EzCatDB: S00243
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DB codeS00243
RLCP classification4.151.774000.401 : Addition
4.16.66400.7 : Addition
5.41.2776000.400 : Elimination
CATH domainDomain 13.20.20.70 : TIM BarrelCatalytic domain
E.C.2.5.1.54

CATH domainRelated DB codes (homologues)
3.20.20.70 : TIM BarrelS00215,S00217,S00218,S00219,S00532,S00198,S00220,S00745,S00537,S00538,S00539,S00826,S00841,S00235,S00239,S00240,S00244,S00199,S00200,S00201,S00221,S00222,S00847,S00224,S00225,S00226,D00014,D00029,M00141,T00015,T00239,D00664,D00665,D00804,D00863,T00089

Enzyme Name
UniProtKBKEGG

P0AB91P32449
Protein namePhospho-2-dehydro-3-deoxyheptonate aldolase, Phe-sensitivePhospho-2-dehydro-3-deoxyheptonate aldolase, tyrosine-inhibited3-deoxy-7-phosphoheptulonate synthase
2-dehydro-3-deoxy-phosphoheptonate aldolase
2-keto-3-deoxy-D-arabino-heptonic acid 7-phosphate synthetase
3-deoxy-D-arabino-2-heptulosonic acid 7-phosphate synthetase
3-deoxy-D-arabino-heptolosonate-7-phosphate synthetase
3-deoxy-D-arabino-heptulosonate 7-phosphate synthetase
7-phospho-2-keto-3-deoxy-D-arabino-heptonate D-erythrose-4-phosphatelyase (pyruvate-phosphorylating)
7-phospho-2-dehydro-3-deoxy-D-arabino-heptonateD-erythrose-4-phosphate lyase (pyruvate-phosphorylating)
D-erythrose-4-phosphate-lyase
D-erythrose-4-phosphate-lyase (pyruvate-phosphorylating)
DAH7-P synthase
DAHP synthase
DS-Co
DS-Mn
KDPH synthase
KDPH synthetase
deoxy-D-arabino-heptulosonate-7-phosphate synthetase
phospho-2-dehydro-3-deoxyheptonate aldolase
phospho-2-keto-3-deoxyheptanoate aldolase
phospho-2-keto-3-deoxyheptonate aldolase
phospho-2-keto-3-deoxyheptonic aldolase
phospho-2-oxo-3-deoxyheptonate aldolase
SynonymsEC 2.5.1.54
Phospho-2-keto-3-deoxyheptonate aldolase
3-deoxy-D-arabino-heptulosonate 7-phosphate synthase
DAHP synthetase
EC 2.5.1.54
Phospho-2-keto-3-deoxyheptonate aldolase
3-deoxy-D-arabino-heptulosonate 7-phosphate synthase
DAHP synthetase
RefSeqNP_415275.1 (Protein)
NC_000913.2 (DNA/RNA sequence)
YP_489027.1 (Protein)
NC_007779.1 (DNA/RNA sequence)
NP_009808.1 (Protein)
NM_001178597.1 (DNA/RNA sequence)
PfamPF00793 (DAHP_synth_1)
[Graphical view]
PF00793 (DAHP_synth_1)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00400Phenylalanine, tyrosine and tryptophan biosynthesis

UniProtKB:Accession NumberP0AB91P32449
Entry nameAROG_ECOLIAROG_YEAST
ActivityPhosphoenolpyruvate + D-erythrose 4-phosphate + H(2)O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate.Phosphoenolpyruvate + D-erythrose 4-phosphate + H(2)O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate.
SubunitHomotetramer.
Subcellular location

Cofactor


Compound table: links to PDB-related databases & PoSSuM

CofactorsSubstratesProductsintermediates
KEGG-idC00034C00074C00279C00001C04691C00009

