EzCatDB: D00524
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DB codeD00524
CATH domainDomain 13.40.30.10 : GlutaredoxinCatalytic domain
Domain 21.20.1050.10 : Glutathione S-transferase Yfyf (Class Pi); Chain A, domain 2Catalytic domain
E.C.2.5.1.18,1.11.1.9


Enzyme Name
UniProtKBKEGG

P30711P0CG30P0CG29
Protein nameGlutathione S-transferase theta-1Glutathione S-transferase theta-2BGlutathione S-transferase theta-2Glutathione transferase
   (EC 2.5.1.18)

Glutathione S-transferase
   (EC 2.5.1.18)

Glutathione S-alkyltransferase
   (EC 2.5.1.18)

Glutathione S-aryltransferase
   (EC 2.5.1.18)

S-(Hydroxylalkyl)-glutathione liase
   (EC 2.5.1.18)

Glutathione S-aralkyltransferase
   (EC 2.5.1.18)

Glutathione peroxidase
   (EC 1.11.1.9)

GSH peroxidase
   (EC 1.11.1.9)

Selenium-glutathione peroxidase
   (EC 1.11.1.9)

Reduced glutathione peroxidase
   (EC 1.11.1.9)

SynonymsEC 2.5.1.18
GST class-theta-1
Glutathione transferase T1-1
EC 2.5.1.18
GST class-theta-2
Glutathione S-transferase theta-2
EC 2.5.1.18
GST class-theta-2
RefSeqNP_000844.2 (Protein)
NM_000853.2 (DNA/RNA sequence)
NP_000845.1 (Protein)
NM_000854.3 (DNA/RNA sequence)
NP_001074312.1 (Protein)
NM_001080843.2 (DNA/RNA sequence)

PfamPF00043 (GST_C)
PF02798 (GST_N)
[Graphical view]
PF00043 (GST_C)
PF02798 (GST_N)
[Graphical view]
PF00043 (GST_C)
PF02798 (GST_N)
[Graphical view]

KEGG pathways
MAP codePathwaysE.C.
MAP00480Glutathione metabolism2.5.1.18,1.11.1.9
MAP00980Metabolism of xenobiotics by cytochrome P4502.5.1.18
MAP00982Drug metabolism - cytochrome P4502.5.1.18
MAP00590Arachidonic acid metabolism1.11.1.9

UniProtKB:Accession NumberP30711P0CG30P0CG29
Entry nameGSTT1_HUMANGSTT2_HUMANGST2_HUMAN
ActivityRX + glutathione = HX + R-S-glutathione.RX + glutathione = HX + R-S-glutathione.RX + glutathione = HX + R-S-glutathione.
SubunitHomodimer.Homodimer.Homodimer.
Subcellular locationCytoplasm.Cytoplasm.Cytoplasm.
Cofactor



Compound table: links to PDB-related databases & PoSSuM

SubstratesProducts
KEGG-idC01322C00051C16738L00111C00722C01372C15498C01318C02320C00059L00112L00113L00114C01335C00127C00001
E.C.2.5.1.182.5.1.18,1.11.1.92.5.1.182.5.1.182.5.1.182.5.1.181.11.1.92.5.1.182.5.1.182.5.1.182.5.1.182.5.1.182.5.1.181.11.1.91.11.1.91.11.1.9
CompoundRXGlutathioneSulfuric monoester1-menaphthyl sulfateEpoxideAlkeneROOHHXR-S-Glutathionesulfate1-menaphthyl glutathioneGlutathione-conjugated alcoholGlutathione-conjugated compoundROHGlutathione disulfideWater
Typehalideamino acids,carboxyl group,peptide/protein,sulfhydryl groupsulfate grouparomatic ring (only carbon atom),sulfate groupcarbohydratelipidothershalideamide group,carboxyl group,peptide/protein,sulfide groupsulfate groupamide group,aromatic ring (only carbon atom),carboxyl group,peptide/protein,sulfide groupamide group,carbohydrate,carboxyl group,peptide/protein,sulfide groupamide group,carboxyl group,peptide/protein,sulfide groupcarbohydrateamino acids,carboxyl group,peptide/protein,disulfide bondH2O
ChEBI
16856







