EzCatDB: T00088

DB codeT00088
CATH domainDomain 13.40.50.1100Catalytic domain
Domain 23.40.50.1100Catalytic domain
Domain 33.40.1020.10
E.C.4.3.1.19
CSA1tdj

CATH domainRelated DB codes (homologues)
3.40.50.1100D00264,T00089

Enzyme Name
Swiss-protKEGG

P04968
Protein nameThreonine dehydratase biosyntheticthreonine ammonia-lyase
threonine deaminase
L-serine dehydratase
serine deaminase
L-threonine dehydratase
threonine dehydrase
L-threonine deaminase
threonine dehydratase
L-threonine hydro-lyase (deaminating)
L-threonine ammonia-lyase
SynonymsEC 4.3.1.19
Threonine deaminase

KEGG pathways
MAP codePathways
MAP00260Glycine, serine and threonine metabolism
MAP00290Valine, leucine and isoleucine biosynthesis

Swiss-prot:Accession NumberP04968
Entry nameTHD1_ECOLI
ActivityL-threonine = 2-oxobutanoate + NH(3).
SubunitHomotetramer.
Subcellular location
CofactorPyridoxal phosphate.


CofactorsSubstratesProducts
KEGG-idC00018C00188C00109C00014
CompoundPyridoxal phosphateL-Threonine2-OxobutanoateNH3
Typearomatic ring (with nitrogen atoms),phosphate group/phosphate ionamino acids,carbohydratecarbohydrate,carboxyl groupamine group,organic ion
1tdjA01Bound:PLPUnboundUnboundUnbound
1tdjA02UnboundUnboundUnboundUnbound
1tdjA03UnboundUnboundUnboundUnbound

Active-site residues
resource
literature [24]
pdbCatalytic residuesModified residues
1tdjA01LYS 62
LYS 62(PLP binding)
1tdjA02ASN 89

