EzCatDB: D00037
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DB codeD00037
CATH domainDomain 13.40.50.720 : Rossmann foldCatalytic domain
Domain 23.30.9.10 : D-Amino Acid Oxidase; Chain A, domain 2Catalytic domain
E.C.1.4.3.3

CATH domainRelated DB codes (homologues)
3.30.9.10 : D-Amino Acid Oxidase; Chain A, domain 2D00041,D00064,D00494,T00025
3.40.50.720 : Rossmann foldS00543,S00551,S00552,S00553,S00602,S00604,S00605,S00608,S00610,S00625,S00319,S00328,S00329,S00330,S00331,S00332,D00456,D00457,D00458,S00324,S00320,S00325,S00326,S00327,D00459,S00335,S00336,S00334,T00219,S00339,D00513,D00001,D00002,D00003,D00005,D00007,D00008,D00010,D00012,D00017,D00018,D00023,D00027,D00028,D00031,D00032,D00033,D00034,D00035,D00048,D00071,D00476,D00481,D00482,D00490,D00492,D00494,D00545,D00601,D00603,D00604,D00605,D00615,D00845,D00857,D00858,M00161,M00171,M00210,T00002,T00010,T00011,T00015,T00227,T00247,T00408,T00414,D00827,D00262,D00274,D00275,M00035,T00109

Enzyme Name
UniProtKBKEGG

P00371
Protein nameD-amino-acid oxidaseD-amino-acid oxidase
ophio-amino-acid oxidase
L-amino acid:O2 oxidoreductase
new yellow enzyme
SynonymsDAMOX
DAAO
DAO
EC 1.4.3.3
RefSeqNP_999231.1 (Protein)
NM_214066.2 (DNA/RNA sequence)
PfamPF01266 (DAO)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00260Glycine, serine and threonine metabolism
MAP00311Penicillin and cephalosporin biosynthesis
MAP00330Arginine and proline metabolism
MAP00472D-Arginine and D-ornithine metabolism

UniProtKB:Accession NumberP00371
Entry nameOXDA_PIG
ActivityA D-amino acid + H(2)O + O(2) = a 2-oxo acid + NH(3) + H(2)O(2).
SubunitHomodimer.
Subcellular locationPeroxisome.
CofactorFAD.

Compound table: links to PDB-related databases & PoSSuM

CofactorsSubstratesProductsintermediates
KEGG-idC00016C00405C00001C00007C00161C00014C00027
CompoundFADD-Amino acidH2OO22-Oxo acidNH3H2O2Imino acid
Typeamide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carbohydrate,nucleotideamino acidsH2Ootherscarbohydrate,carboxyl groupamine group,organic ionothers
ChEBI16238

