D00210
type: Enzyme
rlcp: p13
cath: Rossmann fold
cath: Methylamine Dehydrogenase; Chain H
ec: https://purl.uniprot.org/enzyme/3.4.21.26
csa: 1qfm
uniprot: P23687
kegg enzyme: prolyl oligopeptidase
kegg enzyme: post-proline cleaving enzyme
kegg enzyme: proline-specific endopeptidase
kegg enzyme: post-proline endopeptidase
kegg enzyme: proline endopeptidase
kegg enzyme: endoprolylpeptidase
kegg enzyme: prolyl endopeptidase
kegg substrate: H2O
kegg substrate: Peptide
kegg substrate: Oxytocin
kegg substrate: Vasopressin
kegg product: Peptide
kegg product: Oligopeptide
kegg intermediate: Peptidyl-tetrahedral intermediate
kegg intermediate: Acyl-enzyme
kegg intermediate: Tetrahedral intermediate
pdb: 1e5tA01
pdb: 1e8mA01
pdb: 1e8nA01
pdb: 1qfmA01
pdb: 1qfsA01
pdb: 1e5tA02
pdb: 1e8mA02
pdb: 1e8nA02
pdb: 1qfmA02
pdb: 1qfsA02
pdb bound state: Unbound
  compound: Peptide
  pdb: 1e5tA01
pdb bound state: Unbound
  compound: Peptide
  pdb: 1e8mA01
pdb bound state: Unbound
  compound: Peptide
  pdb: 1qfmA01
pdb bound state: Unbound
  compound: Peptide
  pdb: 1qfsA01
active site residues resources: Structure of proline iminopeptidase from Xanthomonas campestris pv. citri: a prototype for the prolyl oligopeptidase family.
active site residues resources: Prolyl endopeptidase inhibitors from the underground part of Rhodiola sachalinensis.
active site residues resources: Enzyme inhibitory constituents from Duranta repens.
active site residues resources: Substrate-dependent competency of the catalytic triad of prolyl oligopeptidase.
active site residues resources: A prolyl endopeptidase-inhibiting benzofuran dimer from Polyozellus multiflex.
active site residues resources: P23687
references: Inactivation of prolyl endopeptidase by a peptidylchloromethane. Kinetics of inactivation and identification of sites of modification.
references: cDNA cloning of porcine brain prolyl endopeptidase and identification of the active-site seryl residue.
references: pH-dependent mechanism in the catalysis of prolyl endopeptidase from pig muscle.
references: Prolyl endopeptidase catalysis. A physical rather than a chemical step is rate-limiting.
references: Peptidyldiazomethanes. A novel mechanism of interaction with prolyl endopeptidase.
references: Unusual secondary specificity of prolyl oligopeptidase and the different reactivities of its two forms toward charged substrates.
references: Cleavage of the Lys196-Ser197 bond of prolyl oligopeptidase: enhanced catalytic activity for one of the two active enzyme forms.
references: Characterization of a prolyl endopeptidase from Flavobacterium meningosepticum. Complete sequence and localization of the active-site serine.
references: Prolyl oligopeptidase catalysis. Reactions with thiono substrates reveal substrate-induced conformational change to be the rate-limiting step.
references: New potent prolyl endopeptidase inhibitors: synthesis and structure-activity relationships of indan and tetralin derivatives and their analogues.
references: Synthesis and structure-activity relationships of peptidyl alpha-keto heterocycles as novel inhibitors of prolyl endopeptidase.
references: Benzyloxycarbonylprolylprolinal, a transition-state analogue for prolyl oligopeptidase, forms a tetrahedral adduct with catalytic serine, not a reactive cysteine.
references: Probing substrate backbone function in prolyl oligopeptidase catalysis--large positional effects of peptide bond monothioxylation.
references: Low barrier hydrogen bond is absent in the catalytic triads in the ground state but Is present in a transition-state complex in the prolyl oligopeptidase family of serine proteases.
references: New fluorogenic substrates for the study of secondary specificity of prolyl oligopeptidase.
references: The specificity of prolyl endopeptidase from Flavobacterium meningoseptum: mapping the S' subsites by positional scanning via acyl transfer.
references: Prolyl oligopeptidase: an unusual beta-propeller domain regulates proteolysis.
references: Structure of proline iminopeptidase from Xanthomonas campestris pv. citri: a prototype for the prolyl oligopeptidase family.
references: Engineering cyclophilin into a proline-specific endopeptidase.
references: Catalysis of serine oligopeptidases is controlled by a gating filter mechanism.
references: The noncatalytic beta-propeller domain of prolyl oligopeptidase enhances the catalytic capability of the peptidase domain.
references: Substrate- and pH-dependent contribution of oxyanion binding site to the catalysis of prolyl oligopeptidase, a paradigm of the serine oligopeptidase family.
references: Prolyl endopeptidase inhibitors from the underground part of Rhodiola sachalinensis.
references: Structures of prolyl oligopeptidase substrate/inhibitor complexes. Use of inhibitor binding for titration of the catalytic histidine residue.
references: Trypanosoma cruzi prolyl oligopeptidase Tc80 is involved in nonphagocytic mammalian cell invasion by trypomastigotes.
references: Kinetic and mechanistic studies of prolyl oligopeptidase from the hyperthermophile Pyrococcus furiosus.
references: Substrate-dependent, non-hyperbolic kinetics of pig brain prolyl oligopeptidase and its tight binding inhibition by JTP-4819.
references: 4-Phenylbutanoyl-2(S)-acylpyrrolidines and 4-phenylbutanoyl-L-prolyl-2(S)-acylpyrrolidines as prolyl oligopeptidase inhibitors.
references: The prolyl oligopeptidase family.
references: Enzyme inhibitory constituents from Duranta repens.
references: Substrate recognition properties of oligopeptidase B from Salmonella enterica serovar Typhimurium.
references: Electrostatic effects and binding determinants in the catalysis of prolyl oligopeptidase. Site specific mutagenesis at the oxyanion binding site.
references: Substrate-dependent competency of the catalytic triad of prolyl oligopeptidase.
references: A prolyl endopeptidase-inhibiting benzofuran dimer from Polyozellus multiflex.
references: Electrostatic environment at the active site of prolyl oligopeptidase is highly influential during substrate binding.
references: Concerted structural changes in the peptidase and the propeller domains of prolyl oligopeptidase are required for substrate binding.
comment: This enzyme belongs to the peptidase family-S9A. According to the literature [22] & [29], this enzyme has got a catalytic triad (Ser554, Asp641, His680) as in the classical serine proteases such as trypsin. However, the oxyanion hole, which stabilizes the tetrahedral intermediate, is composed of the hydroxyl group of Tyr473 and mainchain amide group of Asn555 (see [29]).

