D00257
type: Enzyme
cath: Aspartate Aminotransferase, domain 1
cath: Aspartate Aminotransferase; domain 2
ec: https://purl.uniprot.org/enzyme/4.1.99.1
csa: 1ax4
uniprot: P28796
kegg enzyme: tryptophanase
kegg enzyme: L-tryptophanase
kegg enzyme: L-tryptophan indole-lyase (deaminating)
kegg pathway: Tryptophan metabolism
kegg pathway: Nitrogen metabolism
kegg cofactor: Pyridoxal phosphate
kegg cofactor: Potassium
kegg substrate: L-Tryptophan
kegg substrate: H2O
kegg product: Indole
kegg product: Pyruvate
kegg product: NH3
pdb: 1ax4A01
pdb: 1ax4B01
pdb: 1ax4C01
pdb: 1ax4D01
pdb: 1ax4A02
pdb: 1ax4B02
pdb: 1ax4C02
pdb: 1ax4D02
pdb bound state: Unbound
  compound: L-Tryptophan
  pdb: 1ax4A01
pdb bound state: Unbound
  compound: L-Tryptophan
  pdb: 1ax4B01
pdb bound state: Unbound
  compound: L-Tryptophan
  pdb: 1ax4C01
pdb bound state: Unbound
  compound: L-Tryptophan
  pdb: 1ax4D01
pdb bound state: Unbound
  compound: L-Tryptophan
  pdb: 1ax4A02
pdb bound state: Unbound
  compound: L-Tryptophan
  pdb: 1ax4B02
pdb bound state: Unbound
  compound: L-Tryptophan
  pdb: 1ax4C02
pdb bound state: Unbound
  compound: L-Tryptophan
  pdb: 1ax4D02
pdb bound state: Unbound
  compound: Pyridoxal phosphate
  pdb: 1ax4A01
pdb bound state: Unbound
  compound: Pyridoxal phosphate
  pdb: 1ax4B01
pdb bound state: Unbound
  compound: Pyridoxal phosphate
  pdb: 1ax4C01
pdb bound state: Unbound
  compound: Pyridoxal phosphate
  pdb: 1ax4D01
pdb bound state: Analogue
  compound: Pyridoxal phosphate
  pdb: 1ax4A02
  ligand het code: LLP
pdb bound state: Analogue
  compound: Pyridoxal phosphate
  pdb: 1ax4B02
  ligand het code: LLP
pdb bound state: Analogue
  compound: Pyridoxal phosphate
  pdb: 1ax4C02
  ligand het code: LLP
pdb bound state: Analogue
  compound: Pyridoxal phosphate
  pdb: 1ax4D02
  ligand het code: LLP
pdb bound state: Unbound
  compound: Potassium
  pdb: 1ax4A01
pdb bound state: Unbound
  compound: Potassium
  pdb: 1ax4B01
pdb bound state: Unbound
  compound: Potassium
  pdb: 1ax4C01
pdb bound state: Unbound
  compound: Potassium
  pdb: 1ax4D01
pdb bound state: Unbound
  compound: Indole
  pdb: 1ax4A01
pdb bound state: Unbound
  compound: Indole
  pdb: 1ax4B01
pdb bound state: Unbound
  compound: Indole
  pdb: 1ax4C01
pdb bound state: Unbound
  compound: Indole
  pdb: 1ax4D01
pdb bound state: Unbound
  compound: Indole
  pdb: 1ax4A02
pdb bound state: Unbound
  compound: Indole
  pdb: 1ax4B02
pdb bound state: Unbound
  compound: Indole
  pdb: 1ax4C02
pdb bound state: Unbound
  compound: Indole
  pdb: 1ax4D02
pdb bound state: Unbound
  compound: Pyruvate
  pdb: 1ax4A01
pdb bound state: Unbound
  compound: Pyruvate
  pdb: 1ax4B01
pdb bound state: Unbound
  compound: Pyruvate
  pdb: 1ax4C01
pdb bound state: Unbound
  compound: Pyruvate
  pdb: 1ax4D01
active site residues resources: Analysis of stability and catalytic properties of two tryptophanases from a thermophile.
references: Preparation of pyridoxal 5'-phosphate-bound sepharose and its use for immobilization of tryptophanase.
references: Reactivation of enzymes by light-stimulated cleavage of reduced pyridoxal 5'-phosphate-enzyme complexes.
references: Phosphorus 31 nuclear magnetic resonance study of tryptophanase. Pyridoxal phosphate-binding site.
references: Phosphorus-31 nuclear magnetic resonance studies on four pyridoxal 5'-phosphate dependent enzymes.
references: Functional role of cysteinyl residues in tryptophanase.
references: Catalytic function of a tyrosyl residue in tryptophanase.
references: Reactions of O-acyl-L-serines with tryptophanase, tyrosine phenol-lyase, and tryptophan synthase.
references: Mechanistic deductions from multiple kinetic and solvent deuterium isotope effects and pH studies of pyridoxal phosphate dependent carbon-carbon lyases: Escherichia coli tryptophan indole-lyase.
references: Overproduction and crystallization of tryptophanase from recombinant cells of Escherichia coli.
references: NMR spectra of exchangeable protons of pyridoxal phosphate-dependent enzymes.
references: Preliminary X-ray crystallographic analysis of tryptophanase from Escherichia coli.
references: Indole protects tryptophan indole-lyase, but not tryptophan synthase, from inactivation by trifluoroalanine.
references: Identification of indigo-related pigments produced by Escherichia coli containing a cloned Rhodococcus gene.
references: Tryptophanase from Escherichia coli: catalytic and spectral properties in water-organic solvents.
references: Crystallization and preliminary X-ray investigation of holotryptophanases from Escherichia coli and Proteus vulgaris.
references: Analysis of the pH- and ligand-induced spectral transitions of tryptophanase: activation of the coenzyme at the early steps of the catalytic cycle.
references: Crystal structure of tryptophanase.
references: Analysis of stability and catalytic properties of two tryptophanases from a thermophile.
references: Stereochemistry of the transamination reaction catalyzed by aminodeoxychorismate lyase from Escherichia coli: close relationship between fold type and stereochemistry.
references: Crystals of tryptophan indole-lyase and tyrosine phenol-lyase form stable quinonoid complexes.
comment: Although this enzyme binds potassium ion, it is too distant from the active site to be involved in catalysis directly (see [17]). According to the literature [17], this enzyme catalyzes five reactions: (A) Formation of external aldimine (Schiff-base between PLP & substrate amino group), (B) Elimination of indole ring from the external aldimine complex, (C) Addition of water to double-bonded carbon atom (or Hydration), (D) Elimination of imine group from the product, (E) Formation of internal aldimine (Schiff-base between PLP & catalytic lysine).