CompoundManganesePhosphoenolpyruvateD-Erythrose 4-phosphateH2O2-Dehydro-3-deoxy-D-arabino-heptonate 7-phosphateOrthophosphateTransition-state with an oxocarbenium ionA linear tetrahedral intermediate
Typeheavy metalcarboxyl group,phosphate group/phosphate ioncarbohydrate,phosphate group/phosphate ionH2Ocarbohydrate,carboxyl group,phosphate group/phosphate ionphosphate group/phosphate ion

ChEBI18291
35154
44897
48153
15377
18150
26078


PubChem23930
59658623
58114173
1005
122357
962
22247451
160647
22486802
1004


                
1gg1ABound:_MNAnalogue:PGAUnbound UnboundAnalogue:SO4 1373UnboundUnbound
1gg1BBound:_MNAnalogue:PGAUnbound UnboundAnalogue:SO4 2373UnboundUnbound
1gg1CBound:_MNAnalogue:PGAUnbound UnboundAnalogue:SO4 3373UnboundUnbound
1gg1DBound:_MNAnalogue:PGAUnbound UnboundAnalogue:SO4 4373UnboundUnbound
1qr7AAnalogue:_PBBound:PEPUnbound UnboundAnalogue:SO4UnboundUnbound
1qr7BAnalogue:_PBBound:PEPUnbound UnboundAnalogue:SO4UnboundUnbound
1qr7CAnalogue:_PBBound:PEPUnbound UnboundAnalogue:SO4UnboundUnbound
1qr7DAnalogue:_PBBound:PEPUnbound UnboundAnalogue:SO4UnboundUnbound
1kflABound:_MNBound:PEPUnbound UnboundUnboundUnboundUnbound
1kflBBound:_MNBound:PEPUnbound UnboundUnboundUnboundUnbound
1kflCBound:_MNBound:PEPUnbound UnboundUnboundUnboundUnbound
1kflDBound:_MNBound:PEPUnbound UnboundUnboundUnboundUnbound
1kflEBound:_MNBound:PEPUnbound UnboundUnboundUnboundUnbound
1kflFBound:_MNBound:PEPUnbound UnboundUnboundUnboundUnbound
1kflGBound:_MNBound:PEPUnbound UnboundUnboundUnboundUnbound
1kflHBound:_MNBound:PEPUnbound UnboundUnboundUnboundUnbound
1n8fABound:_MNBound:PEPUnbound UnboundAnalogue:SO4 5353UnboundUnbound
1n8fBBound:_MNBound:PEPUnbound UnboundAnalogue:SO4 2353UnboundUnbound
1n8fCBound:_MNBound:PEPUnbound UnboundAnalogue:SO4 3353UnboundUnbound
1n8fDBound:_MNBound:PEPUnbound UnboundAnalogue:SO4 4353UnboundUnbound
1hfbAUnboundBound:PEPUnbound UnboundUnboundUnboundUnbound
1hfbBUnboundBound:PEPUnbound UnboundUnboundUnboundUnbound
1hfbCUnboundBound:PEPUnbound UnboundUnboundUnboundUnbound
1hfbDUnboundBound:PEPUnbound UnboundUnboundUnboundUnbound
1hfbEUnboundBound:PEPUnbound UnboundUnboundUnboundUnbound
1hfbFUnboundBound:PEPUnbound UnboundUnboundUnboundUnbound
1hfbGUnboundBound:PEPUnbound UnboundUnboundUnboundUnbound
1hfbHUnboundBound:PEPUnbound UnboundUnboundUnboundUnbound
1oabABound:_MNBound:PEPUnbound UnboundUnboundUnboundUnbound
1oabBBound:_MNBound:PEPUnbound UnboundUnboundUnboundUnbound
1of8AAnalogue:_COBound:PEPAnalogue:G3PBound:HOH 2003UnboundUnboundUnboundUnbound
1of8BAnalogue:_COBound:PEPAnalogue:G3PBound:HOH 2003UnboundUnboundUnboundUnbound
1ofaAAnalogue:_COBound:PEPUnbound UnboundUnboundUnboundUnbound
1ofaBAnalogue:_COBound:PEPUnbound UnboundUnboundUnboundUnbound
1ofpAUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1ofpBUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1ofpCUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1ofpDUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1ofqABound:_MNUnboundUnbound UnboundUnboundUnboundUnbound
1ofqBBound:_MNUnboundUnbound UnboundUnboundUnboundUnbound
1ofqCBound:_MNUnboundUnbound UnboundUnboundUnboundUnbound
1ofqDBound:_MNUnboundUnbound UnboundUnboundUnboundUnbound

