EzCatDB: D00482
Related links:    PDB-formatted query search system Fasta-formatted query search system Fasta-formatted query search system

DB codeD00482
CATH domainDomain 13.90.180.10 : Quinone Oxidoreductase; Chain A, domain 1Catalytic domain
Domain 23.40.50.720 : Rossmann fold
E.C.1.1.1.1

CATH domainRelated DB codes (homologues)
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,D00037,D00048,D00071,D00476,D00481,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
3.90.180.10 : Quinone Oxidoreductase; Chain A, domain 1D00001,D00002,D00018,D00048,D00481,D00490,D00492,D00615

Enzyme Name
UniProtKBKEGG

P07327P00325P40394
Protein nameAlcohol dehydrogenase 1AAlcohol dehydrogenase 1BAlcohol dehydrogenase class 4 mu/sigma chainalcohol dehydrogenase
aldehyde reductase
ADH
alcohol dehydrogenase (NAD)
aliphatic alcohol dehydrogenase
ethanol dehydrogenase
NAD-dependent alcohol dehydrogenase
NAD-specific aromatic alcohol dehydrogenase
NADH-alcohol dehydrogenase
NADH-aldehyde dehydrogenase
primary alcohol dehydrogenase
yeast alcohol dehydrogenase
SynonymsEC 1.1.1.1
Alcohol dehydrogenase subunit alpha
EC 1.1.1.1
Alcohol dehydrogenase subunit beta
EC 1.1.1.1
Alcohol dehydrogenase class IV mu/sigma chain
Retinol dehydrogenase
Gastric alcohol dehydrogenase
RefSeqNP_000658.1 (Protein)
NM_000667.3 (DNA/RNA sequence)
NP_000659.2 (Protein)
NM_000668.4 (DNA/RNA sequence)
NP_000664.2 (Protein)
NM_000673.4 (DNA/RNA sequence)
NP_001159976.1 (Protein)
NM_001166504.1 (DNA/RNA sequence)
PfamPF08240 (ADH_N)
PF00107 (ADH_zinc_N)
[Graphical view]
PF08240 (ADH_N)
PF00107 (ADH_zinc_N)
[Graphical view]
PF08240 (ADH_N)
PF00107 (ADH_zinc_N)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00010Glycolysis / Gluconeogenesis
MAP00071Fatty acid metabolism
MAP00120Bile acid biosynthesis
MAP00260Glycine, serine and threonine metabolism
MAP00350Tyrosine metabolism
MAP006241- and 2-Methylnaphthalene degradation
MAP006413-Chloroacrylic acid degradation
MAP00830Retinol metabolism
MAP00980Metabolism of xenobiotics by cytochrome P450
MAP00982Drug metabolism - cytochrome P450

UniProtKB:Accession NumberP07327P00325P40394
Entry nameADH1A_HUMANADH1B_HUMANADH7_HUMAN
ActivityAn alcohol + NAD(+) = an aldehyde or ketone + NADH.An alcohol + NAD(+) = an aldehyde or ketone + NADH.An alcohol + NAD(+) = an aldehyde or ketone + NADH.
SubunitDimer of identical or non-identical chains of three types, alpha, beta and gamma.Dimer of identical or non-identical chains of three types, alpha, beta and gamma.Homodimer.
Subcellular locationCytoplasm.Cytoplasm.Cytoplasm.
CofactorBinds 2 zinc ions per subunit.Binds 2 zinc ions per subunit.Binds 2 zinc ions per subunit.

Compound table: links to PDB-related databases & PoSSuM

CofactorsSubstratesProducts
KEGG-idC00038C00003C00069C00004C00071C00709C00080
CompoundZincNAD+AlcoholNADHAldehydeKetoneH+
Typeheavy metalamide group,amine group,nucleotidecarbohydrateamide group,amine group,nucleotidecarbohydratecarbohydrateothers
ChEBI29105
15846