Aspartate Aminotransferase, domain 1
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.90.1150.10

Aspartate Aminotransferase; domain 2
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.40.640.10
catalytic domain: index.html

Tryptophan metabolism
type: KeggPathway
references: KEGG:MAP00380

Nitrogen metabolism
type: KeggPathway
references: KEGG:MAP00910

Pyridoxal phosphate
type: KeggCofactor
references: KEGG:C00018
compound type: aromatic ring (with nitrogen atoms)
compound type: phosphate group/phosphate ion
references: CHEBI:18405
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Potassium
type: KeggCofactor
references: KEGG:C00238
compound type: univalent metal (Na+, K+)
references: CHEBI:29103
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

L-Tryptophan
type: KeggSubstrate
references: KEGG:C00078
compound type: amino acids
compound type: aromatic ring (only carbon atom)
compound type: aromatic ring (with nitrogen atoms)
references: CHEBI:16828
references: CHEBI:57912
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

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

Indole
type: KeggProduct
references: KEGG:C00463
compound type: aromatic ring (only carbon atom)
compound type: aromatic ring (with nitrogen atoms)
references: CHEBI:16881
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Pyruvate
type: KeggProduct
references: KEGG:C00022
compound type: carbohydrate
compound type: carboxyl group
references: CHEBI:32816
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

NH3
type: KeggProduct
references: KEGG:C00014
compound type: amine group
compound type: organic ion
references: CHEBI:16134
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

1ax4A01
type: Pdb
references: 1ax4
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ax4
cofactor binding residue: GLY 53(Potassium binding)

1ax4B01
type: Pdb
references: 1ax4
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ax4
cofactor binding residue: GLY 53(Potassium binding)