Rossmann fold
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.40.50.1820
catalytic domain: index.html

Methylamine Dehydrogenase; Chain H
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/2.130.10.120

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

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

Oxytocin
type: KeggSubstrate
references: KEGG:C00746
compound type: amide group
compound type: amine group
compound type: aromatic ring (only carbon atom)
compound type: disulfide bond
compound type: peptide/protein
references: CHEBI:7872
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Vasopressin
type: KeggSubstrate
references: KEGG:C00840
compound type: amide group
compound type: amine group
compound type: aromatic ring (only carbon atom)
compound type: carbohydrate
compound type: disulfide bond
compound type: lipid
compound type: peptide/protein

Oligopeptide
type: KeggProduct
references: KEGG:C00098
compound type: amine group
compound type: carboxyl group
compound type: peptide/protein

Peptidyl-tetrahedral intermediate
type: KeggIntermediate
references: KEGG:I00087

Acyl-enzyme
type: KeggIntermediate
references: KEGG:I00085

Tetrahedral intermediate
type: KeggIntermediate
references: KEGG:I00086

1e5tA01
type: Pdb
references: 1e5t
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e5t
catalytic residue: TYR 473;SER 554;ASP 641;HIS 680
main chain in catalysis: ASN 555

1e8mA01
type: Pdb
references: 1e8m
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e8m
catalytic residue: TYR 473; ;ASP 641;HIS 680
main chain in catalysis: ASN 555
comment: mutant S554A

1e8nA01
type: Pdb
references: 1e8n
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e8n
catalytic residue: TYR 473; ;ASP 641;HIS 680
main chain in catalysis: ASN 555
comment: mutant S554A

1qfmA01
type: Pdb
references: 1qfm
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qfm
catalytic residue: TYR 473;SER 554;ASP 641;HIS 680
main chain in catalysis: ASN 555

