D00258
type: Enzyme
cath: Aspartate Aminotransferase, domain 1
cath: Aspartate Aminotransferase; domain 2
ec: https://purl.uniprot.org/enzyme/4.1.99.2
csa: 2tpl
uniprot: P31013
uniprot: P31012
kegg enzyme: tyrosine phenol-lyase
kegg enzyme: beta-tyrosinase
kegg enzyme: L-tyrosine phenol-lyase (deaminating)
kegg pathway: Tyrosine metabolism
kegg pathway: Nitrogen metabolism
kegg cofactor: Pyridoxal phosphate
kegg substrate: L-Tyrosine
kegg substrate: H2O
kegg product: Phenol
kegg product: Pyruvate
kegg product: NH3
pdb: 1tplA01
pdb: 1tplB01
pdb: 2tplA01
pdb: 2tplB01
pdb: 1tplA02
pdb: 1tplB02
pdb: 2tplA02
pdb: 2tplB02
pdb bound state: Unbound
  compound: L-Tyrosine
  pdb: 1tplA01
pdb bound state: Unbound
  compound: L-Tyrosine
  pdb: 1tplB01
pdb bound state: Unbound
  compound: L-Tyrosine
  pdb: 2tplA01
pdb bound state: Analogue
  compound: L-Tyrosine
  pdb: 2tplB01
  ligand het code: HPP
pdb bound state: Unbound
  compound: L-Tyrosine
  pdb: 1tplA02
pdb bound state: Unbound
  compound: L-Tyrosine
  pdb: 1tplB02
pdb bound state: Unbound
  compound: L-Tyrosine
  pdb: 2tplA02
pdb bound state: Unbound
  compound: L-Tyrosine
  pdb: 2tplB02
pdb bound state: Unbound
  compound: Pyridoxal phosphate
  pdb: 1tplA01
pdb bound state: Unbound
  compound: Pyridoxal phosphate
  pdb: 1tplB01
pdb bound state: Unbound
  compound: Pyridoxal phosphate
  pdb: 2tplA01
pdb bound state: Unbound
  compound: Pyridoxal phosphate
  pdb: 2tplB01
pdb bound state: Unbound
  compound: Pyridoxal phosphate
  pdb: 1tplA02
pdb bound state: Unbound
  compound: Pyridoxal phosphate
  pdb: 1tplB02
pdb bound state: Unbound
  compound: Pyridoxal phosphate
  pdb: 2tplA02
pdb bound state: Unbound
  compound: Pyridoxal phosphate
  pdb: 2tplB02
pdb bound state: Unbound
  compound: Phenol
  pdb: 1tplA01
pdb bound state: Unbound
  compound: Phenol
  pdb: 1tplB01
pdb bound state: Unbound
  compound: Phenol
  pdb: 2tplA01
pdb bound state: Unbound
  compound: Phenol
  pdb: 2tplB01
pdb bound state: Unbound
  compound: Phenol
  pdb: 1tplA02
pdb bound state: Unbound
  compound: Phenol
  pdb: 1tplB02
pdb bound state: Unbound
  compound: Phenol
  pdb: 2tplA02
pdb bound state: Unbound
  compound: Phenol
  pdb: 2tplB02
pdb bound state: Unbound
  compound: Pyruvate
  pdb: 1tplA01
pdb bound state: Unbound
  compound: Pyruvate
  pdb: 1tplB01
pdb bound state: Unbound
  compound: Pyruvate
  pdb: 2tplA01
pdb bound state: Unbound
  compound: Pyruvate
  pdb: 2tplB01
pdb bound state: Unbound
  compound: Pyruvate
  pdb: 1tplA02
pdb bound state: Unbound
  compound: Pyruvate
  pdb: 1tplB02
active site residues resources: Purification and crystals of tyrosine phenol-lyase from Erwinia herbicola.
active site residues resources: Synthesis of (2S,3R)-beta-methyltyrosine catalyzed by tyrosine phenol-lyase.
active site residues resources: Inhibition of tyrosine phenol-lyase from Citrobacter freundii by 2-azatyrosine and 3-azatyrosine.
active site residues resources: Crystals of tryptophan indole-lyase and tyrosine phenol-lyase form stable quinonoid complexes.
references: Synthesis of L-tyrosine-related amino acids by beta-tyrosinase.
references: Synthesis of 2,3,4-trihydroxy-L-phenylalanine from s-methyl-L-cysteine and pyrogallol by L-tyrosine phenol-lyase.
references: Stereochemistry of beta-replacement reactions catalyzed by tyrosine phenol-lyase.
references: Elementary processes in the interaction of tyrosine phenol lyase with inhibitors and substrate.
references: Reactions of O-acyl-L-serines with tryptophanase, tyrosine phenol-lyase, and tryptophan synthase.
references: Tyrosine phenol-lyase from Citrobacter intermedius. Factors controlling substrate specificity.
references: Crystallization and crystal data on tyrosine phenol-lyase.
references: The polypeptide chain fold in tyrosine phenol-lyase, a pyridoxal-5'-phosphate-dependent enzyme.
references: Three-dimensional structure of tyrosine phenol-lyase.
references: http://ezcatdb.cbrc.jp/EzCatDB/reference/D00258#10
references: Purification and crystals of tyrosine phenol-lyase from Erwinia herbicola.
references: http://ezcatdb.cbrc.jp/EzCatDB/reference/D00258#12
references: Synthesis of (2S,3R)-beta-methyltyrosine catalyzed by tyrosine phenol-lyase.
references: Conversion of tyrosine phenol-lyase to dicarboxylic amino acid beta-lyase, an enzyme not found in nature.
references: The role of glutamic acid-69 in the activation of Citrobacter freundii tyrosine phenol-lyase by monovalent cations.
references: Interaction of tyrosine phenol-lyase with phosphoroorganic analogues of substrate amino acids.
references: Inhibition of tyrosine phenol-lyase from Citrobacter freundii by 2-azatyrosine and 3-azatyrosine.
references: Threonine-124 and phenylalanine-448 in Citrobacter freundii tyrosine phenol-lyase are necessary for activity with L-tyrosine.
references: Crystals of tryptophan indole-lyase and tyrosine phenol-lyase form stable quinonoid complexes.
comment: This enzyme catalyzes several reactions; (A) Formation of external aldimine from internal aldimine (with pyridoxal phosphate;PLP) involves addition to double-bond and elimination accompanied by double-bond formation. (Arg217 can be involved in the formation.) (B) Elimination of phenol, accompanied by double-bond formation. (C) Return to internal aldimine involves addition to double-bond, and elimination accompanied by double-bond formation. (D) Hydrolysis of aldimine bond. However, the mechanism of hydrolysis has not been elucidated.