1ax4C01
type: Pdb
references: 1ax4
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ax4
cofactor binding residue: GLY 53(Potassium binding)

1ax4D01
type: Pdb
references: 1ax4
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ax4
cofactor binding residue: GLY 53(Potassium binding)

1ax4A02
type: Pdb
references: 1ax4
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ax4
catalytic residue: ARG 226;LLP 266
cofactor binding residue: GLU 70;ASN 271(Potassium binding)
modified residue: LLP 266(PLP-bound to Lys)

1ax4B02
type: Pdb
references: 1ax4
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ax4
catalytic residue: ARG 226;LLP 266
cofactor binding residue: GLU 70;ASN 271(Potassium binding)
modified residue: LLP 266(PLP-bound to Lys)

1ax4C02
type: Pdb
references: 1ax4
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ax4
catalytic residue: ARG 226;LLP 266
cofactor binding residue: GLU 70;ASN 271(Potassium binding)
modified residue: LLP 266(PLP-bound to Lys)

1ax4D02
type: Pdb
references: 1ax4
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ax4
catalytic residue: ARG 226;LLP 266
cofactor binding residue: GLU 70;ASN 271(Potassium binding)
modified residue: LLP 266(PLP-bound to Lys)

Preparation of pyridoxal 5'-phosphate-bound sepharose and its use for immobilization of tryptophanase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/4575958
journal: Biochem Biophys Res Commun
volume: 52
pages: 482-8
published year: 1973
authors:
  item: Ikeda S
  item: Fukui S

Reactivation of enzymes by light-stimulated cleavage of reduced pyridoxal 5'-phosphate-enzyme complexes.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/20936
journal: Biochemistry
volume: 16
pages: 4584-90
published year: 1977
authors:
  item: Ritchey JM
  item: Gibbons I
  item: Schachman HK

Phosphorus 31 nuclear magnetic resonance study of tryptophanase. Pyridoxal phosphate-binding site.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/6339506
journal: J Biol Chem
volume: 258
pages: 4839-41
published year: 1983
authors:
  item: Schnackerz KD
  item: Snell EE

Phosphorus-31 nuclear magnetic resonance studies on four pyridoxal 5'-phosphate dependent enzymes.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/6728845
journal: Prog Clin Biol Res
volume: 144A
pages: 195-208
published year: 1984
authors:
  item: Schnackerz KD

Functional role of cysteinyl residues in tryptophanase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/3888623
journal: Eur J Biochem
volume: 149
pages: 129-33
published year: 1985
authors:
  item: Nihira T
  item: Yasuda T
  item: Kakizono T
  item: Taguchi H
  item: Ichikawa M
  item: Toraya T
  item: Fukui S

Catalytic function of a tyrosyl residue in tryptophanase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/3524569
journal: Biochem Biophys Res Commun
volume: 137
pages: 964-9
published year: 1986
authors:
  item: Kakizono T
  item: Nihira T
  item: Taguchi H

Reactions of O-acyl-L-serines with tryptophanase, tyrosine phenol-lyase, and tryptophan synthase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/3111376
journal: Arch Biochem Biophys
volume: 256
pages: 302-10
published year: 1987
authors:
  item: Phillips RS

Mechanistic deductions from multiple kinetic and solvent deuterium isotope effects and pH studies of pyridoxal phosphate dependent carbon-carbon lyases: Escherichia coli tryptophan indole-lyase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/3061452
journal: Biochemistry
volume: 27
pages: 7339-44
published year: 1988
authors:
  item: Kiick DM
  item: Phillips RS

Overproduction and crystallization of tryptophanase from recombinant cells of Escherichia coli.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/2178632
journal: Biotechnol Appl Biochem
volume: 12
pages: 28-33
published year: 1990
authors:
  item: Tani S
  item: Tsujimoto N
  item: Kawata Y
  item: Tokushige M

NMR spectra of exchangeable protons of pyridoxal phosphate-dependent enzymes.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/2069576
journal: Biochem Biophys Res Commun
volume: 178
pages: 385-92
published year: 1991
authors:
  item: Metzler CM
  item: Metzler DE
  item: Kintanar A
  item: Scott RD
  item: Marceau M