26836




17858
15377
PubChem
25246407
124886

33524





5152822
22066174
1118
449471



65359
11215652
962
22247451
                        
2c3nA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound 
2c3nB01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound 
2c3nC01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound 
2c3nD01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound 
2c3qA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundBound:GTXUnboundUnboundUnboundUnboundUnboundUnbound 
2c3qB01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundBound:GTXUnboundUnboundUnboundUnboundUnboundUnbound 
2c3qC01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundBound:GTXUnboundUnboundUnboundUnboundUnboundUnbound 
2c3qD01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundBound:GTXUnboundUnboundUnboundUnboundUnboundUnbound 
2c3tA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound 
2c3tB01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound 
2c3tC01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound 
2c3tD01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound 
1ljrA01UnboundBound:GSHUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound 
1ljrB01UnboundBound:GSHUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound 
2ljrA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound 
2ljrB01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound 
3ljrA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundBound:GGCUnboundUnboundUnboundUnbound 
3ljrB01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundBound:GGCUnboundUnboundUnboundUnbound 
4mpgA01UnboundBound:GSHUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound 
4mpgB01UnboundBound:GSHUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound 
4mpfA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound 
4mpfB01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound 
2c3nA02UnboundUnboundUnboundUnboundUnboundUnboundUnboundBound:IODUnboundUnboundUnboundUnboundUnboundUnboundUnbound 
2c3nB02UnboundUnboundUnboundUnboundUnboundUnboundUnboundBound:IODUnboundUnboundUnboundUnboundUnboundUnboundUnbound 
2c3nC02UnboundUnboundUnboundUnboundUnboundUnboundUnboundBound:IODUnboundUnboundUnboundUnboundUnboundUnboundUnbound 
2c3nD02UnboundUnboundUnboundUnboundUnboundUnboundUnboundBound:IODUnboundUnboundUnboundUnboundUnboundUnboundUnbound 
2c3qA02UnboundUnboundUnboundUnboundUnboundUnboundUnboundBound:IODUnboundUnboundUnboundUnboundUnboundUnboundUnbound 
2c3qB02UnboundUnboundUnboundUnboundUnboundUnboundUnboundBound:IODUnboundUnboundUnboundUnboundUnboundUnboundUnbound 
2c3qC02UnboundUnboundUnboundUnboundUnboundUnboundUnboundBound:IODUnboundUnboundUnboundUnboundUnboundUnboundUnbound 
2c3qD02UnboundUnboundUnboundUnboundUnboundUnboundUnboundBound:IODUnboundUnboundUnboundUnboundUnboundUnboundUnbound 
2c3tA02UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound 
2c3tB02UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound 
2c3tC02UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound 
2c3tD02UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound 
1ljrA02UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound 
1ljrB02UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound 
2ljrA02UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound 
2ljrB02UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound 
3ljrA02UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundBound:SO4UnboundUnboundUnboundUnboundUnbound 
3ljrB02UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundBound:SO4UnboundUnboundUnboundUnboundUnbound 
4mpgA02UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound 
4mpgB02UnboundUnboundUnboundAnalogue:UNLUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound 
4mpfA02UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundAnalogue:PO4UnboundUnboundUnboundUnboundUnbound 
4mpfB02UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundAnalogue:PO4UnboundUnboundUnboundUnboundUnbound 

Active-site residues
resource
literature [1] and [6]
pdbCatalytic residuescomment
          
2c3nA01SER 11
 
2c3nB01SER 11
 
2c3nC01SER 11
 
2c3nD01SER 11
 
2c3qA01SER 11
 
2c3qB01SER 11
 
2c3qC01SER 11
 
2c3qD01SER 11
 
2c3tA01SER 11
 
2c3tB01SER 11
 
2c3tC01SER 11
 
2c3tD01SER 11
 
1ljrA01SER 11
 
1ljrB01SER 11
 
2ljrA01SER 11
 
2ljrB01SER 11
 
3ljrA01SER 11
 
3ljrB01SER 11
 
4mpgA01SER 11
 
4mpgB01SER 11
 
4mpfA01SER 11
 
4mpfB01SER 11
 
2c3nA02ARG 107
 
2c3nB02ARG 107
 
2c3nC02ARG 107
 
2c3nD02ARG 107
 
2c3qA02ARG 107
mutant W234R
2c3qB02ARG 107
mutant W234R
2c3qC02ARG 107
mutant W234R
2c3qD02ARG 107
mutant W234R
2c3tA02ARG 107
mutant W234R
2c3tB02ARG 107
mutant W234R
2c3tC02ARG 107
mutant W234R
2c3tD02ARG 107
mutant W234R
1ljrA02ARG 107
 