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

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

Tyrosine metabolism
type: KeggPathway
references: KEGG:MAP00350

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

L-Tyrosine
type: KeggSubstrate
references: KEGG:C00082
compound type: amino acids
compound type: aromatic ring (only carbon atom)
references: CHEBI:17895
references: CHEBI:58315
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

Phenol
type: KeggProduct
references: KEGG:C00146
compound type: aromatic ring (only carbon atom)
references: CHEBI:15882
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

1tplA01
type: Pdb
references: 1tpl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1tpl
catalytic residue: ARG 381
cofactor binding residue: GLY 52(Monovalent cation)

1tplB01
type: Pdb
references: 1tpl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1tpl
catalytic residue: ARG 381
cofactor binding residue: GLY 52(Monovalent cation)

2tplA01
type: Pdb
references: 2tpl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2tpl
catalytic residue: ARG 381
cofactor binding residue: GLY 52(Monovalent cation)

2tplB01
type: Pdb
references: 2tpl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2tpl
catalytic residue: ARG 381
cofactor binding residue: GLY 52(Monovalent cation)

1tplA02
type: Pdb
references: 1tpl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1tpl
catalytic residue: TYR 71; ;LYS 257
cofactor binding residue: GLU 69;ASN 262(Monovalent cation)
comment: invisible 123-131

