D00436
type: Enzyme
rlcp: p966
cath: Cathepsin D, subunit A; domain 1
ec: https://purl.uniprot.org/enzyme/3.4.23.1
uniprot: P00791
uniprot: P0DJD9
kegg enzyme: pepsin A
kegg substrate: Peptide
kegg substrate: Protein
kegg substrate: H2O
kegg product: Peptide
kegg product: Protein
kegg intermediate: Amino-diol-tetrahedral intermediate
pdb: 1f34A01
pdb: 1psaA01
pdb: 1psaB01
pdb: 1yx9A01
pdb: 2psgA01
pdb: 3pepA01
pdb: 3psgA01
pdb: 4pepA01
pdb: 5pepA01
pdb: 1flhA01
pdb: 1psnA01
pdb: 1psoE01
pdb: 1qrpE01
pdb: 3utlA01
pdb: 1f34A02
pdb: 1psaA02
pdb: 1psaB02
pdb: 1yx9A02
pdb: 2psgA02
pdb: 3pepA02
pdb: 3psgA02
pdb: 4pepA02
pdb: 5pepA02
pdb: 1flhA02
pdb: 1psnA02
pdb: 1psoE02
pdb: 1qrpE02
pdb: 3utlA02
references: An aspartic acid residue at the active site of pepsin. The isolation and sequence of the heptapeptide.
references: Disulfide bonds of pepsinogen and pepsin: identification of the disulfide bonds which can be reversibly reduced and reoxidized.
references: The pepsin catalysed hydrolysis of bis-P-nitrophenyl sulfite.
references: Evidence for an acyl intermediate in pepsin-catalysed reactions.
references: Acyl and amino intermediates in reactions catalysed by pig pepsin. Analysis of transpeptidation products.
references: X-ray crystallographic studies of pepsin.
references: Mechanism of pepsin catalysis: general base catalysis by the active-site carboxylate ion.
references: The effect of polycations on the activity of pepsin.
references: http://ezcatdb.cbrc.jp/EzCatDB/reference/D00436#9
references: Binding of a reduced peptide inhibitor to the aspartic proteinase from Rhizopus chinensis: implications for a mechanism of action.
references: A reversible unfolding reaction of swine pepsin; implications for pepsinogen's folding mechanism.
references: X-ray analyses of aspartic proteinases. II. Three-dimensional structure of the hexagonal crystal form of porcine pepsin at 2.3 A resolution.
references: Molecular and crystal structures of monoclinic porcine pepsin refined at 1.8 A resolution.
references: Revised 2.3 A structure of porcine pepsin: evidence for a flexible subdomain.
references: Why does pepsin have a negative charge at very low pH? An analysis of conserved charged residues in aspartic proteinases.
references: The number of cooperative regions (energetic domains) in a pepsin molecule depends on the pH of the medium.
references: Pepsin-catalyzed peptide synthesis in biphasic systems.
references: Pepsin behavior as a catalyst in equilibrium-controlled peptide synthesis.
references: Refined structure of porcine pepsinogen at 1.8 A resolution.
references: Structure of a pepsin/renin inhibitor complex reveals a novel crystal packing induced by minor chemical alterations in the inhibitor.
references: Pepsin as a catalyst of peptide synthesis. Enzyme co-precipitation with emerging peptide products.
references: Enzymic activities of two-chain pepsinogen, two-chain pepsin, and the amino-terminal lobe of pepsinogen.
references: pH dependence of kinetic parameters of pepsin, rhizopuspepsin, and their active-site hydrogen bond mutants.
references: The high-resolution crystal structure of porcine pepsinogen.
references: A quantum mechanical study of the active site of aspartic proteinases.
references: Conformational instability of the N- and C-terminal lobes of porcine pepsin in neutral and alkaline solutions.
references: Aspartic proteinases--Fourier transform IR studies of the aspartic carboxylic groups in the active site of pepsin.
references: Mechanism of pepsin-catalyzed aminotranspeptidation reactions.
references: Pepsin-catalyzed peptide synthesis in organic media: studies with free and immobilized enzyme.
references: A new way of looking at aspartic proteinase structures: a comparison of pepsin structure to other aspartic proteinases in the near active site region.
references: Evidence for electrostatic interactions in the S2 subsite of porcine pepsin.
references: Raising the pH of the pepsin-catalysed hydrolysis of bovine whey proteins increases the antigenicity of the hydrolysates.
references: The sole lysine residue in porcine pepsin works as a key residue for catalysis and conformational flexibility.
references: Restrained molecular dynamics study of the interaction between bovine kappa-casein peptide 98-111 and bovine chymosin and porcine pepsin.
references: Crystal structure of human pepsin and its complex with pepstatin.
references: Proteinase-catalyzed peptide synthesis in concentrated solutions of urea and other denaturing agents.
references: Engineering of porcine pepsin. Alteration of S1 substrate specificity of pepsin to those of fungal aspartic proteinases by site-directed mutagenesis.
references: Structure and proposed amino-acid sequence of a pepsin from atlantic cod (Gadus morhua).
references: Pepsin as a catalyst for peptide synthesis: formation of peptide bonds not typical for pepsin substrate specificity.