1ljrB02ARG 107
 
2ljrA02ARG 107
 
2ljrB02ARG 107
 
3ljrA02ARG 107
 
3ljrB02ARG 107
 
4mpgA02ARG 107
 
4mpgB02ARG 107
 
4mpfA02ARG 107
 
4mpfB02ARG 107
 

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[6]p.317-318
[7]Fig.1
[9]p.249-253
[14]


references
[1]
PubMed ID7575461
JournalBiochem J
Year1995
Volume311
Pages247-50
AuthorsBoard PG, Coggan M, Wilce MC, Parker MW
TitleEvidence for an essential serine residue in the active site of the Theta class glutathione transferases.
[2]
PubMed ID8870684
JournalBiochem J
Year1996
Volume319
Pages315-21
AuthorsTan KL, Chelvanayagam G, Parker MW, Board PG
TitleMutagenesis of the active site of the human Theta-class glutathione transferase GSTT2-2: catalysis with different substrates involves different residues.
[3]
PubMed ID9074797
JournalChem Res Toxicol
Year1997
Volume10
Pages2-18
AuthorsArmstrong RN
TitleStructure, catalytic mechanism, and evolution of the glutathione transferases.
[4]
PubMed ID9307035
JournalBiochem J
Year1997
Volume326
Pages837-46
AuthorsSherratt PJ, Pulford DJ, Harrison DJ, Green T, Hayes JD
TitleEvidence that human class Theta glutathione S-transferase T1-1 can catalyse the activation of dichloromethane, a liver and lung carcinogen in the mouse. Comparison of the tissue distribution of GST T1-1 with that of classes Alpha, Mu and Pi GST in human.
[5]
PubMed ID9434735
JournalArch Biochem Biophys
Year1997
Volume348
Pages247-54
AuthorsJemth P, Mannervik B
TitleKinetic characterization of recombinant human glutathione transferase T1-1, a polymorphic detoxication enzyme.
[6]
CommentsX-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS).
PubMed ID9551553
JournalStructure
Year1998
Volume6
Pages309-22
AuthorsRossjohn J, McKinstry WJ, Oakley AJ, Verger D, Flanagan J, Chelvanayagam G, Tan KL, Board PG, Parker MW
TitleHuman theta class glutathione transferase: the crystal structure reveals a sulfate-binding pocket within a buried active site.
Related PDB1ljr,2ljr,3ljr
Related UniProtKBP0CG30
[7]
PubMed ID10190541
JournalChem Biol Interact
Year1999
Volume117
Pages1-14
AuthorsBogaards JJ, Venekamp JC, Salmon FG, van Bladeren PJ
TitleConjugation of isoprene monoepoxides with glutathione, catalyzed by alpha, mu, pi and theta-class glutathione S-transferases of rat and man.
[8]
PubMed ID10548067
JournalProtein Sci
Year1999
Volume8
Pages2205-12
AuthorsFlanagan JU, Rossjohn J, Parker MW, Board PG, Chelvanayagam G
TitleMutagenic analysis of conserved arginine residues in and around the novel sulfate binding pocket of the human Theta class glutathione transferase T2-2.
[9]
PubMed ID11018744
JournalMutat Res
Year2000
Volume463
Pages247-83
AuthorsLandi S
TitleMammalian class theta GST and differential susceptibility to carcinogens: a review.