1qfsA01
type: Pdb
references: 1qfs
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qfs
catalytic residue: TYR 473;SER 554;ASP 641;HIS 680
main chain in catalysis: ASN 555

Inactivation of prolyl endopeptidase by a peptidylchloromethane. Kinetics of inactivation and identification of sites of modification.
type: BibliographicResource
comment: ACTIVE SITE HIS-680.
medline id: 91291146
references: http://www.ncbi.nlm.nih.gov/pubmed/2064618
journal: Biochem J
volume: 276
pages: 837-40
published year: 1991
authors:
  item: Stone SR
  item: Rennex D
  item: Wikstrom P
  item: Shaw E
  item: Hofsteenge J
references: P23687

cDNA cloning of porcine brain prolyl endopeptidase and identification of the active-site seryl residue.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1900195
journal: Biochemistry
volume: 30
pages: 2195-203
published year: 1991
authors:
  item: Rennex D
  item: Hemmings BA
  item: Hofsteenge J
  item: Stone SR

pH-dependent mechanism in the catalysis of prolyl endopeptidase from pig muscle.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/2026166
journal: Eur J Biochem
volume: 197
pages: 441-7
published year: 1991
authors:
  item: Polgar L

Prolyl endopeptidase catalysis. A physical rather than a chemical step is rate-limiting.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1590752
journal: Biochem J
volume: 283
pages: 647-8
published year: 1992
authors:
  item: Polgar L

Peptidyldiazomethanes. A novel mechanism of interaction with prolyl endopeptidase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1590775
journal: Biochem J
volume: 283
pages: 871-6
published year: 1992
authors:
  item: Stone SR
  item: Rennex D
  item: Wikstrom P
  item: Shaw E
  item: Hofsteenge J

Unusual secondary specificity of prolyl oligopeptidase and the different reactivities of its two forms toward charged substrates.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1510958
journal: Biochemistry
volume: 31
pages: 7729-35
published year: 1992
authors:
  item: Polgar L

Cleavage of the Lys196-Ser197 bond of prolyl oligopeptidase: enhanced catalytic activity for one of the two active enzyme forms.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1420194
journal: Biochemistry
volume: 31
pages: 10769-73
published year: 1992
authors:
  item: Polgar L
  item: Patthy A

Characterization of a prolyl endopeptidase from Flavobacterium meningosepticum. Complete sequence and localization of the active-site serine.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1569074
journal: J Biol Chem
volume: 267
pages: 8192-9
published year: 1992
authors:
  item: Chevallier S
  item: Goeltz P
  item: Thibault P
  item: Banville D
  item: Gagnon J

Prolyl oligopeptidase catalysis. Reactions with thiono substrates reveal substrate-induced conformational change to be the rate-limiting step.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8486154
journal: FEBS Lett
volume: 322
pages: 227-30
published year: 1993
authors:
  item: Polgar L
  item: Kollt E
  item: Hollosi M

New potent prolyl endopeptidase inhibitors: synthesis and structure-activity relationships of indan and tetralin derivatives and their analogues.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8027988
journal: J Med Chem
volume: 37
pages: 2071-8
published year: 1994
authors:
  item: Tanaka Y
  item: Niwa S
  item: Nishioka H
  item: Yamanaka T
  item: Torizuka M
  item: Yoshinaga K
  item: Kobayashi N
  item: Ikeda Y
  item: Arai H

Synthesis and structure-activity relationships of peptidyl alpha-keto heterocycles as novel inhibitors of prolyl endopeptidase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7932578
journal: J Med Chem
volume: 37
pages: 3492-502
published year: 1994
authors:
  item: Tsutsumi S
  item: Okonogi T
  item: Shibahara S
  item: Ohuchi S
  item: Hatsushiba E
  item: Patchett AA
  item: Christensen BG

Benzyloxycarbonylprolylprolinal, a transition-state analogue for prolyl oligopeptidase, forms a tetrahedral adduct with catalytic serine, not a reactive cysteine.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9148758
journal: Biochem J
volume: 322
pages: 839-43
published year: 1997
authors:
  item: Kahyaoglu A
  item: Haghjoo K
  item: Kraicsovits F
  item: Jordan F
  item: Polgar L

Probing substrate backbone function in prolyl oligopeptidase catalysis--large positional effects of peptide bond monothioxylation.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9151967
journal: Eur J Biochem
volume: 245
pages: 381-5
published year: 1997
authors:
  item: Schutkowski M
  item: Jakob M
  item: Landgraf G
  item: Born I
  item: Neubert K
  item: Fischer G

