EzCatDB: D00258

DB codeD00258
CATH domainDomain 13.90.1150.10Catalytic domain
Domain 23.40.640.10Catalytic domain
E.C.4.1.99.2
CSA2tpl

CATH domainRelated DB codes (homologues)
3.40.640.10D00085,D00092,D00101,D00102,D00103,D00104,D00107,D00108,D00109,D00255,D00257,D00265,D00269,D00515,M00031,D00279
3.90.1150.10D00085,D00092,D00101,D00102,D00103,D00104,D00107,D00108,D00109,D00255,D00257,D00265,D00269,D00515,M00031,D00279

Enzyme Name
Swiss-protKEGG

P31013P31012
Protein nameTyrosine phenol-lyaseTyrosine phenol-lyasetyrosine phenol-lyase
beta-tyrosinase
L-tyrosine phenol-lyase (deaminating)
SynonymsEC 4.1.99.2
Beta-tyrosinase
EC 4.1.99.2
Beta-tyrosinase

KEGG pathways
MAP codePathways
MAP00350Tyrosine metabolism
MAP00910Nitrogen metabolism

Swiss-prot:Accession NumberP31013P31012
Entry nameTPL_CITFRTPL_ESCIN
ActivityL-tyrosine + H(2)O = phenol + pyruvate + NH(3).L-tyrosine + H(2)O = phenol + pyruvate + NH(3).
SubunitHomotetramer.Homotetramer.
Subcellular location

CofactorPyridoxal phosphate.Pyridoxal phosphate.


CofactorsSubstratesProducts
KEGG-idC00018C00082C00001C00146C00022C00014
CompoundPyridoxal phosphateL-TyrosineH2OPhenolPyruvateNH3
Typearomatic ring (with nitrogen atoms),phosphate group/phosphate ionamino acids,aromatic ring (only carbon atom)H2Oaromatic ring (only carbon atom)carbohydrate,carboxyl groupamine group,organic ion
1tplA01UnboundUnbound
UnboundUnboundUnbound
1tplB01UnboundUnbound
UnboundUnboundUnbound
2tplA01UnboundUnbound
UnboundUnboundUnbound
2tplB01UnboundAnalogue:HPP
UnboundUnboundUnbound
1tplA02UnboundUnbound
UnboundUnboundUnbound
1tplB02UnboundUnbound
UnboundUnboundUnbound
2tplA02UnboundUnbound
UnboundUnboundUnbound
2tplB02UnboundUnbound
UnboundUnboundUnbound

Active-site residues
resource
literature [10], [12], [16] & [18]
pdbCatalytic residuesCofactor-binding residuesModified residuescomment
1tplA01ARG 381
GLY 52(Monovalent cation)


1tplB01ARG 381
GLY 52(Monovalent cation)


2tplA01ARG 381
GLY 52(Monovalent cation)


2tplB01ARG 381
GLY 52(Monovalent cation)


1tplA02TYR 71;       ;LYS 257
GLU 69;ASN 262(Monovalent cation)
                        
invisible 123-131
1tplB02TYR 71;       ;LYS 257
GLU 69;ASN 262(Monovalent cation)
                        
invisible 123-131
2tplA02TYR 71;THR 124;       
GLU 69;ASN 262(Monovalent cation)
LLP 257(Modified by PLP)
LLP(modified Lys)
2tplB02TYR 71;THR 124;       
GLU 69;ASN 262(Monovalent cation)
LLP 257(Modified by PLP)
LLP(modified Lys)

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[6]Scheme 1, Scheme 2, p.399-4013
[10]Scheme 2, p.12282-122836
[12]Scheme 1, p.6509-65106
[14]SCHEME1, p.1324-13255
[15]Scheme 1, p.85554
[16]Scheme 1, p.6899-69007
[18]Scheme 3, p.751-7525
[19]SCHEME 3