15377
27140
26689
15379

16134
16240

PubChem643975

962
22247451
977

222
784
22326046

                
1aa8A01Bound:FADUnbound UnboundUnboundUnboundUnboundUnbound
1aa8B01Bound:FADUnbound UnboundUnboundUnboundUnboundUnbound
1an9A01Bound:FADUnbound UnboundUnboundUnboundUnboundUnbound
1an9B01Bound:FADUnbound UnboundUnboundUnboundUnboundUnbound
1daoA01Analogue:FABUnbound UnboundUnboundUnboundUnboundUnbound
1daoB01Analogue:FABUnbound UnboundUnboundUnboundUnboundUnbound
1daoC01Analogue:FABUnbound UnboundUnboundUnboundUnboundUnbound
1daoD01Analogue:FABUnbound UnboundUnboundUnboundUnboundUnbound
1daoE01Analogue:FABUnbound UnboundUnboundUnboundUnboundUnbound
1daoF01Analogue:FABUnbound UnboundUnboundUnboundUnboundUnbound
1daoG01Analogue:FABUnbound UnboundUnboundUnboundUnboundUnbound
1daoH01Analogue:FABUnbound UnboundUnboundUnboundUnboundUnbound
1ddoA01Bound:FADUnbound UnboundUnboundUnboundUnboundUnbound
1ddoB01Bound:FADUnbound UnboundUnboundUnboundUnboundUnbound
1ddoC01Bound:FADUnbound UnboundUnboundUnboundUnboundUnbound
1ddoD01Bound:FADUnbound UnboundUnboundUnboundUnboundUnbound
1ddoE01Bound:FADUnbound UnboundUnboundUnboundUnboundUnbound
1ddoF01Bound:FADUnbound UnboundUnboundUnboundUnboundUnbound
1ddoG01Bound:FADUnbound UnboundUnboundUnboundUnboundUnbound
1ddoH01Bound:FADUnbound UnboundUnboundUnboundUnboundUnbound
1eviA01Bound:FADUnbound UnboundUnboundUnboundUnboundUnbound
1eviB01Bound:FADUnbound UnboundUnboundUnboundUnboundUnbound
1kifA01Bound:FADUnbound UnboundUnboundUnboundUnboundUnbound
1kifB01Bound:FADUnbound UnboundUnboundUnboundUnboundUnbound
1kifC01Bound:FADUnbound UnboundUnboundUnboundUnboundUnbound
1kifD01Bound:FADUnbound UnboundUnboundUnboundUnboundUnbound
1kifE01Bound:FADUnbound UnboundUnboundUnboundUnboundUnbound
1kifF01Bound:FADUnbound UnboundUnboundUnboundUnboundUnbound
1kifG01Bound:FADUnbound UnboundUnboundUnboundUnboundUnbound
1kifH01Bound:FADUnbound UnboundUnboundUnboundUnboundUnbound
1ve9A01Bound:FADUnbound UnboundUnboundUnboundUnboundUnbound
1ve9B01Bound:FADUnbound UnboundUnboundUnboundUnboundUnbound
1aa8A02UnboundUnbound UnboundUnboundUnboundUnboundIntermediate-analogue:BEZ
1aa8B02UnboundUnbound UnboundUnboundUnboundUnboundIntermediate-analogue:BEZ
1an9A02UnboundUnbound UnboundUnboundUnboundUnboundIntermediate-analogue:BE2
1an9B02UnboundUnbound UnboundUnboundUnboundUnboundIntermediate-analogue:BE2
1daoA02UnboundUnbound UnboundUnboundUnboundUnboundUnbound
1daoB02UnboundUnbound UnboundUnboundUnboundUnboundUnbound
1daoC02UnboundUnbound UnboundUnboundUnboundUnboundUnbound
1daoD02UnboundUnbound UnboundUnboundUnboundUnboundUnbound
1daoE02UnboundUnbound UnboundUnboundUnboundUnboundUnbound
1daoF02UnboundUnbound UnboundUnboundUnboundUnboundUnbound
1daoG02UnboundUnbound UnboundUnboundUnboundUnboundUnbound
1daoH02UnboundUnbound UnboundUnboundUnboundUnboundUnbound
1ddoA02UnboundUnbound UnboundUnboundUnboundUnboundIntermediate-bound:ITR
1ddoB02UnboundUnbound UnboundUnboundUnboundUnboundIntermediate-bound:ITR
1ddoC02UnboundUnbound UnboundUnboundUnboundUnboundIntermediate-bound:ITR
1ddoD02UnboundUnbound UnboundUnboundUnboundUnboundIntermediate-bound:ITR
1ddoE02UnboundUnbound UnboundUnboundUnboundUnboundIntermediate-bound:ITR
1ddoF02UnboundUnbound UnboundUnboundUnboundUnboundIntermediate-bound:ITR
1ddoG02UnboundUnbound UnboundUnboundUnboundUnboundIntermediate-bound:ITR
1ddoH02UnboundUnbound UnboundUnboundUnboundUnboundIntermediate-bound:ITR
1eviA02UnboundUnbound UnboundUnboundUnboundUnboundIntermediate-analogue:2PC
1eviB02UnboundUnbound UnboundUnboundUnboundUnboundIntermediate-analogue:2PC
1kifA02UnboundUnbound UnboundUnboundUnboundUnboundIntermediate-analogue:BEZ
1kifB02UnboundUnbound UnboundUnboundUnboundUnboundIntermediate-analogue:BEZ
1kifC02UnboundUnbound UnboundUnboundUnboundUnboundIntermediate-analogue:BEZ
1kifD02UnboundUnbound UnboundUnboundUnboundUnboundIntermediate-analogue:BEZ
1kifE02UnboundUnbound UnboundUnboundUnboundUnboundIntermediate-analogue:BEZ
1kifF02UnboundUnbound UnboundUnboundUnboundUnboundIntermediate-analogue:BEZ
1kifG02UnboundUnbound UnboundUnboundUnboundUnboundIntermediate-analogue:BEZ
1kifH02UnboundUnbound UnboundUnboundUnboundUnboundIntermediate-analogue:BEZ
1ve9A02UnboundUnbound UnboundUnboundUnboundUnboundIntermediate-analogue:BEZ
1ve9B02UnboundUnbound UnboundUnboundUnboundUnboundIntermediate-analogue:BEZ

