EzCatDB: D00257
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DB codeD00257
CATH domainDomain 13.90.1150.10 : Aspartate Aminotransferase, domain 1
Domain 23.40.640.10 : Aspartate Aminotransferase; domain 2Catalytic domain
E.C.4.1.99.1
CSA1ax4

CATH domainRelated DB codes (homologues)
3.40.640.10 : Aspartate Aminotransferase; domain 2D00085,D00092,D00101,D00102,D00103,D00104,D00107,D00108,D00109,D00255,D00258,D00265,D00269,D00515,M00031,D00279
3.90.1150.10 : Aspartate Aminotransferase, domain 1D00085,D00092,D00101,D00102,D00103,D00104,D00107,D00108,D00109,D00255,D00258,D00265,D00269,D00515,M00031,D00279

Enzyme Name
UniProtKBKEGG

P28796
Protein nameTryptophanasetryptophanase
L-tryptophanase
L-tryptophan indole-lyase (deaminating)
SynonymsEC 4.1.99.1
L-tryptophan indole-lyase
TNase
PfamPF01212 (Beta_elim_lyase)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00380Tryptophan metabolism
MAP00910Nitrogen metabolism

UniProtKB:Accession NumberP28796
Entry nameTNAA_PROVU
ActivityL-tryptophan + H(2)O = indole + pyruvate + NH(3).
SubunitHomotetramer.
Subcellular location
CofactorPyridoxal phosphate.

Compound table: links to PDB-related databases & PoSSuM

CofactorsSubstratesProducts
KEGG-idC00018C00238C00078C00001C00463C00022C00014
CompoundPyridoxal phosphatePotassiumL-TryptophanH2OIndolePyruvateNH3
Typearomatic ring (with nitrogen atoms),phosphate group/phosphate ionunivalent metal (Na+, K+)amino acids,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms)H2Oaromatic ring (only carbon atom),aromatic ring (with nitrogen atoms)carbohydrate,carboxyl groupamine group,organic ion
ChEBI18405
29103
16828
57912
15377
16881
32816
16134
PubChem1051
813
6923516
6305
962
22247451
798
1060
222
               
1ax4A01UnboundUnboundUnbound UnboundUnboundUnbound
1ax4B01UnboundUnboundUnbound UnboundUnboundUnbound
1ax4C01UnboundUnboundUnbound UnboundUnboundUnbound
1ax4D01UnboundUnboundUnbound UnboundUnboundUnbound
1ax4A02Analogue:LLPBound:__KUnbound UnboundUnboundUnbound
1ax4B02Analogue:LLPBound:__KUnbound UnboundUnboundUnbound
1ax4C02Analogue:LLPBound:__KUnbound UnboundUnboundUnbound
1ax4D02Analogue:LLPBound:__KUnbound UnboundUnboundUnbound

Active-site residues
resource
literature [17]
pdbCatalytic residuesCofactor-binding residuesModified residues
           
1ax4A01 
GLY 53(Potassium binding)
 
1ax4B01 
GLY 53(Potassium binding)
 
1ax4C01 
GLY 53(Potassium binding)
 
1ax4D01 
GLY 53(Potassium binding)
 
1ax4A02ARG 226;LLP 266
GLU 70;ASN 271(Potassium binding)
LLP 266(PLP-bound to Lys)
1ax4B02ARG 226;LLP 266
GLU 70;ASN 271(Potassium binding)
LLP 266(PLP-bound to Lys)
1ax4C02ARG 226;LLP 266
GLU 70;ASN 271(Potassium binding)
LLP 266(PLP-bound to Lys)
1ax4D02ARG 226;LLP 266
GLU 70;ASN 271(Potassium binding)
LLP 266(PLP-bound to Lys)

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[7]SCHEME 2A
[8]Fig.5, p.73433
[12]SCHEME I
[14]Fig.1
[17]Figure 1p.604
[19]Fig. 3
[20]Scheme 3, p.21595-215973