[10]
PubMed ID12054768
JournalJ Mol Biol
Year2002
Volume318
Pages59-70
AuthorsBroo K, Larsson AK, Jemth P, Mannervik B
TitleAn ensemble of theta class glutathione transferases with novel catalytic properties generated by stochastic recombination of fragments of two mammalian enzymes.
[11]
PubMed ID11884241
JournalToxicol Appl Pharmacol
Year2002
Volume179
Pages89-97
AuthorsSherratt PJ, Williams S, Foster J, Kernohan N, Green T, Hayes JD
TitleDirect comparison of the nature of mouse and human GST T1-1 and the implications on dichloromethane carcinogenicity.
[12]
PubMed ID14615977
JournalChem Res Toxicol
Year2003
Volume16
Pages1493-9
AuthorsGuengerich FP, McCormick WA, Wheeler JB
TitleAnalysis of the kinetic mechanism of haloalkane conjugation by mammalian theta-class glutathione transferases.
[13]
PubMed ID12588193
JournalChem Res Toxicol
Year2003
Volume16
Pages216-26
AuthorsRoss MK, Pegram RA
TitleGlutathione transferase theta 1-1-dependent metabolism of the water disinfection byproduct bromodichloromethane.
[14]
PubMed ID12542971
JournalJ Biochem Mol Biol
Year2003
Volume36
Pages20-7
AuthorsGuengerich FP
TitleActivation of dihaloalkanes by thiol-dependent mechanisms.
[15]
CommentsX-RAY CRYSTALLOGRAPHY.
PubMed ID16298388
JournalJ Mol Biol
Year2006
Volume355
Pages96-105
AuthorsTars K, Larsson AK, Shokeer A, Olin B, Mannervik B, Kleywegt GJ
TitleStructural basis of the suppressed catalytic activity of wild-type human glutathione transferase T1-1 compared to its W234R mutant.
Related PDB2c3n,2c3t,2c3q
[16]
PubMed ID17011574
JournalJ Mol Biol
Year2006
Volume364
Pages400-10
AuthorsGriswold KE, Aiyappan NS, Iverson BL, Georgiou G
TitleThe evolution of catalytic efficiency and substrate promiscuity in human theta class 1-1 glutathione transferase.
[17]
PubMed ID19664997
JournalArch Biochem Biophys
Year2009
Volume490
Pages24-9
AuthorsJosephy PD, Kent M, Mannervik B
TitleSingle-nucleotide polymorphic variants of human glutathione transferase T1-1 differ in stability and functional properties.
[18]
PubMed ID20097269
JournalBiochim Biophys Acta
Year2010
Volume1800
Pages466-73
AuthorsShokeer A, Mannervik B
TitleResidue 234 is a master switch of the alternative-substrate activity profile of human and rodent theta class glutathione transferase T1-1.
[19]
PubMed ID24756107
JournalPLoS Biol
Year2014
Volume12
Pagese1001843
AuthorsMashiyama ST, Malabanan MM, Akiva E, Bhosle R, Branch MC, Hillerich B, Jagessar K, Kim J, Patskovsky Y, Seidel RD, Stead M, Toro R, Vetting MW, Almo SC, Armstrong RN, Babbitt PC
TitleLarge-scale determination of sequence, structure, and function relationships in cytosolic glutathione transferases across the biosphere.

