37]
CommentsX-ray crystallography (Ph D Thesis 1999 London University Birkbeck College)
JournalCrystallographic Studies
Year1999
Volume
Pages237 leaves
AuthorsRead JA
TitleRefinement of Four Endothiapepsin Inhibitor Complexes. Crystallographic Studies of Cytochrome Ch from Methylobacterium Extorquens and Inhibitor Complexes of Aspartic Proteinases.
Related PDB1e5o,1e80,1e81,1e82
[38]
PubMed ID10842341
JournalProteins
Year2000
Volume40
Pages258-89
AuthorsStultz CM, Karplus M
TitleDynamic ligand design and combinatorial optimization: designing inhibitors to endothiapepsin.
[39]
CommentsNeutron diffraction
PubMed ID11683623
JournalBiochemistry
Year2001
Volume40
Pages13149-57
AuthorsCoates L, Erskine PT, Wood SP, Myles DA, Cooper JB
TitleA neutron Laue diffraction study of endothiapepsin: implications for the aspartic proteinase mechanism.
Related PDB1gkt
[40]
CommentsX-ray crystallography
PubMed ID12083527
JournalJ Mol Biol
Year2002
Volume318
Pages1405-15
AuthorsCoates L, Erskine PT, Crump MP, Wood SP, Cooper JB
TitleFive atomic resolution structures of endothiapepsin inhibitor complexes: implications for the aspartic proteinase mechanism.
Related PDB1gvt,1gvu,1gvv,1gvw,1gvx
[41]
CommentsX-ray crystallography
PubMed ID12777758
JournalActa Crystallogr D Biol Crystallogr
Year2003
Volume59
Pages978-81
AuthorsCoates L, Erskine PT, Mall S, Williams PA, Gill RS, Wood SP, Cooper JB
TitleThe structure of endothiapepsin complexed with the gem-diol inhibitor PD-135,040 at 1.37 A.
Related PDB1od1
[42]
CommentsX-ray crystallography
PubMed ID12876323
JournalProtein Sci
Year2003
Volume12
Pages1741-9
AuthorsErskine PT, Coates L, Mall S, Gill RS, Wood SP, Myles DA, Cooper JB
TitleAtomic resolution analysis of the catalytic site of an aspartic proteinase and an unexpected mode of binding by short peptides.
Related PDB1oew,1oex
[43]
PubMed ID15229889
JournalProteins
Year2004
Volume56
Pages572-84
AuthorsAlexov E
TitleCalculating 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.

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).

createdupdated
2005-02-152012-07-03


Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
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