D00529
type: Enzyme
rlcp: p966
cath: Cathepsin D, subunit A; domain 1
ec: https://purl.uniprot.org/enzyme/3.4.23.-
csa: 1am5
uniprot: P56272
kegg substrate: Peptide
kegg substrate: Protein
kegg substrate: H2O
kegg product: Peptide
kegg product: Protein
kegg intermediate: Amino-diol-tetrahedral intermediate
pdb: 1am5A01
pdb: 1am5A02
pdb bound state: Unbound
  compound: Peptide
  pdb: 1am5A01
pdb bound state: Unbound
  compound: Peptide
  pdb: 1am5A02
pdb bound state: Unbound
  compound: Protein
  pdb: 1am5A01
pdb bound state: Unbound
  compound: Protein
  pdb: 1am5A02
pdb bound state: Unbound
  compound: Peptide
  pdb: 1am5A01
pdb bound state: Unbound
  compound: Peptide
  pdb: 1am5A02
pdb bound state: Unbound
  compound: Protein
  pdb: 1am5A01
pdb bound state: Unbound
  compound: Protein
  pdb: 1am5A02
pdb bound state: Unbound
  compound: Amino-diol-tetrahedral intermediate
  pdb: 1am5A01
pdb bound state: Unbound
  compound: Amino-diol-tetrahedral intermediate
  pdb: 1am5A02
reference for catalytic mechanism: ReferenceForCatalyticMechanism
  reference index: 10
  reference section: Fig.5, p.7010-7012
  reference step: 3
reference for catalytic mechanism: ReferenceForCatalyticMechanism
  reference index: 23
  reference section: p.18414-18417
reference for catalytic mechanism: ReferenceForCatalyticMechanism
  reference index: 25
  reference section: Fig.5, p.3331-3332
  reference step: 3
reference for catalytic mechanism: ReferenceForCatalyticMechanism
  reference index: 41
  reference section: p.276-278
reference for catalytic mechanism: ReferenceForCatalyticMechanism
  reference index: 46
  reference section: Fig.6
references: N-terminal portion acts as an initiator of the inactivation of pepsin at neutral pH.
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/D00529#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.
references: The role of the flap residue, threonine 77, in the activation and catalytic activity of pepsin A.
references: Structural study of the complex between human pepsin and a phosphorus-containing peptidic -transition-state analog.
references: The pepsin residue glycine-76 contributes to active-site loop flexibility and participates in catalysis.
references: Structural basis for the inhibition of porcine pepsin by Ascaris pepsin inhibitor-3.
references: Structure of human uropepsin at 2.45 A resolution.
references: Analysis of crystal structures of aspartic proteinases: on the role of amino acid residues adjacent to the catalytic site of pepsin-like enzymes.
references: A history of pepsin and related enzymes.
comment: This enzyme belongs to the peptidase family-A1. This enzyme is closely related to the counter part enzyme (D00436 in EzCatDB). According to the literature [10], [25] & [41], the catalytic reaction proceeds as follows: (1) Asp215 acts as a general base, abstracting a proton from a water molecule, which is bound between Asp32 and Asp215. (2) The activated water, or the nucleophilic hydroxide ion, makes an attack on the carbonyl carbon atom of the substrate peptide bond, leading to the formation of a tetrahedral transition state with a negatively charged oxyanion (or gem-diol). (3) The protonated carboxyl sidechain of Asp32 stabilzes the negative charge of the transition state. (4) Asp215 acts as a general acid, protonating to the leaving amine group. This step leads to the cleavage of the peptide bond.

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

1am5A01
type: Pdb
references: 1am5
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1am5
catalytic residue: ASP 32

1am5A02
type: Pdb
references: 1am5
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1am5
catalytic residue: ASP 215

N-terminal portion acts as an initiator of the inactivation of pepsin at neutral pH.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11707613
journal: Protein Eng
volume: 14
pages: 669-74
published year: 2001
authors:
  item: Tanaka T
  item: Yada RY

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/D00529#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
  item: Meijer RJ
  item: Slangen CJ
  item: van Beresteijn EC

The sole lysine residue in porcine pepsin works as a key residue for catalysis and conformational flexibility.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7650014
journal: J Biol Chem
volume: 270
pages: 19974-8
published year: 1995
authors:
  item: Cottrell TJ
  item: Harris LJ
  item: Tanaka T
  item: Yada RY