1tplB02
type: Pdb
references: 1tpl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1tpl
catalytic residue: TYR 71; ;LYS 257
cofactor binding residue: GLU 69;ASN 262(Monovalent cation)
comment: invisible 123-131

2tplA02
type: Pdb
references: 2tpl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2tpl
catalytic residue: TYR 71;THR 124;
cofactor binding residue: GLU 69;ASN 262(Monovalent cation)
modified residue: LLP 257(Modified by PLP)
comment: LLP(modified Lys)

2tplB02
type: Pdb
references: 2tpl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2tpl
catalytic residue: TYR 71;THR 124;
cofactor binding residue: GLU 69;ASN 262(Monovalent cation)
modified residue: LLP 257(Modified by PLP)
comment: LLP(modified Lys)

Synthesis of L-tyrosine-related amino acids by beta-tyrosinase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1190012
journal: Adv Appl Microbiol
volume: 19
pages: 249-88
published year: 1975
authors:
  item: Yamada H
  item: Kumagai H

Synthesis of 2,3,4-trihydroxy-L-phenylalanine from s-methyl-L-cysteine and pyrogallol by L-tyrosine phenol-lyase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1147922
journal: Biochem Biophys Res Commun
volume: 64
pages: 241-7
published year: 1975
authors:
  item: Rapp P
  item: Kumagai H
  item: Yamada H
  item: Ueno T
  item: Fukami H

Stereochemistry of beta-replacement reactions catalyzed by tyrosine phenol-lyase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1141596
journal: J Am Chem Soc
volume: 97
pages: 4334-7
published year: 1975
authors:
  item: Sawada S
  item: Kumagai H
  item: Yamada H
  item: Hill RK

Elementary processes in the interaction of tyrosine phenol lyase with inhibitors and substrate.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/721797
journal: J Biochem (Tokyo)
volume: 84
pages: 633-40
published year: 1978
authors:
  item: Muro T
  item: Nakatani H
  item: Hiromi K
  item: Kumagai H
  item: Yamada 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

Tyrosine phenol-lyase from Citrobacter intermedius. Factors controlling substrate specificity.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/2847927
journal: Eur J Biochem
volume: 177
pages: 395-401
published year: 1988
authors:
  item: Faleev NG
  item: Ruvinov SB
  item: Demidkina TV
  item: Myagkikh IV
  item: Gololobov MYu
  item: Bakhmutov VI
  item: Belikov VM

Crystallization and crystal data on tyrosine phenol-lyase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/3378628
journal: FEBS Lett
volume: 232
pages: 381-2
published year: 1988
authors:
  item: Demidkina TV
  item: Myagkikh IV
  item: Antson AA
  item: Harutyunyan EH

The polypeptide chain fold in tyrosine phenol-lyase, a pyridoxal-5'-phosphate-dependent enzyme.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
medline id: 92290010
references: http://www.ncbi.nlm.nih.gov/pubmed/1601133
journal: FEBS Lett
volume: 302
pages: 256-60
published year: 1992
authors:
  item: Antson AA
  item: Strokopytov BV
  item: Murshudov GN
  item: Isupov MN
  item: Harutyunyan EH
  item: Demidkina TV
  item: Vassylyev DG
  item: Dauter Z
  item: Terry H
  item: Wilson KS
references: P31013

Three-dimensional structure of tyrosine phenol-lyase.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/7916622
journal: Biochemistry
volume: 32
pages: 4195-206
published year: 1993
authors:
  item: Antson AA
  item: Demidkina TV
  item: Gollnick P
  item: Dauter Z
  item: von Tersch RL
  item: Long J
  item: Berezhnoy SN
  item: Phillips RS
  item: Harutyunyan EH
  item: Wilson KS
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

http://ezcatdb.cbrc.jp/EzCatDB/reference/D00258#10
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7547970
journal: Biochemistry
volume: 34
pages: 12276-83
published year: 1995
authors:
  item: Chen HY
  item: Demidkina TV
  item: Phillips RS
title: Site-directed mutagenesis of tyrosine-71 to phenylalanine in Citrobacter freundii tyrosine phenol-lyase: evidence for dual roles of tyrosine-71 as a general acid catalyst in the reaction mechanism and in cofactor binding.

