EzCatDB: D00258
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DB codeD00258
CATH domainDomain 13.90.1150.10 : Aspartate Aminotransferase, domain 1Catalytic domain
Domain 23.40.640.10 : Aspartate Aminotransferase; domain 2Catalytic domain
E.C.4.1.99.2
CSA2tpl

CATH domainRelated DB codes (homologues)
3.40.640.10 : Aspartate Aminotransferase; domain 2D00085,D00092,D00101,D00102,D00103,D00104,D00107,D00108,D00109,D00255,D00257,D00265,D00269,D00515,M00031,D00279
3.90.1150.10 : Aspartate Aminotransferase, domain 1D00085,D00092,D00101,D00102,D00103,D00104,D00107,D00108,D00109,D00255,D00257,D00265,D00269,D00515,M00031,D00279

Enzyme Name
UniProtKBKEGG

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
PfamPF01212 (Beta_elim_lyase)
[Graphical view]
PF01212 (Beta_elim_lyase)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00350Tyrosine metabolism
MAP00910Nitrogen metabolism

UniProtKB: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.

Compound table: links to PDB-related databases & PoSSuM

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
ChEBI18405
17895
58315
15377
15882
32816
16134
PubChem1051
6942100
6057
962
22247451
996
20488062
1060
222
              
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 UniProtKBP31013
[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 UniProtKBP31013
[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


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