Low barrier hydrogen bond is absent in the catalytic triads in the ground state but Is present in a transition-state complex in the prolyl oligopeptidase family of serine proteases.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9325271
journal: J Biol Chem
volume: 272
pages: 25547-54
published year: 1997
authors:
  item: Kahyaoglu A
  item: Haghjoo K
  item: Guo F
  item: Jordan F
  item: Kettner C
  item: Felfoldi F
  item: Polgar L

New fluorogenic substrates for the study of secondary specificity of prolyl oligopeptidase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9128099
journal: J Pept Res
volume: 49
pages: 46-51
published year: 1997
authors:
  item: Noula C
  item: Kokotos G
  item: Barth T
  item: Tzougraki C

The specificity of prolyl endopeptidase from Flavobacterium meningoseptum: mapping the S' subsites by positional scanning via acyl transfer.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9839007
journal: Bioorg Med Chem
volume: 6
pages: 1775-80
published year: 1998
authors:
  item: Bordusa F
  item: Jakubke HD

Prolyl oligopeptidase: an unusual beta-propeller domain regulates proteolysis.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS).
medline id: 98359116
references: http://www.ncbi.nlm.nih.gov/pubmed/9695945
journal: Cell
volume: 94
pages: 161-70
published year: 1998
authors:
  item: Fulop V
  item: Bocskei Z
  item: Polgar L
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P23687

Structure of proline iminopeptidase from Xanthomonas campestris pv. citri: a prototype for the prolyl oligopeptidase family.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9427736
journal: EMBO J
volume: 17
pages: 1-9
published year: 1998
authors:
  item: Medrano FJ
  item: Alonso J
  item: Garcia JL
  item: Romero A
  item: Bode W
  item: Gomis-Ruth FX

Engineering cyclophilin into a proline-specific endopeptidase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9440697
journal: Nature
volume: 391
pages: 301-4
published year: 1998
authors:
  item: Quemeneur E
  item: Moutiez M
  item: Charbonnier JB
  item: Menez A

Catalysis of serine oligopeptidases is controlled by a gating filter mechanism.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/11256612
journal: EMBO Rep
volume: 1
pages: 277-81
published year: 2000
authors:
  item: Fulop V
  item: Szeltner Z
  item: Polgar L
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

The noncatalytic beta-propeller domain of prolyl oligopeptidase enhances the catalytic capability of the peptidase domain.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10747969
journal: J Biol Chem
volume: 275
pages: 15000-5
published year: 2000
authors:
  item: Szeltner Z
  item: Renner V
  item: Polgar L

Substrate- and pH-dependent contribution of oxyanion binding site to the catalysis of prolyl oligopeptidase, a paradigm of the serine oligopeptidase family.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10716187
journal: Protein Sci
volume: 9
pages: 353-60
published year: 2000
authors:
  item: Szeltner Z
  item: Renner V
  item: Polgar L

Prolyl endopeptidase inhibitors from the underground part of Rhodiola sachalinensis.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11310664
journal: Chem Pharm Bull (Tokyo)
volume: 49
pages: 396-401
published year: 2001
authors:
  item: Fan W
  item: Tezuka Y
  item: Ni KM
  item: Kadota S

Structures of prolyl oligopeptidase substrate/inhibitor complexes. Use of inhibitor binding for titration of the catalytic histidine residue.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/11031266
journal: J Biol Chem
volume: 276
pages: 1262-6
published year: 2001
authors:
  item: Fulop V
  item: Szeltner Z
  item: Renner V
  item: Polgar L
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Trypanosoma cruzi prolyl oligopeptidase Tc80 is involved in nonphagocytic mammalian cell invasion by trypomastigotes.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11598112
journal: J Biol Chem
volume: 276
pages: 47078-86
published year: 2001
authors:
  item: Grellier P
  item: Vendeville S
  item: Joyeau R
  item: Bastos IM
  item: Drobecq H
  item: Frappier F
  item: Teixeira AR
  item: Schrevel J
  item: Davioud-Charvet E
  item: Sergheraert C
  item: Santana JM

Kinetic and mechanistic studies of prolyl oligopeptidase from the hyperthermophile Pyrococcus furiosus.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11278687
journal: J Biol Chem
volume: 276
pages: 19310-7
published year: 2001
authors:
  item: Harris MN
  item: Madura JD
  item: Ming LJ
  item: Harwood VJ