Cathepsin D, subunit A; domain 1
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/2.40.70.10
catalytic domain: index.html

Peptide
type: KeggSubstrate
references: KEGG:C00012
compound type: peptide/protein
type: KeggProduct

Protein
type: KeggSubstrate
references: KEGG:C00017
compound type: peptide/protein
type: KeggProduct

H2O
type: KeggSubstrate
references: KEGG:C00001
compound type: H2O
references: CHEBI:15377
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Amino-diol-tetrahedral intermediate
type: KeggIntermediate
references: KEGG:I00136

1f34A01
type: Pdb
references: 1f34
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1f34
catalytic residue: ASP 32

1psaA01
type: Pdb
references: 1psa
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1psa
catalytic residue: ASP 32

1psaB01
type: Pdb
references: 1psa
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1psa
catalytic residue: ASP 32

1yx9A01
type: Pdb
references: 1yx9
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1yx9
catalytic residue: ASP 32

2psgA01
type: Pdb
references: 2psg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2psg
catalytic residue: ASP 32

3pepA01
type: Pdb
references: 3pep
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3pep
catalytic residue: ASP 32

3psgA01
type: Pdb
references: 3psg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3psg
catalytic residue: ASP 32

4pepA01
type: Pdb
references: 4pep
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:4pep
catalytic residue: ASP 32

5pepA01
type: Pdb
references: 5pep
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:5pep
catalytic residue: ASP 32

1flhA01
type: Pdb
references: 1flh
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1flh
catalytic residue: ASP 32

1psnA01
type: Pdb
references: 1psn
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1psn
catalytic residue: ASP 32

1psoE01
type: Pdb
references: 1pso
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1pso
catalytic residue: ASP 32

1qrpE01
type: Pdb
references: 1qrp
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qrp
catalytic residue: ASP 32

3utlA01
type: Pdb
references: 3utl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3utl
catalytic residue: ASP 32

1f34A02
type: Pdb
references: 1f34
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1f34
catalytic residue: ASP 215

1psaA02
type: Pdb
references: 1psa
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1psa
catalytic residue: ASP 215

1psaB02
type: Pdb
references: 1psa
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1psa
catalytic residue: ASP 215

1yx9A02
type: Pdb
references: 1yx9
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1yx9
catalytic residue: ASP 215

2psgA02
type: Pdb
references: 2psg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2psg
catalytic residue: ASP 215

3pepA02
type: Pdb
references: 3pep
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3pep
catalytic residue: ASP 215

3psgA02
type: Pdb
references: 3psg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3psg
catalytic residue: ASP 215

4pepA02
type: Pdb
references: 4pep
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:4pep
catalytic residue: ASP 215

5pepA02
type: Pdb
references: 5pep
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:5pep
catalytic residue: ASP 215

1flhA02
type: Pdb
references: 1flh
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1flh
catalytic residue: ASP 215

1psnA02
type: Pdb
references: 1psn
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1psn
catalytic residue: ASP 215

1psoE02
type: Pdb
references: 1pso
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1pso
catalytic residue: ASP 215

1qrpE02
type: Pdb
references: 1qrp
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qrp
catalytic residue: ASP 215

3utlA02
type: Pdb
references: 3utl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3utl
catalytic residue: ASP 215