Active-site residues
resource
literature[8] & [15]
pdbCatalytic residuesCofactor-binding residuesMain-chain involved in catalysiscomment
            
1gg1ALYS   97;GLU  143;LYS  186;ARG  165;ARG  234
CYS   61;HIS  268;GLU  302;ASP  326(Manganese binding)
ALA  164
 
1gg1BLYS   97;GLU  143;LYS  186;ARG  165;ARG  234
CYS   61;HIS  268;GLU  302;ASP  326(Manganese binding)
ALA  164
 
1gg1CLYS   97;GLU  143;LYS  186;ARG  165;ARG  234
CYS   61;HIS  268;GLU  302;ASP  326(Manganese binding)
ALA  164
 
1gg1DLYS   97;GLU  143;LYS  186;ARG  165;ARG  234
CYS   61;HIS  268;GLU  302;ASP  326(Manganese binding)
ALA  164
 
1qr7ALYS   97;GLU  143;LYS  186;ARG  165;ARG  234
CYS   61;HIS  268;GLU  302;ASP  326(Manganese binding)
ALA  164
 
1qr7BLYS   97;GLU  143;LYS  186;ARG  165;ARG  234
CYS   61;HIS  268;GLU  302;ASP  326(Manganese binding)
ALA  164
 
1qr7CLYS   97;GLU  143;LYS  186;ARG  165;ARG  234
CYS   61;HIS  268;GLU  302;ASP  326(Manganese binding)
ALA  164
 
1qr7DLYS   97;GLU  143;LYS  186;ARG  165;ARG  234
CYS   61;HIS  268;GLU  302;ASP  326(Manganese binding)
ALA  164
 
1kflALYS   97;GLU  143;LYS  186;ARG  165;ARG  234
CYS   61;HIS  268;GLU  302;ASP  326(Manganese binding)
ALA  164
 
1kflBLYS   97;GLU  143;LYS  186;ARG  165;ARG  234
CYS   61;HIS  268;GLU  302;ASP  326(Manganese binding)
ALA  164
 
1kflCLYS   97;GLU  143;LYS  186;ARG  165;ARG  234
CYS   61;HIS  268;GLU  302;ASP  326(Manganese binding)
ALA  164
 
1kflDLYS   97;GLU  143;LYS  186;ARG  165;ARG  234
CYS   61;HIS  268;GLU  302;ASP  326(Manganese binding)
ALA  164
 
1kflELYS   97;GLU  143;LYS  186;ARG  165;ARG  234
CYS   61;HIS  268;GLU  302;ASP  326(Manganese binding)
ALA  164
 
1kflFLYS   97;GLU  143;LYS  186;ARG  165;ARG  234
CYS   61;HIS  268;GLU  302;ASP  326(Manganese binding)
ALA  164
 
1kflGLYS   97;GLU  143;LYS  186;ARG  165;ARG  234
CYS   61;HIS  268;GLU  302;ASP  326(Manganese binding)
ALA  164
 
1kflHLYS   97;GLU  143;LYS  186;ARG  165;ARG  234
CYS   61;HIS  268;GLU  302;ASP  326(Manganese binding)
ALA  164
 
1n8fALYS   97;GLU  143;LYS  186;ARG  165;ARG  234
CYS   61;HIS  268;GLU  302;ASP  326(Manganese binding)
ALA  164
 