references
[1]
PubMed ID4575958
JournalBiochem Biophys Res Commun
Year1973
Volume52
Pages482-8
AuthorsIkeda S, Fukui S
TitlePreparation of pyridoxal 5'-phosphate-bound sepharose and its use for immobilization of tryptophanase.
[2]
PubMed ID20936
JournalBiochemistry
Year1977
Volume16
Pages4584-90
AuthorsRitchey JM, Gibbons I, Schachman HK
TitleReactivation of enzymes by light-stimulated cleavage of reduced pyridoxal 5'-phosphate-enzyme complexes.
[3]
PubMed ID6339506
JournalJ Biol Chem
Year1983
Volume258
Pages4839-41
AuthorsSchnackerz KD, Snell EE
TitlePhosphorus 31 nuclear magnetic resonance study of tryptophanase. Pyridoxal phosphate-binding site.
[4]
PubMed ID6728845
JournalProg Clin Biol Res
Year1984
Volume144A
Pages195-208
AuthorsSchnackerz KD
TitlePhosphorus-31 nuclear magnetic resonance studies on four pyridoxal 5'-phosphate dependent enzymes.
[5]
PubMed ID3888623
JournalEur J Biochem
Year1985
Volume149
Pages129-33
AuthorsNihira T, Yasuda T, Kakizono T, Taguchi H, Ichikawa M, Toraya T, Fukui S
TitleFunctional role of cysteinyl residues in tryptophanase.
[6]
PubMed ID3524569
JournalBiochem Biophys Res Commun
Year1986
Volume137
Pages964-9
AuthorsKakizono T, Nihira T, Taguchi H
TitleCatalytic function of a tyrosyl residue in tryptophanase.
[7]
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.
[8]
PubMed ID3061452
JournalBiochemistry
Year1988
Volume27
Pages7339-44
AuthorsKiick DM, Phillips RS
TitleMechanistic deductions from multiple kinetic and solvent deuterium isotope effects and pH studies of pyridoxal phosphate dependent carbon-carbon lyases: Escherichia coli tryptophan indole-lyase.
[9]
PubMed ID2178632
JournalBiotechnol Appl Biochem
Year1990
Volume12
Pages28-33
AuthorsTani S, Tsujimoto N, Kawata Y, Tokushige M
TitleOverproduction and crystallization of tryptophanase from recombinant cells of Escherichia coli.
[10]
PubMed ID2069576
JournalBiochem Biophys Res Commun
Year1991
Volume178
Pages385-92
AuthorsMetzler CM, Metzler DE, Kintanar A, Scott RD, Marceau M
TitleNMR spectra of exchangeable protons of pyridoxal phosphate-dependent enzymes.
[11]
PubMed ID2060649
JournalFEBS Lett
Year1991
Volume284
Pages270-2
AuthorsKawata Y, Tani S, Sato M, Katsube Y, Tokushige M
TitlePreliminary X-ray crystallographic analysis of tryptophanase from Escherichia coli.
[12]
PubMed ID1632641
JournalArch Biochem Biophys
Year1992
Volume296
Pages489-96
AuthorsPhillips RS, Dua RK
TitleIndole protects tryptophan indole-lyase, but not tryptophan synthase, from inactivation by trifluoroalanine.
[13]
PubMed ID1372930
JournalJ Gen Microbiol
Year1992
Volume138
Pages211-6
AuthorsHart S, Koch KR, Woods DR
TitleIdentification of indigo-related pigments produced by Escherichia coli containing a cloned Rhodococcus gene.
[14]
PubMed ID7849621
JournalBiochem Mol Biol Int
Year1994
Volume34
Pages209-16
AuthorsFaleev NG, Dementieva IS, Zakomirdina LN, Gogoleva OI, Belikov VM
TitleTryptophanase from Escherichia coli: catalytic and spectral properties in water-organic solvents.
[15]
PubMed ID8289300
JournalJ Mol Biol
Year1994
Volume235
Pages783-6
AuthorsDementieva IS, Zakomirdina LN, Sinitzina NI, Antson AA, Wilson KS, Isupov MN, Lebedev AA, Harutyunyan EH
TitleCrystallization and preliminary X-ray investigation of holotryptophanases from Escherichia coli and Proteus vulgaris.
[16]
PubMed ID9485457
JournalBiochemistry
Year1998
Volume37
Pages3043-52
AuthorsIkushiro H, Hayashi H, Kawata Y, Kagamiyama H
TitleAnalysis of the pH- and ligand-induced spectral transitions of tryptophanase: activation of the coenzyme at the early steps of the catalytic cycle.
[17]
CommentsX-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
Medline ID98212457
PubMed ID9551100
JournalJ Mol Biol
Year1998
Volume276
Pages603-23
AuthorsIsupov MN, Antson AA, Dodson EJ, Dodson GG, Dementieva IS, Zakomirdina LN, Wilson KS, Dauter Z, Lebedev AA, Harutyunyan EH
TitleCrystal structure of tryptophanase.
Related PDB1ax4
Related UniProtKBP28796
[18]
PubMed ID10469830
JournalProtein Eng
Year1999
Volume12
Pages687-92
AuthorsKudo H, Natsume R, Nishiyama M, Horinouchi S
TitleAnalysis of stability and catalytic properties of two tryptophanases from a thermophile.
[19]
PubMed ID11011151
JournalJ Biochem (Tokyo)
Year2000
Volume128
Pages679-86
AuthorsJhee KH, Yoshimura T, Miles EW, Takeda S, Miyahara I, Hirotsu K, Soda K, Kawata Y, Esaki N
TitleStereochemistry of the transamination reaction catalyzed by aminodeoxychorismate lyase from Escherichia coli: close relationship between fold type and stereochemistry.
[20]
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
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).

createdupdated
2004-06-072009-02-26


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