An aspartic acid residue at the active site of pepsin. The isolation and sequence of the heptapeptide.
type: BibliographicResource
comment: ACTIVE SITE.
medline id: 69283592
references: http://www.ncbi.nlm.nih.gov/pubmed/4897201
journal: Biochem J
volume: 113
pages: 377-86
published year: 1969
authors:
  item: Bayliss RS
  item: Knowles JR
  item: Wybrandt GB
references: P00791

Disulfide bonds of pepsinogen and pepsin: identification of the disulfide bonds which can be reversibly reduced and reoxidized.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/4940603
journal: Arch Biochem Biophys
volume: 144
pages: 59-65
published year: 1971
authors:
  item: Nakagawa Y
  item: Perlmann GE

The pepsin catalysed hydrolysis of bis-P-nitrophenyl sulfite.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/4946266
journal: Biochem Biophys Res Commun
volume: 45
pages: 293-6
published year: 1971
authors:
  item: Hubbard CD
  item: Stein TP

Evidence for an acyl intermediate in pepsin-catalysed reactions.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/4561920
journal: Biochem J
volume: 127
pages: 35P
published year: 1972
authors:
  item: Takahashi M
  item: Hofmann T

Acyl and amino intermediates in reactions catalysed by pig pepsin. Analysis of transpeptidation products.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/782445
journal: Biochem J
volume: 153
pages: 691-9
published year: 1976
authors:
  item: Wang TT
  item: Hofmann T

X-ray crystallographic studies of pepsin.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY.
medline id: 78077917
references: http://www.ncbi.nlm.nih.gov/pubmed/339692
journal: Adv Exp Med Biol
volume: 95
pages: 23-31
published year: 1977
authors:
  item: Andreeva NS
  item: Gustchina AE
  item: Fedorov AA
  item: Shutzkever NE
  item: Volnova TV
references: P00791

Mechanism of pepsin catalysis: general base catalysis by the active-site carboxylate ion.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/346376
journal: FEBS Lett
volume: 88
pages: 87-90
published year: 1978
authors:
  item: Antonov VK
  item: Ginodman LM
  item: Kapitannikov YV
  item: Barshevskaya TN
  item: Gurova AG
  item: Rumsh LD

The effect of polycations on the activity of pepsin.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/2862261
journal: J Pharm Pharmacol
volume: 37
pages: 396-400
published year: 1985
authors:
  item: Lawton JB
  item: Mekas CI

http://ezcatdb.cbrc.jp/EzCatDB/reference/D00436#9
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/3109484
journal: Biochim Biophys Acta
volume: 913
pages: 122-30
published year: 1987
authors:
  item: Dunn BM
  item: Valler MJ
  item: Rolph CE
  item: Foundling SI
  item: Jimenez M
  item: 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.

Binding of a reduced peptide inhibitor to the aspartic proteinase from Rhizopus chinensis: implications for a mechanism of action.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/3313384
journal: Proc Natl Acad Sci U S A
volume: 84
pages: 7009-13
published year: 1987
authors:
  item: Suguna K
  item: Padlan EA
  item: Smith CW
  item: Carlson WD
  item: Davies DR

A reversible unfolding reaction of swine pepsin; implications for pepsinogen's folding mechanism.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/2492190
journal: Biochem Biophys Res Commun
volume: 158
pages: 115-9
published year: 1989
authors:
  item: McPhie P

X-ray analyses of aspartic proteinases. II. Three-dimensional structure of the hexagonal crystal form of porcine pepsin at 2.3 A resolution.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
medline id: 90317821
references: http://www.ncbi.nlm.nih.gov/pubmed/2115088
journal: J Mol Biol
volume: 214
pages: 199-222
published year: 1990
authors:
  item: Cooper JB
  item: Khan G
  item: Taylor G
  item: Tickle IJ
  item: Blundell TL
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P00791

Molecular and crystal structures of monoclinic porcine pepsin refined at 1.8 A resolution.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/2115087
journal: J Mol Biol
volume: 214
pages: 143-70
published year: 1990
authors:
  item: Sielecki AR
  item: Fedorov AA
  item: Boodhoo A
  item: Andreeva NS
  item: James MN
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Revised 2.3 A structure of porcine pepsin: evidence for a flexible subdomain.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
medline id: 91017500
references: http://www.ncbi.nlm.nih.gov/pubmed/2217165
journal: Proteins
volume: 8
pages: 62-81
published year: 1990
authors:
  item: Abad-Zapatero C
  item: Rydel TJ
  item: Erickson J
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P00791