1n8fBLYS   97;GLU  143;LYS  186;ARG  165;ARG  234
CYS   61;HIS  268;GLU  302;ASP  326(Manganese binding)
ALA  164
 
1n8fCLYS   97;GLU  143;LYS  186;ARG  165;ARG  234
CYS   61;HIS  268;GLU  302;ASP  326(Manganese binding)
ALA  164
 
1n8fDLYS   97;GLU  143;LYS  186;ARG  165;ARG  234
CYS   61;HIS  268;GLU  302;ASP  326(Manganese binding)
ALA  164
 
1hfbALYS  112;GLU  158;LYS  201;ARG  180;ARG  249
CYS   76;HIS  282;GLU  316;ASP  342(Manganese binding)
ALA  179
 
1hfbBLYS  112;GLU  158;LYS  201;ARG  180;ARG  249
CYS   76;HIS  282;GLU  316;ASP  342(Manganese binding)
ALA  179
 
1hfbCLYS  112;GLU  158;LYS  201;ARG  180;ARG  249
CYS   76;HIS  282;GLU  316;ASP  342(Manganese binding)
ALA  179
 
1hfbDLYS  112;GLU  158;LYS  201;ARG  180;ARG  249
CYS   76;HIS  282;GLU  316;ASP  342(Manganese binding)
ALA  179
 
1hfbELYS  112;GLU  158;LYS  201;ARG  180;ARG  249
CYS   76;HIS  282;GLU  316;ASP  342(Manganese binding)
ALA  179
 
1hfbFLYS  112;GLU  158;LYS  201;ARG  180;ARG  249
CYS   76;HIS  282;GLU  316;ASP  342(Manganese binding)
ALA  179
 
1hfbGLYS  112;GLU  158;LYS  201;ARG  180;ARG  249
CYS   76;HIS  282;GLU  316;ASP  342(Manganese binding)
ALA  179
 
1hfbHLYS  112;GLU  158;LYS  201;ARG  180;ARG  249
CYS   76;HIS  282;GLU  316;ASP  342(Manganese binding)
ALA  179
 
1oabALYS  112;GLU  158;LYS  201;ARG  180;ARG  249
CYS   76;HIS  282;GLU  316;ASP  342(Manganese binding)
ALA  179
 
1oabBLYS  112;GLU  158;LYS  201;ARG  180;ARG  249
CYS   76;HIS  282;GLU  316;ASP  342(Manganese binding)
ALA  179
 
1of8ALYS  112;GLU  158;LYS  201;ARG  180;ARG  249
CYS   76;HIS  282;GLU  316;ASP  342(Manganese binding)
ALA  179
 
1of8BLYS  112;GLU  158;LYS  201;ARG  180;ARG  249
CYS   76;HIS  282;GLU  316;ASP  342(Manganese binding)
ALA  179
 
1ofaALYS  112;GLU  158;LYS  201;ARG  180;ARG  249
CYS   76;HIS  282;GLU  316;ASP  342(Manganese binding)
ALA  179
 
1ofaBLYS  112;GLU  158;LYS  201;ARG  180;ARG  249
CYS   76;HIS  282;GLU  316;ASP  342(Manganese binding)
ALA  179
 