Active-site residues
resource
Swiss-prot;P00371 & literature [15]
pdbCatalytic residuesMain-chain involved in catalysis
          
1aa8A01        
GLN   53;GLY  313
1aa8B01        
GLN   53;GLY  313
1an9A01        
GLN   53;GLY  313
1an9B01        
GLN   53;GLY  313
1daoA01        
GLN   53;GLY  313
1daoB01        
GLN   53;GLY  313
1daoC01        
GLN   53;GLY  313
1daoD01        
GLN   53;GLY  313
1daoE01        
GLN   53;GLY  313
1daoF01        
GLN   53;GLY  313
1daoG01        
GLN   53;GLY  313
1daoH01        
GLN   53;GLY  313
1ddoA01        
GLN   53;GLY  313
1ddoB01        
GLN   53;GLY  313
1ddoC01        
GLN   53;GLY  313
1ddoD01        
GLN   53;GLY  313
1ddoE01        
GLN   53;GLY  313
1ddoF01        
GLN   53;GLY  313
1ddoG01        
GLN   53;GLY  313
1ddoH01        
GLN   53;GLY  313
1eviA01        
GLN   53;GLY  313
1eviB01        
GLN   53;GLY  313
1kifA01        
GLN   53;GLY  313
1kifB01        
GLN   53;GLY  313
1kifC01        
GLN   53;GLY  313
1kifD01        
GLN   53;GLY  313
1kifE01        
GLN   53;GLY  313
1kifF01        
GLN   53;GLY  313
1kifG01        
GLN   53;GLY  313
1kifH01        
GLN   53;GLY  313
1ve9A01        
GLN   53;GLY  313
1ve9B01        
GLN   53;GLY  313
1aa8A02TYR  224
 
1aa8B02TYR  224
 
1an9A02TYR  224
 
1an9B02TYR  224
 
1daoA02TYR  224
 
1daoB02TYR  224
 
1daoC02TYR  224
 
1daoD02TYR  224
 
1daoE02TYR  224
 
1daoF02TYR  224
 
1daoG02TYR  224
 
1daoH02TYR  224
 
1ddoA02TYR  224
 
1ddoB02TYR  224
 
1ddoC02TYR  224
 
1ddoD02TYR  224
 
1ddoE02TYR  224
 
1ddoF02TYR  224
 
1ddoG02TYR  224
 
1ddoH02TYR  224
 
1eviA02TYR  224
 
1eviB02TYR  224
 
1kifA02TYR  224
 
1kifB02TYR  224
 
1kifC02TYR  224
 
1kifD02TYR  224
 
1kifE02TYR  224
 
1kifF02TYR  224
 
1kifG02TYR  224
 
1kifH02TYR  224
 
1ve9A02TYR  224
 
1ve9B02TYR  224
 

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[9]Scheme 1, Scheme 2, Scheme 3
[11]Fig.7, p.618-619
[13]p.15
[15]Fig.5, p.7498-7499
[16]p.5858-5859
[18]Fig.1, p.804-806
[19]Fig.6, Fig.7, p.829-832
[22]Scheme 2, p.1741-1744
[23]