Why does pepsin have a negative charge at very low pH? An analysis of conserved charged residues in aspartic proteinases.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1812734
journal: Adv Exp Med Biol
volume: 306
pages: 39-45
published year: 1991
authors:
  item: Andreeva NS
  item: James MN

The number of cooperative regions (energetic domains) in a pepsin molecule depends on the pH of the medium.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/2065096
journal: Biochim Biophys Acta
volume: 1078
pages: 283-8
published year: 1991
authors:
  item: Makarov AA
  item: Protasevich II
  item: Frank EG
  item: Grishina IB
  item: Bolotina IA
  item: Esipova NG

Pepsin-catalyzed peptide synthesis in biphasic systems.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1820069
journal: Biomed Biochim Acta
volume: 50
pages: S94-7
published year: 1991
authors:
  item: Bemquerer MP
  item: Theobaldo FC
  item: Tominaga M

Pepsin behavior as a catalyst in equilibrium-controlled peptide synthesis.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1820070
journal: Biomed Biochim Acta
volume: 50
pages: S98-101
published year: 1991
authors:
  item: Filippova IYu
  item: Lysogorskaya EN
  item: Anisimova VV
  item: Abdel Malak CA
  item: Lavrenova GI
  item: Stepanov VM

Refined structure of porcine pepsinogen at 1.8 A resolution.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
medline id: 91278095
references: http://www.ncbi.nlm.nih.gov/pubmed/2056534
journal: J Mol Biol
volume: 219
pages: 671-92
published year: 1991
authors:
  item: Sielecki AR
  item: Fujinaga M
  item: Read RJ
  item: James MN
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P00791

Structure of a pepsin/renin inhibitor complex reveals a novel crystal packing induced by minor chemical alterations in the inhibitor.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/1418819
journal: Acta Crystallogr B
volume: 48
pages: 476-88
published year: 1992
authors:
  item: Chen L
  item: Erickson JW
  item: Rydel TJ
  item: Park CH
  item: Neidhart D
  item: Luly J
  item: Abad-Zapatero C
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Pepsin as a catalyst of peptide synthesis. Enzyme co-precipitation with emerging peptide products.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1428533
journal: Int J Pept Protein Res
volume: 39
pages: 443-9
published year: 1992
authors:
  item: Abdel Malak C
  item: Filippova IY
  item: Lysogorskaya EN
  item: Anisimova VV
  item: Lavrenova GI
  item: Stepanov VM

Enzymic activities of two-chain pepsinogen, two-chain pepsin, and the amino-terminal lobe of pepsinogen.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1512263
journal: J Biol Chem
volume: 267
pages: 17257-63
published year: 1992
authors:
  item: Lin XL
  item: Lin YZ
  item: Koelsch G
  item: Gustchina A
  item: Wlodawer A
  item: Tang J

pH dependence of kinetic parameters of pepsin, rhizopuspepsin, and their active-site hydrogen bond mutants.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1526982
journal: J Biol Chem
volume: 267
pages: 18413-8
published year: 1992
authors:
  item: Lin Y
  item: Fusek M
  item: Lin X
  item: Hartsuck JA
  item: Kezdy FJ
  item: Tang J

The high-resolution crystal structure of porcine pepsinogen.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
medline id: 92279205
references: http://www.ncbi.nlm.nih.gov/pubmed/1594574
journal: Proteins
volume: 13
pages: 1-25
published year: 1992
authors:
  item: Hartsuck JA
  item: Koelsch G
  item: Remington SJ
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P00791

A quantum mechanical study of the active site of aspartic proteinases.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8461297
journal: Biochemistry
volume: 32
pages: 3325-33
published year: 1993
authors:
  item: Beveridge AJ
  item: Heywood GC

Conformational instability of the N- and C-terminal lobes of porcine pepsin in neutral and alkaline solutions.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8401224
journal: Protein Sci
volume: 2
pages: 1383-90
published year: 1993
authors:
  item: Lin X
  item: Loy JA
  item: Sussman F
  item: Tang J