1ofpA        ;        ;LYS  201;ARG  180;ARG  249
CYS   76;        ;GLU  316;ASP  342(Manganese binding)
ALA  179
invisible 111-120, 281-288
1ofpBLYS  112;GLU  158;LYS  201;ARG  180;ARG  249
CYS   76;        ;GLU  316;ASP  342(Manganese binding)
ALA  179
invisible 281-288
1ofpC        ;        ;LYS  201;ARG  180;ARG  249
CYS   76;        ;GLU  316;ASP  342(Manganese binding)
ALA  179
invisible 111-120, 281-288
1ofpD        ;        ;LYS  201;ARG  180;ARG  249
CYS   76;        ;GLU  316;ASP  342(Manganese binding)
ALA  179
invisible 111-120, 281-288
1ofqALYS 1112;GLU 1158;LYS 1201;ARG 1180;ARG 1249
CYS 1076;HIS 1282;GLU 1316;ASP 1342(Manganese binding)
ALA 1179
invisible 1114-1116
1ofqB        ;        ;LYS 2201;ARG 2180;ARG 2249
CYS 2076;HIS 2282;GLU 2316;ASP 2342(Manganese binding)
ALA 2179
invisilbe 2112/2117-2118/2158
1ofqCLYS 3112;GLU 3158;LYS 3201;ARG 3180;ARG 3249
CYS 3076;HIS 3282;GLU 3316;ASP 3342(Manganese binding)
ALA 3179
invisible 3115-3116
1ofqD        ;        ;LYS 4201;ARG 4180;ARG 4249
CYS 4076;HIS 4282;GLU 4316;ASP 4342(Manganese binding)
ALA 4179
invisilbe 4112/2158

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[1]Fig.1, p.4615-4616
[4]p.871-872
[5]Fig.1, Fig.5, p.394-3953
[8]

[12]

[13]p.3775
[15]p.687

references
[1]
PubMed ID8643451
JournalProc Natl Acad Sci U S A
Year1996
Volume93
Pages4612-6
AuthorsLi Y, Evans JN
TitleThe hard-soft acid-base principle in enzymatic catalysis: dual reactivity of phosphoenolpyruvate.
[2]
PubMed ID8778789
JournalProteins
Year1996
Volume24
Pages404-6
AuthorsShumilin IA, Kretsinger RH, Bauerle R
TitlePurification, crystallization, and preliminary crystallographic analysis of 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase from Escherichia coli.
[3]
PubMed ID9398312
JournalBiochemistry
Year1997
Volume36
Pages15817-22
AuthorsAkowski JP, Bauerle R
TitleSteady-state kinetics and inhibitor binding of 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase (tryptophan sensitive) from Escherichia coli.
[4]
CommentsX-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
Medline ID99354419
PubMed ID10425687
JournalStructure Fold Des
Year1999
Volume7
Pages865-75
AuthorsShumilin IA, Kretsinger RH, Bauerle RH
TitleCrystal structure of phenylalanine-regulated 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase from Escherichia coli.
Related PDB1qr7
Related UniProtKBP0AB91
[5]
CommentsX-ray crystallography
PubMed ID10926516
JournalJ Mol Biol
Year2000
Volume301
Pages389-99
AuthorsWagner T, Shumilin IA, Bauerle R, Kretsinger RH
TitleStructure of 3-deoxy-d-arabino-heptulosonate-7-phosphate synthase from Escherichia coli: comparison of the Mn(2+)*2-phosphoglycolate and the Pb(2+)*2-phosphoenolpyruvate complexes and implications for catalysis.
Related PDB1gg1
[6]
PubMed ID10987918
JournalJ Org Chem
Year2000
Volume65
Pages5891-7
AuthorsSundaram AK, Woodard RW
TitleProbing the stereochemistry of E. coli 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase (phenylalanine-sensitive)-catalyzed synthesis of KDO 8-P analogues.
[7]
PubMed ID11444986
JournalBiochemistry
Year2001
Volume40
Pages8387-96
AuthorsJordan PA, Bohle DS, Ramilo CA, Evans JN
TitleNew insights into the metal center of 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase.
[8]
PubMed ID11732901
JournalBiochemistry
Year2001
Volume40
Pages14821-8
AuthorsParker EJ, Bulloch EM, Jameson GB, Abell C
TitleSubstrate deactivation of phenylalanine-sensitive 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase by erythrose 4-phosphate.
[9]
PubMed ID11381336
JournalCurr Microbiol
Year2001
Volume42
Pages426-31
AuthorsLin LL, Liao HF, Chien HR, Hsu WH
TitleIdentification of essential cysteine residues in 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase from Corynebacterium glutamicum.
[10]
PubMed ID11476485
JournalNat Prod Rep
Year2001
Volume18
Pages334-55
AuthorsKnaggs AR
TitleThe biosynthesis of shikimate metabolites.
[11]
PubMed ID11429861
JournalOrg Lett
Year2001
Volume3
Pages21-4
AuthorsSundaram AK, Woodard RW
TitleNeisseria gonorrhoeae 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase does not catalyze the formation of the ribo analogue.
[12]
PubMed ID12126632
JournalJ Mol Biol
Year2002
Volume320
Pages1147-56
AuthorsShumilin IA, Zhao C, Bauerle R, Kretsinger RH
TitleAllosteric inhibition of 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase alters the coordination of both substrates.
Related PDB1kfl
[13]
PubMed ID12667068
JournalBiochemistry
Year2003
Volume42
Pages3766-76
AuthorsShumilin IA, Bauerle R, Kretsinger RH
TitleThe high-resolution structure of 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase reveals a twist in the plane of bound phosphoenolpyruvate.
Related PDB1n8f
[14]
PubMed ID12540830
JournalProc Natl Acad Sci U S A
Year2003
Volume100
Pages862-7
AuthorsHartmann M, Schneider TR, Pfeil A, Heinrich G, Lipscomb WN, Braus GH
TitleEvolution of feedback-inhibited beta /alpha barrel isoenzymes by gene duplication and a single mutation.
[15]
PubMed ID15019786
JournalJ Mol Biol
Year2004
Volume337
Pages675-90
AuthorsKonig V, Pfeil A, Braus GH, Schneider TR
TitleSubstrate and metal complexes of 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase from Saccharomyces cerevisiae provide new insights into the catalytic mechanism.
Related PDB1hfb,1ofp,1ofq,1ofa,1of8