Preliminary X-ray crystallographic analysis of tryptophanase from Escherichia coli.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/2060649
journal: FEBS Lett
volume: 284
pages: 270-2
published year: 1991
authors:
  item: Kawata Y
  item: Tani S
  item: Sato M
  item: Katsube Y
  item: Tokushige M

Indole protects tryptophan indole-lyase, but not tryptophan synthase, from inactivation by trifluoroalanine.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1632641
journal: Arch Biochem Biophys
volume: 296
pages: 489-96
published year: 1992
authors:
  item: Phillips RS
  item: Dua RK

Identification of indigo-related pigments produced by Escherichia coli containing a cloned Rhodococcus gene.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1372930
journal: J Gen Microbiol
volume: 138
pages: 211-6
published year: 1992
authors:
  item: Hart S
  item: Koch KR
  item: Woods DR

Tryptophanase from Escherichia coli: catalytic and spectral properties in water-organic solvents.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7849621
journal: Biochem Mol Biol Int
volume: 34
pages: 209-16
published year: 1994
authors:
  item: Faleev NG
  item: Dementieva IS
  item: Zakomirdina LN
  item: Gogoleva OI
  item: Belikov VM

Crystallization and preliminary X-ray investigation of holotryptophanases from Escherichia coli and Proteus vulgaris.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8289300
journal: J Mol Biol
volume: 235
pages: 783-6
published year: 1994
authors:
  item: Dementieva IS
  item: Zakomirdina LN
  item: Sinitzina NI
  item: Antson AA
  item: Wilson KS
  item: Isupov MN
  item: Lebedev AA
  item: Harutyunyan EH

Analysis of the pH- and ligand-induced spectral transitions of tryptophanase: activation of the coenzyme at the early steps of the catalytic cycle.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9485457
journal: Biochemistry
volume: 37
pages: 3043-52
published year: 1998
authors:
  item: Ikushiro H
  item: Hayashi H
  item: Kawata Y
  item: Kagamiyama H

Crystal structure of tryptophanase.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
medline id: 98212457
references: http://www.ncbi.nlm.nih.gov/pubmed/9551100
journal: J Mol Biol
volume: 276
pages: 603-23
published year: 1998
authors:
  item: Isupov MN
  item: Antson AA
  item: Dodson EJ
  item: Dodson GG
  item: Dementieva IS
  item: Zakomirdina LN
  item: Wilson KS
  item: Dauter Z
  item: Lebedev AA
  item: Harutyunyan EH
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P28796

Analysis of stability and catalytic properties of two tryptophanases from a thermophile.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10469830
journal: Protein Eng
volume: 12
pages: 687-92
published year: 1999
authors:
  item: Kudo H
  item: Natsume R
  item: Nishiyama M
  item: Horinouchi S

Stereochemistry of the transamination reaction catalyzed by aminodeoxychorismate lyase from Escherichia coli: close relationship between fold type and stereochemistry.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11011151
journal: J Biochem (Tokyo)
volume: 128
pages: 679-86
published year: 2000
authors:
  item: Jhee KH
  item: Yoshimura T
  item: Miles EW
  item: Takeda S
  item: Miyahara I
  item: Hirotsu K
  item: Soda K
  item: Kawata Y
  item: Esaki N

Crystals of tryptophan indole-lyase and tyrosine phenol-lyase form stable quinonoid complexes.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11934889
journal: J Biol Chem
volume: 277
pages: 21592-7
published year: 2002
authors:
  item: Phillips RS
  item: Demidkina TV
  item: Zakomirdina LN
  item: Bruno S
  item: Ronda L
  item: Mozzarelli A

ReferenceForCatalyticMechanism
reference index: 7
reference section: SCHEME 2A

ReferenceForCatalyticMechanism
reference index: 8
reference section: Fig.5, p.7343
reference step: 3

ReferenceForCatalyticMechanism
reference index: 12
reference section: SCHEME I

ReferenceForCatalyticMechanism
reference index: 14
reference section: Fig.1

ReferenceForCatalyticMechanism
reference index: 17
reference section: Figure 1
reference step: p.604

ReferenceForCatalyticMechanism
reference index: 19
reference section: Fig. 3

ReferenceForCatalyticMechanism
reference index: 20
reference section: Scheme 3, p.21595-21597
reference step: 3