Substrate-dependent, non-hyperbolic kinetics of pig brain prolyl oligopeptidase and its tight binding inhibition by JTP-4819.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12147298
journal: Biochem Pharmacol
volume: 64
pages: 463-71
published year: 2002
authors:
  item: Venalainen JI
  item: Juvonen RO
  item: Forsberg MM
  item: Garcia-Horsman A
  item: Poso A
  item: Wallen EA
  item: Gynther J
  item: Mannisto PT

4-Phenylbutanoyl-2(S)-acylpyrrolidines and 4-phenylbutanoyl-L-prolyl-2(S)-acylpyrrolidines as prolyl oligopeptidase inhibitors.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11983517
journal: Bioorg Med Chem
volume: 10
pages: 2199-206
published year: 2002
authors:
  item: Wallen EA
  item: Christiaans JA
  item: Saario SM
  item: Forsberg MM
  item: Venalainen JI
  item: Paso HM
  item: Mannisto PT
  item: Gynther J

The prolyl oligopeptidase family.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11915948
journal: Cell Mol Life Sci
volume: 59
pages: 349-62
published year: 2002
authors:
  item: Polgar L

Enzyme inhibitory constituents from Duranta repens.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11964000
journal: Chem Pharm Bull (Tokyo)
volume: 50
pages: 515-8
published year: 2002
authors:
  item: Anis I
  item: Ahmed S
  item: Malik A
  item: Yasin A
  item: Choudary MI

Substrate recognition properties of oligopeptidase B from Salmonella enterica serovar Typhimurium.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12029050
journal: J Bacteriol
volume: 184
pages: 3329-37
published year: 2002
authors:
  item: Morty RE
  item: Fulop V
  item: Andrews NW

Electrostatic effects and binding determinants in the catalysis of prolyl oligopeptidase. Site specific mutagenesis at the oxyanion binding site.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12202494
journal: J Biol Chem
volume: 277
pages: 42613-22
published year: 2002
authors:
  item: Szeltner Z
  item: Rea D
  item: Renner V
  item: Fulop V
  item: Polgar L

Substrate-dependent competency of the catalytic triad of prolyl oligopeptidase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12228249
journal: J Biol Chem
volume: 277
pages: 44597-605
published year: 2002
authors:
  item: Szeltner Z
  item: Rea D
  item: Juhasz T
  item: Renner V
  item: Mucsi Z
  item: Orosz G
  item: Fulop V
  item: Polgar L

A prolyl endopeptidase-inhibiting benzofuran dimer from Polyozellus multiflex.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11809072
journal: J Nat Prod
volume: 65
pages: 76-8
published year: 2002
authors:
  item: Song KS
  item: Raskin I

Electrostatic environment at the active site of prolyl oligopeptidase is highly influential during substrate binding.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/14514675
journal: J Biol Chem
volume: 278
pages: 48786-93
published year: 2003
authors:
  item: Szeltner Z
  item: Rea D
  item: Renner V
  item: Juliano L
  item: Fulop V
  item: Polgar L

Concerted structural changes in the peptidase and the propeller domains of prolyl oligopeptidase are required for substrate binding.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/15210359
journal: J Mol Biol
volume: 340
pages: 627-37
published year: 2004
authors:
  item: Szeltner Z
  item: Rea D
  item: Juhasz T
  item: Renner V
  item: Fulop V
  item: Polgar L

Analogue
compound: Oligopeptide
pdb: 1e8mA01
ligand het code: PHQ-GLY-PRO (chain I)

IntermediateAnalogue
compound: Tetrahedral intermediate
pdb: 1e5tA01
ligand het code: GOL

IntermediateAnalogue
compound: Tetrahedral intermediate
pdb: 1qfmA01
ligand het code: SGL

IntermediateAnalogue
compound: Tetrahedral intermediate
pdb: 1qfsA01
ligand het code: ZPR

ReferenceForCatalyticMechanism
reference index: 9

ReferenceForCatalyticMechanism
reference index: 14
reference section: Scheme 1

ReferenceForCatalyticMechanism
reference index: 17
reference section: p.165

ReferenceForCatalyticMechanism
reference index: 22

ReferenceForCatalyticMechanism
reference index: 29
reference section: p.354