comments
Formerly EC 4.1.2.15, transferred to 2.5.1.54.
This enzyme catalyze three successive reactions, two additive reactions and an elimination.
According to the literature [15], two possible mechanisms have been proposed so far. The earlier studies proposed a reaction mechanism, in which the metal-activated water initiates the reaction (see [5], [13] & [15]). However, considering the stereochemistry, it is unlikely. Instead, the literature [15] proposed an alternative mechanism.
According to the alternative mechanism, this enzyme catalyzes the following three reactions successively.
(A) Addition of the double-bonded carbon of PEP to the carbonyl group of another substrate, E4P, leading to the formation of oxocarbenium ion and hydroxyl oxygen from carbonyl oxygen:
(A1) The pi-electrons on the C3=C2 double-bond of PEP make a nucleophilic attack from the si-face onto the re-face of the metal-activated aldehyde group of E4P, to form a covalent bond.
(A2) Lys112 acts as a general acid, which protonates the C1-carbonyl oxygen of E4P, converting the carbonyl oxygen to hydroxyl one.
(B) Addition of water to the oxocarbenium-ion intermediate, created by the condensation of PEP and E4P:
(B1) Glu158 acts as a general base, activating a water molecule positioned on the re-side (opposite to si-face) of PEP. Here, Lys112 act as a second general base, accepting the proton of Glu158, left over by the attacking water.
(B2) The activated water, the hydroxide ion, makes a nucleophilic attack on the oxocarbenium ion (C2 atom of originarily PEP), leading to the a linear intermediate.
(C) Elimination of phosphate oxygen leading to formation of carbonyl group (cf. [2] & S00243):
(C1) Sidechains of Arg180 and Arg249, and mainchain amide of Ala179 stabilize the negative charge on the eliminated phosphate group.
(C2) Lys201 acts as a general acid, which donates a proton to the eliminated phosphate group, leading to the cleavage of the C-O bond.
(C3) Lys201 acts as a general base to deprotonate the hydroxyl group (created by the attacking water), leading to the formation of the carbonyl group.
During these reactions, metal ions, such as manganese, assisted the reactions by interacting with the substrates.

createdupdated
2004-04-042009-02-26


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 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)
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