Aspartic proteinases--Fourier transform IR studies of the aspartic carboxylic groups in the active site of pepsin.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7925992
journal: FEBS Lett
volume: 352
pages: 315-7
published year: 1994
authors:
  item: Iliadis G
  item: Zundel G
  item: Brzezinski B

Mechanism of pepsin-catalyzed aminotranspeptidation reactions.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8138045
journal: Int J Biochem
volume: 26
pages: 35-42
published year: 1994
authors:
  item: Balbaa M
  item: Blum M
  item: Hofmann T

Pepsin-catalyzed peptide synthesis in organic media: studies with free and immobilized enzyme.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7896503
journal: Int J Pept Protein Res
volume: 44
pages: 448-56
published year: 1994
authors:
  item: Bemquerer MP
  item: Adlercreutz P
  item: Tominaga M

A new way of looking at aspartic proteinase structures: a comparison of pepsin structure to other aspartic proteinases in the near active site region.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8540318
journal: Adv Exp Med Biol
volume: 362
pages: 19-32
published year: 1995
authors:
  item: Andreeva NS
  item: Bochkarev A
  item: Pechik I

Evidence for electrostatic interactions in the S2 subsite of porcine pepsin.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8540385
journal: Adv Exp Med Biol
volume: 362
pages: 91-4
published year: 1995
authors:
  item: Rao C
  item: Dunn BM

Raising the pH of the pepsin-catalysed hydrolysis of bovine whey proteins increases the antigenicity of the hydrolysates.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8556555
journal: Clin Exp Allergy
volume: 25
pages: 1007-17
published year: 1995
authors:
  item: Schmidt DG
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Restrained molecular dynamics study of the interaction between bovine kappa-casein peptide 98-111 and bovine chymosin and porcine pepsin.
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Engineering of porcine pepsin. Alteration of S1 substrate specificity of pepsin to those of fungal aspartic proteinases by site-directed mutagenesis.
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Structure and proposed amino-acid sequence of a pepsin from atlantic cod (Gadus morhua).
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Pepsin as a catalyst for peptide synthesis: formation of peptide bonds not typical for pepsin substrate specificity.
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The role of the flap residue, threonine 77, in the activation and catalytic activity of pepsin A.
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Structural study of the complex between human pepsin and a phosphorus-containing peptidic -transition-state analog.
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The pepsin residue glycine-76 contributes to active-site loop flexibility and participates in catalysis.
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Structural basis for the inhibition of porcine pepsin by Ascaris pepsin inhibitor-3.
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Structure of human uropepsin at 2.45 A resolution.
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N-terminal portion acts as an initiator of the inactivation of pepsin at neutral pH.
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Analysis of crystal structures of aspartic proteinases: on the role of amino acid residues adjacent to the catalytic site of pepsin-like enzymes.
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A history of pepsin and related enzymes.
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Effect of dimethyl sulphoxide on the crystal structure of porcine pepsin.
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An analysis of subdomain orientation, conformational change and disorder in relation to crystal packing of aspartic proteinases.
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pepsin
type: KeggEnzyme

lactated pepsin
type: KeggEnzyme

pepsin fortior
type: KeggEnzyme

fundus-pepsin
type: KeggEnzyme

elixir lactate of pepsin
type: KeggEnzyme

P I
type: KeggEnzyme

lactated pepsin elixir
type: KeggEnzyme

P II
type: KeggEnzyme

pepsin R
type: KeggEnzyme

pepsin D
type: KeggEnzyme

Analogue
compound: Peptide
pdb: 1psaA01
ligand het code: 0ZL

Analogue
compound: Peptide
pdb: 1psaB01
ligand het code: 0ZL

Analogue
compound: Peptide
pdb: 1psoE01
ligand het code: IVA-VAL-VAL-STA-ALA-STA(chain I)

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
pdb: 1qrpE01
ligand het code: HH0

ReferenceForCatalyticMechanism
reference index: 10
reference section: Fig.5, p.7010-7012
reference step: 3

ReferenceForCatalyticMechanism
reference index: 23
reference section: p.18414-18417

ReferenceForCatalyticMechanism
reference index: 25
reference section: Fig.5, p.3331-3332
reference step: 3

ReferenceForCatalyticMechanism
reference index: 41
reference section: p.276-278

ReferenceForCatalyticMechanism
reference index: 46
reference section: Fig.6