[24]Scheme 2
[26]Fig.6, p.12466-12468
[28]Fig.1, p.14120-14121
[29]p.540-541, p.542-544
[30]Scheme 1, Scheme 3, p.29-31

references
[1]
PubMed ID20559
JournalMed J Osaka Univ
Year1976
Volume27
Pages33-46
AuthorsHoriike K, Shiga K, Nishina Y, Yamano T
TitlepH dependence of catalysis of the monomer of hog kidney D-amino acid oxidase.
[2]
CommentsPRELIMINARY STUDIES ON ACTIVE SITE
Medline ID82120157
PubMed ID6120171
JournalJ Biol Chem
Year1982
Volume257
Pages1937-44
AuthorsSwenson RP, Williams CH Jr, Massey V
TitleChemical modification of D-amino acid oxidase. Amino acid sequence of the tryptic peptides containing tyrosine and lysine residues modified by fluorodinitrobenzene.
Related UniProtKBP00371
[3]
CommentsPRELIMINARY STUDIES ON ACTIVE SITE
Medline ID83082913
PubMed ID6129252
JournalJ Biol Chem
Year1983
Volume258
Pages497-502
AuthorsSwenson RP, Williams CH Jr, Massey V
TitleIdentification of the histidine residue in D-amino acid oxidase that is covalently modified during inactivation by 5-dimethylaminonaphthalene-1-sulfonyl chloride.
Related UniProtKBP00371
[4]
CommentsMUTAGENESIS OF Y-55/M-110/H-217 TO SHOW THEY ARE NOT IN ACTIVE SITE
Medline ID8900569
PubMed ID2901989
JournalFEBS Lett
Year1988
Volume238
Pages269-72
AuthorsWatanabe F, Fukui K, Momoi K, Miyake Y
TitleEffect of site-specific mutagenesis of tyrosine-55, methionine-110 and histidine-217 in porcine kidney D-amino acid oxidase on its catalytic function.
Related UniProtKBP00371
[5]
PubMed ID2907883
JournalInt J Biochem
Year1988
Volume20
Pages1235-8
AuthorsNagata Y, Shimojo T, Akino T
TitleTwo spectrophotometric assays for D-amino acid oxidase: for the study of distribution patterns.
[6]
PubMed ID2570065
JournalJ Biochem (Tokyo)
Year1989
Volume105
Pages1024-9
AuthorsWatanabe F, Fukui K, Momoi K, Miyake Y
TitleSite-specific mutagenesis of lysine-204, tyrosine-224, tyrosine-228, and histidine-307 of porcine kidney D-amino acid oxidase and the implications as to its catalytic function.
[7]
CommentsACTIVE SITES TYR-228 AND HIS-307
Medline ID91201275
PubMed ID1673125
JournalJ Biochem (Tokyo)
Year1991
Volume109
Pages171-7
AuthorsMiyano M, Fukui K, Watanabe F, Takahashi S, Tada M, Kanashiro M, Miyake Y
TitleStudies on Phe-228 and Leu-307 recombinant mutants of porcine kidney D-amino acid oxidase: expression, purification, and characterization.
Related UniProtKBP00371
[8]
PubMed ID1351830
JournalComp Biochem Physiol B
Year1992
Volume101
Pages509-11
AuthorsBrachet P, Puigserver A
TitleRegional differences for the D-amino acid oxidase-catalysed oxidation of D-methionine in chicken small intestine.
[9]
PubMed ID7908225
JournalBiochemistry
Year1994
Volume33
Pages4001-7
AuthorsDenu JM, Fitzpatrick PF
TitleIntrinsic primary, secondary, and solvent kinetic isotope effects on the reductive half-reaction of D-amino acid oxidase: evidence against a concerted mechanism.
[10]
PubMed ID7989339
JournalJ Biol Chem
Year1994
Volume269
Pages31666-73
AuthorsPollegioni L, Fukui K, Massey V
TitleStudies on the kinetic mechanism of pig kidney D-amino acid oxidase by site-directed mutagenesis of tyrosine 224 and tyrosine 228.
[11]
PubMed ID8690726
JournalJ Biochem (Tokyo)
Year1995
Volume118
Pages614-20
AuthorsNishina Y, Sato K, Miura R, Shiga K