comments
Cytosolic glutathione transferases (GSTs), with EC number 2.5.1.18, comprise a large superfamily, to which this enzyme belongs (see [3], [19]). cytosolic GSTs catalyze various reactions, such as nucleophilic substitution, nucleophilic addition, epoxide ring opening, isomerization, hydrolytic dehalogenation, disulfide reductase, peroxidase, thiocyanate reductase, reductive dehalogenation, deglutathionylation (see [19]). These reactions can be classified into three categories: (1) reactions where glutathione (GSH) is consumed, (2) reactions where GSH is not consumed, and (3) reactions where two GSH molecules are oxidized to produce GSSG (see [19]).
In addition to this superfamily, there are three more GST families with EC 2.5.1.18: (a) cytosolic GST kappa class with a thioredoxin domain (CATH 3.40.30.10), (b) membrane-bound GSTs (CATH 1.20.120.50), and (c) metal-dependent GST, which is called fosfomycin resistance protein (CATH 3.10.180.10) (see [3], [19]).
This enzyme class, the human theta class glutathione transferase (GST), is the most ancient class among other GSTs (see [9]).This enzyme class has a sulfatase activity and a halogenase activity, unlike the other classes of the homologous enzymes (GSTs), alpha, mu, pi and sigma (see [2], [6], [8] and [9]). In contrast, theta class enzyme lacks activity toward the model substrate, 1-chloro-2,4-dinitrobenzene (CDNB), compared to the other classes of GSTs (see [2], [8] and [9]).
In the sulfatase reaction for this enzyme class, 1-menaphthyl sulphate (MSu)(L00111) reacts with glutathione (C00051), giving rise to 1-menaphthyl glutathione conjugate (L00112) and sulfate (C00059) (see [2], [8], [9]). However, this reaction does not involve any water molecule, which is essential in hydrolysis of sulfatase reaction. Consequently, this reaction is similar to transfer reaction, in which sulfate is a leaving group instead of other substances such as halide ion. Thus, these reactions are classified as nucleophilic substitution (see [19]).
RX + Glutathione => HX + R-S-Glutathione; nucleophilic substitution for ordinary GST reaction;
MSu(L00111) + Glutathione => sulfate + 1-menaphthyl-glutathione(L00112); theta GST reaction
or
Sulfuric monoester(C16738) + Glutathione => sulfate + R-S-Glutathione; theta GST reaction
According to the literature [8], the interaction between Arg107 and the sulfate group of MSu (L00111) will lead to the the positive charge increases on the methyl carbon of MSu, giving rise to the carbonium cation. The thiolate group of glutathione may make a nucleophilic attack on the carbonium cation, to produce 1-menaphthyl glutathione and free sulfate (see [8]).
Human GSTT1-1 shows suppressed catalytic activity, due to Trp234 that is occupying a significant portion of the active site, compared to the counterpart enzyme, GSTT1-1, from mouse (see [15]). In contrast to the wild type, Trp234Arg mutant shows an enhanced activity, probably because Arg234 interacts with the carboxylate group of glutathione (see [15]).
In addition to these transfer reactions, this enzyme can catalyze the following reactions (see [19]):
Epoxide ring opening; Epoxide + Glutathione => Glutathione-conjucated alcohol(L00113)
Conjugate addition; Alkene + Glutathione => Glutathione-conjugated compound(L00114)
Peroxidase reaction; 2 x Glutathione + ROOH(hydroperoxide) => ROH + glutathione disulfide + H2O
Here, epoxide ring opening may be classified into intramolecular transfer reaction.
####
For GSTT1-1, the following substances can be substrates: dichloromethane (DCM), ethylene-dibromide (EDB), p-nitrobenzyl chloride (PNBC), p-nitrophenethyl bromide (PNPB), methyl chloride (MeC), methyl iodide (MeI), and various halogenated methanes and ethanes, 1,2-epoxy-3-(p-nitro-phenoxy)propane (EPNPP) and the isoprene monoepoxides 3,4 epoxy-3-methyl-1-butene (EPOX-I) and 3,4-epoxy-2-methyl-1-butene (EPOX-II). In addition, ethylene epoxide (EO) and 1,3-butadiene derivatives such as the 3,4-epoxybutene (MEB), and the 1,2,3,4-diepoxybutane (DEB) are highly suspected substrates for GSTT1-1 (see [9])
GSTT1-1 also shows a peroxidase activity towards phospholipid hydroperoxides, cumene hydroperoxide and t-butyl hydroperoxide, but not towards a range of secondary lipid-peroxidation products, such as the trans-alk-2-enals and trans,trans-alka-2,4-dienals (see [9]).
GSTT2-2, in contrast to GSTT1-1, shows a significant activity against most lipid peroxidation products or the polycyclic aromatic hydrocarbon (PAH) 5-hydroxy-methylchrysene and the food-derivative mutagen N-acetoxy-PhIP, although no activity was shown towards steroid hydroperoxides, EPNPP, and PNBC (see [9]).
GSTT2-2, but not GSTT1-1, also shows a sulfatase activity towards the menaphthyl sulfate [12] and the 1-methyl-sulfate (see [9]).

createdupdated
2009-02-042015-04-24


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 2008)
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)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
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