references
[1]
PubMed ID1190012
JournalAdv Appl Microbiol
Year1975
Volume19
Pages249-88
AuthorsYamada H, Kumagai H
TitleSynthesis of L-tyrosine-related amino acids by beta-tyrosinase.
[2]
PubMed ID1147922
JournalBiochem Biophys Res Commun
Year1975
Volume64
Pages241-7
AuthorsRapp P, Kumagai H, Yamada H, Ueno T, Fukami H
TitleSynthesis of 2,3,4-trihydroxy-L-phenylalanine from s-methyl-L-cysteine and pyrogallol by L-tyrosine phenol-lyase.
[3]
PubMed ID1141596
JournalJ Am Chem Soc
Year1975
Volume97
Pages4334-7
AuthorsSawada S, Kumagai H, Yamada H, Hill RK
TitleStereochemistry of beta-replacement reactions catalyzed by tyrosine phenol-lyase.
[4]
PubMed ID721797
JournalJ Biochem (Tokyo)
Year1978
Volume84
Pages633-40
AuthorsMuro T, Nakatani H, Hiromi K, Kumagai H, Yamada H
TitleElementary processes in the interaction of tyrosine phenol lyase with inhibitors and substrate.
[5]
PubMed ID3111376
JournalArch Biochem Biophys
Year1987
Volume256
Pages302-10
AuthorsPhillips RS
TitleReactions of O-acyl-L-serines with tryptophanase, tyrosine phenol-lyase, and tryptophan synthase.
[6]
PubMed ID2847927
JournalEur J Biochem
Year1988
Volume177
Pages395-401
AuthorsFaleev NG, Ruvinov SB, Demidkina TV, Myagkikh IV, Gololobov MYu, Bakhmutov VI, Belikov VM
TitleTyrosine phenol-lyase from Citrobacter intermedius. Factors controlling substrate specificity.
[7]
PubMed ID3378628
JournalFEBS Lett
Year1988
Volume232
Pages381-2
AuthorsDemidkina TV, Myagkikh IV, Antson AA, Harutyunyan EH
TitleCrystallization and crystal data on tyrosine phenol-lyase.
[8]
CommentsX-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
Medline ID92290010
PubMed ID1601133
JournalFEBS Lett
Year1992
Volume302
Pages256-60
AuthorsAntson AA, Strokopytov BV, Murshudov GN, Isupov MN, Harutyunyan EH, Demidkina TV, Vassylyev DG, Dauter Z, Terry H, Wilson KS
TitleThe polypeptide chain fold in tyrosine phenol-lyase, a pyridoxal-5'-phosphate-dependent enzyme.
Related Swiss-protP31013
[9]
CommentsX-ray crystallography
PubMed ID7916622
JournalBiochemistry
Year1993
Volume32
Pages4195-206
AuthorsAntson AA, Demidkina TV, Gollnick P, Dauter Z, von Tersch RL, Long J, Berezhnoy SN, Phillips RS, Harutyunyan EH, Wilson KS
TitleThree-dimensional structure of tyrosine phenol-lyase.
Related PDB1tpl
[10]
PubMed ID7547970
JournalBiochemistry
Year1995
Volume34
Pages12276-83
AuthorsChen HY, Demidkina TV, Phillips RS
TitleSite-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.
[11]
PubMed ID8932517
JournalBiochem Mol Biol Int
Year1996
Volume38
Pages37-42
AuthorsPletnev SV, Isupov MN, Dauter Z, Wilson KS, Faleev NG, Harutyunyan EG, Demidkina TV
TitlePurification and crystals of tyrosine phenol-lyase from Erwinia herbicola.
[12]
CommentsX-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
Medline ID97317094
PubMed ID9174368
JournalBiochemistry
Year1997
Volume36
Pages6502-10
AuthorsSundararaju B, Antson AA, Phillips RS, Demidkina TV, Barbolina MV, Gollnick P, Dodson GG, Wilson KS
TitleThe 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.
Related PDB2tpl
Related Swiss-protP31013
[13]
PubMed ID10328314
JournalBioorg Med Chem Lett
Year1999
Volume9
Pages1205-8
AuthorsKim K, Cole PA
TitleSynthesis of (2S,3R)-beta-methyltyrosine catalyzed by tyrosine phenol-lyase.
[14]
PubMed ID9880502
JournalJ Biol Chem
Year1999
Volume274
Pages1320-5
AuthorsMouratou B, Kasper P, Gehring H, Christen P
TitleConversion of tyrosine phenol-lyase to dicarboxylic amino acid beta-lyase, an enzyme not found in nature.
[15]
PubMed ID10913261
JournalBiochemistry
Year2000
Volume39
Pages8546-55
AuthorsSundararaju B, Chen H, Shilcutt S, Phillips RS
TitleThe role of glutamic acid-69 in the activation of Citrobacter freundii tyrosine phenol-lyase by monovalent cations.
[16]
PubMed ID11082202
JournalEur J Biochem
Year2000
Volume267
Pages6897-902
AuthorsFaleev NG, Zhukov YN, Khurs EN, Gogoleva OI, Barbolina MV, Bazhulina NP, Belikov VM, Demidkina TV, Khomutov RM
TitleInteraction of tyrosine phenol-lyase with phosphoroorganic analogues of substrate amino acids.
[17]
PubMed ID11732906
JournalBiochemistry
Year2001
Volume40
Pages14862-8
AuthorsWatkins EB, Phillips RS
TitleInhibition of tyrosine phenol-lyase from Citrobacter freundii by 2-azatyrosine and 3-azatyrosine.
[18]
PubMed ID11964175
JournalBiochem J
Year2002
Volume363
Pages745-52
AuthorsDemidkina TV, Barbolina MV, Faleev NG, Sundararaju B, Gollnick PD, Phillips RS
TitleThreonine-124 and phenylalanine-448 in Citrobacter freundii tyrosine phenol-lyase are necessary for activity with L-tyrosine.
[19]
PubMed ID11934889
JournalJ Biol Chem
Year2002
Volume277
Pages21592-7
AuthorsPhillips RS, Demidkina TV, Zakomirdina LN, Bruno S, Ronda L, Mozzarelli A
TitleCrystals of tryptophan indole-lyase and tyrosine phenol-lyase form stable quinonoid complexes.

comments
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.

createdupdated
2004-07-012009-02-26


Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2010)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)

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