TitleStructures of charge-transfer complexes of flavoenzyme D-amino acid oxidase: a study by resonance Raman spectroscopy and extended Huckel molecular orbital method.
[12]
PubMed ID8681967
JournalEur J Biochem
Year1996
Volume238
Pages519-28
AuthorsStocker A, Hecht HJ, Buckmann AF
TitleSynthesis, characterization and preliminary crystallographic data of N6-(6-carbamoylhexyl)-FAD-D-amino-acid oxidase from pig kidney, a semi-synthetic oxidase.
[13]
CommentsX-RAY CRYSTALLOGRAPHY
Medline ID97018220
PubMed ID8864836
JournalJ Biochem (Tokyo)
Year1996
Volume120
Pages14-7
AuthorsMizutani H, Miyahara I, Hirotsu K, Nishina Y, Shiga K, Setoyama C, Miura R
TitleThree-dimensional structure of porcine kidney D-amino acid oxidase at 3.0 A resolution.
Related PDB1aa8,1ve9
Related UniProtKBP00371
[14]
PubMed ID8827446
JournalJ Biochem (Tokyo)
Year1996
Volume119
Pages1114-7
AuthorsSetoyama C, Miura R, Nishina Y, Shiga K, Mizutani H, Miyahara I, Hirotsu K
TitleCrystallization of expressed porcine kidney D-amino acid oxidase and preliminary X-ray crystallographic characterization.
[15]
CommentsX-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS)
Medline ID96353844
PubMed ID8755502
JournalProc Natl Acad Sci U S A
Year1996
Volume93
Pages7496-501
AuthorsMattevi A, Vanoni MA, Todone F, Rizzi M, Teplyakov A, Coda A, Bolognesi M, Curti B
TitleCrystal structure of D-amino acid oxidase: a case of active site mirror-image convergent evolution with flavocytochrome b2.
Related PDB1kif
Related UniProtKBP00371
[16]
CommentsX-RAY CRYSTALLOGRAPHY
Medline ID97297794
PubMed ID9153426
JournalBiochemistry
Year1997
Volume36
Pages5853-60
AuthorsTodone F, Vanoni MA, Mozzarelli A, Bolognesi M, Coda A, Curti B, Mattevi A
TitleActive site plasticity in D-amino acid oxidase: a crystallographic analysis.
Related PDB1ddo,1dao
Related UniProtKBP00371
[17]
PubMed ID9153402
JournalBiochemistry
Year1997
Volume36
Pages5624-32
AuthorsVanoni MA, Cosma A, Mazzeo D, Mattevi A, Todone F, Curti B
TitleLimited proteolysis and X-ray crystallography reveal the origin of substrate specificity and of the rate-limiting product release during oxidation of D-amino acids catalyzed by mammalian D-amino acid oxidase.
[18]
PubMed ID9434899
JournalCurr Opin Struct Biol
Year1997
Volume7
Pages804-10
AuthorsMattevi A, Vanoni MA, Curti B
TitleStructure of D-amino acid oxidase: new insights from an old enzyme.
[19]
CommentsX-ray crystallography
PubMed ID9399588
JournalJ Biochem (Tokyo)
Year1997
Volume122
Pages825-33
AuthorsMiura R, Setoyama C, Nishina Y, Shiga K, Mizutani H, Miyahara I, Hirotsu K
TitleStructural and mechanistic studies on D-amino acid oxidase x substrate complex: implications of the crystal structure of enzyme x substrate analog complex.
Related PDB1an9
[20]
PubMed ID9268372
JournalJ Biol Chem
Year1997
Volume272
Pages22248-52
AuthorsRaibekas AA, Massey V
TitleGlycerol-assisted restorative adjustment of flavoenzyme conformation perturbed by site-directed mutagenesis.
[21]
PubMed ID10427728
JournalFEMS Microbiol Lett
Year1999
Volume176
Pages443-8
AuthorsLin LL, Wang WC, Ju SS, Chien HR, Hsu WH
TitleThe role of a conserved histidine residue, His324, in Trigonopsis variabilis D-amino acid oxidase.
[22]
PubMed ID11130179
JournalCell Mol Life Sci
Year2000
Volume57
Pages1732-47
AuthorsPilone MS
TitleD-Amino acid oxidase: new findings.
[23]
CommentsX-ray crystallography