Purification and crystals of tyrosine phenol-lyase from Erwinia herbicola.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8932517
journal: Biochem Mol Biol Int
volume: 38
pages: 37-42
published year: 1996
authors:
  item: Pletnev SV
  item: Isupov MN
  item: Dauter Z
  item: Wilson KS
  item: Faleev NG
  item: Harutyunyan EG
  item: Demidkina TV

http://ezcatdb.cbrc.jp/EzCatDB/reference/D00258#12
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
medline id: 97317094
references: http://www.ncbi.nlm.nih.gov/pubmed/9174368
journal: Biochemistry
volume: 36
pages: 6502-10
published year: 1997
authors:
  item: Sundararaju B
  item: Antson AA
  item: Phillips RS
  item: Demidkina TV
  item: Barbolina MV
  item: Gollnick P
  item: Dodson GG
  item: Wilson KS
title: The crystal structure of Citrobacter freundii tyrosine phenol-lyase complexed with 3-(4'-hydroxyphenyl)propionic acid, together with site-directed mutagenesis and kinetic analysis, demonstrates that arginine 381 is required for substrate specificity.
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P31013

Synthesis of (2S,3R)-beta-methyltyrosine catalyzed by tyrosine phenol-lyase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10328314
journal: Bioorg Med Chem Lett
volume: 9
pages: 1205-8
published year: 1999
authors:
  item: Kim K
  item: Cole PA

Conversion of tyrosine phenol-lyase to dicarboxylic amino acid beta-lyase, an enzyme not found in nature.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9880502
journal: J Biol Chem
volume: 274
pages: 1320-5
published year: 1999
authors:
  item: Mouratou B
  item: Kasper P
  item: Gehring H
  item: Christen P

The role of glutamic acid-69 in the activation of Citrobacter freundii tyrosine phenol-lyase by monovalent cations.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10913261
journal: Biochemistry
volume: 39
pages: 8546-55
published year: 2000
authors:
  item: Sundararaju B
  item: Chen H
  item: Shilcutt S
  item: Phillips RS

Interaction of tyrosine phenol-lyase with phosphoroorganic analogues of substrate amino acids.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11082202
journal: Eur J Biochem
volume: 267
pages: 6897-902
published year: 2000
authors:
  item: Faleev NG
  item: Zhukov YN
  item: Khurs EN
  item: Gogoleva OI
  item: Barbolina MV
  item: Bazhulina NP
  item: Belikov VM
  item: Demidkina TV
  item: Khomutov RM

Inhibition of tyrosine phenol-lyase from Citrobacter freundii by 2-azatyrosine and 3-azatyrosine.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11732906
journal: Biochemistry
volume: 40
pages: 14862-8
published year: 2001
authors:
  item: Watkins EB
  item: Phillips RS

Threonine-124 and phenylalanine-448 in Citrobacter freundii tyrosine phenol-lyase are necessary for activity with L-tyrosine.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11964175
journal: Biochem J
volume: 363
pages: 745-52
published year: 2002
authors:
  item: Demidkina TV
  item: Barbolina MV
  item: Faleev NG
  item: Sundararaju B
  item: Gollnick PD
  item: Phillips RS

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: 6
reference section: Scheme 1, Scheme 2, p.399-401
reference step: 3

ReferenceForCatalyticMechanism
reference index: 10
reference section: Scheme 2, p.12282-12283
reference step: 6

ReferenceForCatalyticMechanism
reference index: 12
reference section: Scheme 1, p.6509-6510
reference step: 6

ReferenceForCatalyticMechanism
reference index: 14
reference section: SCHEME1, p.1324-1325
reference step: 5

ReferenceForCatalyticMechanism
reference index: 15
reference section: Scheme 1, p.8555
reference step: 4

ReferenceForCatalyticMechanism
reference index: 16
reference section: Scheme 1, p.6899-6900
reference step: 7

ReferenceForCatalyticMechanism
reference index: 18
reference section: Scheme 3, p.751-752
reference step: 5

ReferenceForCatalyticMechanism
reference index: 19
reference section: SCHEME 3