Restrained molecular dynamics study of the interaction between bovine kappa-casein peptide 98-111 and bovine chymosin and porcine pepsin.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7593830
journal: J Dairy Res
volume: 62
pages: 451-67
published year: 1995
authors:
  item: Plowman JE
  item: Creamer LK

Crystal structure of human pepsin and its complex with pepstatin.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
medline id: 95392399
references: http://www.ncbi.nlm.nih.gov/pubmed/7663352
journal: Protein Sci
volume: 4
pages: 960-72
published year: 1995
authors:
  item: Fujinaga M
  item: Chernaia MM
  item: Tarasova NI
  item: Mosimann SC
  item: James MN
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P00790

Proteinase-catalyzed peptide synthesis in concentrated solutions of urea and other denaturing agents.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8907496
journal: Int J Pept Protein Res
volume: 47
pages: 28-35
published year: 1996
authors:
  item: Anisimova VV
  item: Filippova IY
  item: Lysogorskaya EN
  item: Oksenoit ES
  item: Kolobanova SV
  item: Stepanov VM

Engineering of porcine pepsin. Alteration of S1 substrate specificity of pepsin to those of fungal aspartic proteinases by site-directed mutagenesis.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9228062
journal: J Biol Chem
volume: 272
pages: 18855-61
published year: 1997
authors:
  item: Shintani T
  item: Nomura K
  item: Ichishima E

Structure and proposed amino-acid sequence of a pepsin from atlantic cod (Gadus morhua).
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/9761815
journal: Acta Crystallogr D Biol Crystallogr
volume: 54
pages: 32-46
published year: 1998
authors:
  item: Karlsen S
  item: Hough E
  item: Olsen RL
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Pepsin as a catalyst for peptide synthesis: formation of peptide bonds not typical for pepsin substrate specificity.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10408333
journal: J Pept Res
volume: 53
pages: 606-10
published year: 1999
authors:
  item: Malak CA

The role of the flap residue, threonine 77, in the activation and catalytic activity of pepsin A.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10065711
journal: Protein Eng
volume: 12
pages: 55-61
published year: 1999
authors:
  item: Okoniewska M
  item: Tanaka T
  item: Yada RY

Structural study of the complex between human pepsin and a phosphorus-containing peptidic -transition-state analog.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/10713513
journal: Acta Crystallogr D Biol Crystallogr
volume: 56
pages: 272-9
published year: 2000
authors:
  item: Fujinaga M
  item: Cherney MM
  item: Tarasova NI
  item: Bartlett PA
  item: Hanson JE
  item: James MN
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

The pepsin residue glycine-76 contributes to active-site loop flexibility and participates in catalysis.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10861225
journal: Biochem J
volume: 349
pages: 169-77
published year: 2000
authors:
  item: Okoniewska M
  item: Tanaka T
  item: Yada RY

Structural basis for the inhibition of porcine pepsin by Ascaris pepsin inhibitor-3.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/10932249
journal: Nat Struct Biol
volume: 7
pages: 653-7
published year: 2000
authors:
  item: Ng KK
  item: Petersen JF
  item: Cherney MM
  item: Garen C
  item: Zalatoris JJ
  item: Rao-Naik C
  item: Dunn BM
  item: Martzen MR
  item: Peanasky RJ
  item: James MN
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Structure of human uropepsin at 2.45 A resolution.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/11679720
journal: Acta Crystallogr D Biol Crystallogr
volume: 57
pages: 1560-70
published year: 2001
authors:
  item: Canduri F
  item: Teodoro LG
  item: Fadel V
  item: Lorenzi CC
  item: Hial V
  item: Gomes RA
  item: Neto JR
  item: de Azevedo WF Jr
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Analysis of crystal structures of aspartic proteinases: on the role of amino acid residues adjacent to the catalytic site of pepsin-like enzymes.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11714911
journal: Protein Sci
volume: 10
pages: 2439-50
published year: 2001
authors:
  item: Andreeva NS
  item: Rumsh LD

A history of pepsin and related enzymes.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12089768
journal: Q Rev Biol
volume: 77
pages: 127-47
published year: 2002
authors:
  item: Fruton JS