PubMed ID10876160
JournalJ Biochem (Tokyo)
Year2000
Volume128
Pages73-81
AuthorsMizutani H, Miyahara I, Hirotsu K, Nishina Y, Shiga K, Setoyama C, Miura R
TitleThree-dimensional structure of the purple intermediate of porcine kidney D-amino acid oxidase. Optimization of the oxidative half-reaction through alignment of the product with reduced flavin.
Related PDB1evi
[24]
PubMed ID10920257
JournalJ Biochem (Tokyo)
Year2000
Volume128
Pages213-23
AuthorsNishina Y, Sato K, Miura R, Shiga K
TitleSubstrate recognition and activation mechanism of D-amino acid oxidase: a study using substrate analogs.
[25]
PubMed ID10716694
JournalProc Natl Acad Sci U S A
Year2000
Volume97
Pages3089-93
AuthorsRaibekas AA, Fukui K, Massey V
TitleDesign and properties of human D-amino acid oxidase with covalently attached flavin.
[26]
PubMed ID11070076
JournalProc Natl Acad Sci U S A
Year2000
Volume97
Pages12463-8
AuthorsUmhau S, Pollegioni L, Molla G, Diederichs K, Welte W, Pilone MS, Ghisla S
TitleThe x-ray structure of D-amino acid oxidase at very high resolution identifies the chemical mechanism of flavin-dependent substrate dehydrogenation.
Related PDB1c0k,1c0l,1c0p
[27]
PubMed ID11686926
JournalJ Biochem (Tokyo)
Year2001
Volume130
Pages637-47
AuthorsNishina Y, Sato K, Shi R, Setoyama C, Miura R, Shiga K
TitleOn the ligands in charge-transfer complexes of porcine kidney flavoenzyme D-amino acid oxidase in three redox states: a resonance Raman study.
[28]
PubMed ID12450374
JournalBiochemistry
Year2002
Volume41
Pages14111-21
AuthorsTilocca A, Gamba A, Vanoni MA, Fois E
TitleFirst-principles molecular dynamics investigation of the D-amino acid oxidative half-reaction catalyzed by the flavoenzyme D-amino acid oxidase.
[29]
PubMed ID12445787
JournalJ Mol Biol
Year2002
Volume324
Pages535-46
AuthorsPollegioni L, Diederichs K, Molla G, Umhau S, Welte W, Ghisla S, Pilone MS
TitleYeast D-amino acid oxidase: structural basis of its catalytic properties.
Related PDB1c0i
[30]
PubMed ID15450847
JournalBiochim Biophys Acta
Year2004
Volume1702
Pages19-32
AuthorsBoselli A, Piubelli L, Molla G, Sacchi S, Pilone MS, Ghisla S, Pollegioni L
TitleOn the mechanism of Rhodotorula gracilis D-amino acid oxidase: role of the active site serine 335.

comments
Although the first domain of this enzyme is classified in CATH 3.40.50.720, it should be homologous to sarcosine oxidase (E.C. 1.5.3.1; D00041 in EzCatDB), and is re-classified into CATH 3.50.50.60 in this database.
Although this enzyme is homologous to yeast counterpart (D00494 in EzCatDB), a set of catalytic residues is slightly different from the counterpart. The sidechain of Tyr224 plays a catalytic role as the counterpart of corresponding Ser335 in the yeast enzyme (see D00494) (see [15] & [26]).
According to the literature [22], this enzyme catalyzes the following reactions:
(A) Hydride transfer from D-amino acid to FAD, giving imino acid and FADH2 (reductive half-reaction).
(B) Hydride transfer from FADH2 to O2, giving FAD and H2O2 (oxidative half-reaction).
(C) Exchange of double-bonded atoms of the imino acid (Schiff-base deformation by water)

createdupdated
2005-01-252009-02-26


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)
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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