1tdjA03


References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[24]p.468

references
[1]
PubMed ID235965
JournalBiochemistry
Year1975
Volume14
Pages1760-7
AuthorsFeldman DA, Datta P
TitleCatabolite inactivation of biodegradative threonine dehydratase of Escherichia coli.
[2]
PubMed ID1096954
JournalBiochim Biophys Acta
Year1975
Volume397
Pages220-30
AuthorsKoerner K, Rahimi-Laridjani I, Grimminger H
TitlePurification of biosynthetic threonine deaminase from Escherichia coli.
[3]
PubMed ID986166
JournalBiochemistry
Year1976
Volume15
Pages3745-9
AuthorsKapke G, Davis L
TitleStereochemistry of the reaction of sheep liver threonine dehydratase. A nuclear magnetic resonance and optical rotatory dispersion study of its reaction pathway and products.
[4]
PubMed ID1262564
JournalJ Dairy Res
Year1976
Volume43
Pages75-83
AuthorsLees GJ, Jago GR
TitleFormation of acetaldehyde from threonine by lactic acid bacteria.
[5]
PubMed ID885705
JournalItal J Biochem
Year1977
Volume26
Pages144-61
AuthorsPagani R, Lusini P, Di Stefano A, Aleo F, Marinello E
TitlePurification and properties of rat liver L-threonine deaminase.
[6]
PubMed ID909449
JournalMethods Enzymol
Year1977
Volume46
Pages59-69
AuthorsPhillips AT
TitleDifferential labeling: a general technique for selective modification of binding sites.
[7]
PubMed ID350274
JournalBiochemistry
Year1978
Volume17
Pages1691-9
AuthorsBhadra R, Datta P
TitleAllosteric inhibition and catabolite inactivation of purified biodegradative threonine dehydratase of Salmonella typhimurium.
[8]
PubMed ID342520
JournalJ Biol Chem
Year1978
Volume253
Pages1245-51
AuthorsHofler JG, Burns RO
TitleThreonine deaminase from Salmonella typhimurium. Effect of regulatory ligands on the binding of substrates and substrate analogues to the active sites and the differentiation of the activator and inhibitor sites from the active sites.
[9]
PubMed ID438181
JournalJ Biol Chem
Year1979
Volume254
Pages4126-31
AuthorsDavis L
TitleFunctional and stereochemical specificity at the beta carbon atom of substrates in threonine dehydratase-catalyzed alpha,beta elimination reactions.
[10]
PubMed ID7016853
JournalJ Biol Chem
Year1981
Volume256
Pages5362-7
AuthorsPark LS, Datta P
TitleMechanism of catabolite inactivation of Escherichia coli biodegradative threonine dehydratase by glyoxylate.
[11]
PubMed ID3929853
JournalBiosci Rep
Year1985
Volume5
Pages499-508
AuthorsLeoncini R, Pagani R, Casella A, Marinello E
TitleRat liver L-threonine deaminase: properties and purification.
[12]
PubMed ID3053659
JournalJ Bacteriol
Year1988
Volume170
Pages5352-9
AuthorsGoss TJ, Schweizer HP, Datta P
TitleMolecular characterization of the tdc operon of Escherichia coli K-12.
[13]
PubMed ID2674117
JournalJ Biol Chem
Year1989
Volume264
Pages15818-23
AuthorsOgawa H, Gomi T, Konishi K, Date T, Nakashima H, Nose K, Matsuda Y, Peraino C, Pitot HC, Fujioka M
TitleHuman liver serine dehydratase. cDNA cloning and sequence homology with hydroxyamino acid dehydratases from other sources.
[14]
PubMed ID2015295
JournalBiochim Biophys Acta
Year1991
Volume1077
Pages233-40
AuthorsPagani R, Ponticelli F, Terzuoli L, Leoncini R, Marinello E
TitleThe inhibition of rat liver threonine dehydratase by carbamoyl-phosphate. The formation of carbamoylpyridoxal 5'-phosphate.
[15]
PubMed ID8240316
JournalBioessays
Year1993
Volume15
Pages625-34
AuthorsChangeux JP
TitleAllosteric proteins: from regulatory enzymes to receptors--personal recollections.
[16]
PubMed ID8407838
JournalJ Bacteriol
Year1993
Volume175
Pages6605-13
AuthorsFisher KE, Eisenstein E
TitleAn efficient approach to identify ilvA mutations reveals an amino-terminal catalytic domain in biosynthetic threonine deaminase from Escherichia coli.
[17]
PubMed ID8413189
JournalMol Gen Genet
Year1993
Volume240
Pages395-402
AuthorsGanduri YL, Sadda SR, Datta MW, Jambukeswaran RK, Datta P
TitleTdcA, a transcriptional activator of the tdcABC operon of Escherichia coli, is a member of the LysR family of proteins.
[18]
PubMed ID7815942
JournalMol Microbiol
Year1994
Volume13
Pages833-42
AuthorsMockel B, Eggeling L, Sahm H
TitleThreonine dehydratases of Corynebacterium glutamicum with altered allosteric control: their generation and biochemical and structural analysis.
[19]
PubMed ID7703851
JournalProtein Sci
Year1994
Volume3
Pages2055-63
AuthorsMatsuo Y, Nishikawa K
TitleProtein structural similarities predicted by a sequence-structure compatibility method.
[20]
PubMed ID7840631
JournalArch Biochem Biophys
Year1995
Volume316
Pages311-8
AuthorsEisenstein E
TitleAllosteric regulation of biosynthetic threonine deaminase from Escherichia coli: effects of isoleucine and valine on active-site ligand binding and catalysis.
[21]
PubMed ID8659901
JournalAnn N Y Acad Sci
Year1996
Volume782
Pages25-39
AuthorsSahm H, Eggeling L, Eikmanns B, Kramer R
TitleConstruction of L-lysine-, L-threonine-, and L-isoleucine-overproducing strains of Corynebacterium glutamicum.
[22]
PubMed ID9761930
JournalActa Crystallogr D Biol Crystallogr
Year1998
Volume54
Pages467-9
AuthorsGallagher DT, Eisenstein E, Fisher KE, Zondlo J, Chinchilla D, Yu HD, Dill J, Winborne E, Ducote K, Xiao G, Gilliland GL
TitlePolymorphous crystallization and diffraction of threonine deaminase from Escherichia coli.
[23]
PubMed ID9722552
JournalJ Biol Chem
Year1998
Volume273
Pages23219-24
AuthorsChinchilla D, Schwarz FP, Eisenstein E
TitleAmino acid substitutions in the C-terminal regulatory domain disrupt allosteric effector binding to biosynthetic threonine deaminase from Escherichia coli.
[24]
CommentsX-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS)
Medline ID98230745
PubMed ID9562556
JournalStructure
Year1998
Volume6
Pages465-75
AuthorsGallagher DT, Gilliland GL, Xiao G, Zondlo J, Fisher KE, Chinchilla D, Eisenstein E
TitleStructure and control of pyridoxal phosphate dependent allosteric threonine deaminase.
Related PDB1tdj
Related Swiss-protP04968
[25]
PubMed ID9914259
JournalCurr Opin Struct Biol
Year1998
Volume8
Pages759-69
AuthorsJansonius JN
TitleStructure, evolution and action of vitamin B6-dependent enzymes.
[26]
PubMed ID11106492
JournalBiochemistry
Year2000
Volume39
Pages15136-43
AuthorsWessel PM, Graciet E, Douce R, Dumas R
TitleEvidence for two distinct effector-binding sites in threonine deaminase by site-directed mutagenesis, kinetic, and binding experiments.
[27]
PubMed ID10673430
JournalStructure Fold Des
Year2000
Volume8
PagesR1-6
AuthorsSchneider G, Kack H, Lindqvist Y
TitleThe manifold of vitamin B6 dependent enzymes.
[28]
PubMed ID11389597
JournalBiochemistry
Year2001
Volume40
Pages6836-44
AuthorsLee YT, Duggleby RG
TitleIdentification of the regulatory subunit of Arabidopsis thaliana acetohydroxyacid synthase and reconstitution with its catalytic subunit.
[29]
PubMed ID11751050
JournalCurr Opin Struct Biol
Year2001
Volume11
Pages694-700
AuthorsChipman DM, Shaanan B
TitleThe ACT domain family.
[30]
PubMed ID12427039
JournalBiochemistry
Year2002
Volume41
Pages13767-73
AuthorsHalgand F, Wessel PM, Laprevote O, Dumas R
TitleBiochemical and mass spectrometric evidence for quaternary structure modifications of plant threonine deaminase induced by isoleucine.

comments
This enzyme was transferred from 4.2.1.16 to 4.3.1.19.
This enzyme belongs to type-II PLP-dependent enzyme superfamily (or Tryptophan synthase beta-subunit family), according to the literature [25] & [27].
Although the catalytic mechanism of this enzyme has not been elucidated, this enzyme probably catalyzes the following reactions, considering those of other PLP-dependent enzymes (see [25]):
(A) Formation of external aldimine (with amine group of Threonine substrate),
(B) Isomerization (change in the position of double-bond),
(C) Elimination of hydroxyl group, forming double bonded carbon atoms, leading to aminoacrylate intermediate,
(D) Formation of internal aldimine, leading to the elimination of imine intermediate from PLP,
(E) Schiff-base deforming of the imine product (by hydration), producing ammonia and oxobutanoate.

createdupdated
2004-06-072009-02-26


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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