16908


15378
PubChem32051
5893

439153


1038
               
1hsoA01Bound:2x_ZNUnboundUnboundUnboundUnboundUnbound 
1hsoB01Bound:2x_ZNUnboundUnboundUnboundUnboundUnbound 
1u3tA01Bound:2x_ZNUnboundUnboundUnboundBound:CCBUnbound 
1u3tB01Bound:2x_ZNUnboundUnboundUnboundBound:CCBUnbound 
1dehA01Bound:2x_ZNUnboundUnboundUnboundUnboundUnbound 
1dehB01Bound:2x_ZNUnboundUnboundUnboundUnboundUnbound 
1hdxA01Bound:2x_ZNUnboundUnboundUnboundUnboundUnbound 
1hdxB01Bound:2x_ZNUnboundUnboundUnboundUnboundUnbound 
1hdyA01Bound:2x_ZNUnboundUnboundUnboundUnboundUnbound 
1hdyB01Bound:2x_ZNUnboundUnboundUnboundUnboundUnbound 
1hdzA01Bound:2x_ZNUnboundUnboundUnboundUnboundUnbound 
1hdzB01Bound:2x_ZNUnboundUnboundUnboundUnboundUnbound 
1hszA01Bound:2x_ZNUnboundUnboundUnboundUnboundUnbound 
1hszB01Bound:2x_ZNUnboundUnboundUnboundUnboundUnbound 
1htbA01Bound:2x_ZNUnboundUnboundUnboundUnboundUnbound 
1htbB01Bound:2x_ZNUnboundUnboundUnboundUnboundUnbound 
3hudA01Bound:2x_ZNUnboundUnboundUnboundUnboundUnbound 
3hudB01Bound:2x_ZNUnboundUnboundUnboundUnboundUnbound 
1agnA01Bound:_ZN 376UnboundUnboundUnboundUnboundAnalogue:ACT 378 
1agnB01Bound:_ZN 376UnboundUnboundUnboundUnboundAnalogue:ACT 378 
1agnC01Bound:_ZN 376UnboundUnboundUnboundUnboundAnalogue:ACT 378 
1agnD01Bound:_ZN 376UnboundUnboundUnboundUnboundAnalogue:ACT 378 
1d1sA01Bound:_ZN 376UnboundUnboundUnboundUnboundAnalogue:ACT 501 
1d1sB01Bound:_ZN 376UnboundUnboundUnboundUnboundAnalogue:ACT 506 
1d1sC01Bound:_ZN 376UnboundUnboundUnboundUnboundAnalogue:ACT 505 
1d1sD01Bound:_ZN 376UnboundUnboundUnboundUnboundAnalogue:ACT 511 
1d1tA01Bound:_ZN 376UnboundUnboundUnboundUnboundAnalogue:ACT 501 
1d1tB01Bound:_ZN 376UnboundUnboundUnboundUnboundAnalogue:ACT 506 
1d1tC01Bound:_ZN 376UnboundUnboundUnboundUnboundAnalogue:ACT 505 
1d1tD01Bound:_ZN 376UnboundUnboundUnboundUnboundAnalogue:ACT 511 
1hsoA02UnboundBound:NADUnboundUnboundUnboundUnbound 
1hsoB02UnboundBound:NADUnboundUnboundUnboundUnbound 
1u3tA02UnboundBound:NADUnboundUnboundUnboundUnbound 
1u3tB02UnboundBound:NADUnboundUnboundUnboundUnbound 
1dehA02UnboundAnalogue:NAD-PYZUnboundUnboundUnboundUnbound 
1dehB02UnboundAnalogue:NAD-PYZUnboundUnboundUnboundUnbound 
1hdxA02UnboundBound:NADUnboundUnboundUnboundUnbound 
1hdxB02UnboundBound:NADUnboundUnboundUnboundUnbound 
1hdyA02UnboundAnalogue:NAD-PYZUnboundUnboundUnboundUnbound 
1hdyB02UnboundAnalogue:NAD-PYZUnboundUnboundUnboundUnbound 
1hdzA02UnboundBound:NADUnboundUnboundUnboundUnbound 
1hdzB02UnboundBound:NADUnboundUnboundUnboundUnbound 
1hszA02UnboundBound:NADUnboundUnboundUnboundUnbound 
1hszB02UnboundBound:NADUnboundUnboundUnboundUnbound 
1htbA02UnboundAnalogue:NAD-PYZUnboundUnboundUnboundUnbound 
1htbB02UnboundAnalogue:NAD-PYZUnboundUnboundUnboundUnbound 
3hudA02UnboundBound:NADUnboundUnboundUnboundUnbound 
3hudB02UnboundBound:NADUnboundUnboundUnboundUnbound 
1agnA02UnboundBound:NADUnboundUnboundUnboundUnbound 
1agnB02UnboundBound:NADUnboundUnboundUnboundUnbound 
1agnC02UnboundBound:NADUnboundUnboundUnboundUnbound 
1agnD02UnboundBound:NADUnboundUnboundUnboundUnbound 
1d1sA02UnboundBound:NADUnboundUnboundUnboundUnbound 
1d1sB02UnboundBound:NADUnboundUnboundUnboundUnbound 
1d1sC02UnboundBound:NADUnboundUnboundUnboundUnbound 
1d1sD02UnboundBound:NADUnboundUnboundUnboundUnbound 
1d1tA02UnboundBound:NADUnboundUnboundUnboundUnbound 
1d1tB02UnboundBound:NADUnboundUnboundUnboundUnbound 
1d1tC02UnboundBound:NADUnboundUnboundUnboundUnbound 
1d1tD02UnboundBound:NADUnboundUnboundUnboundUnbound 

Active-site residues
resource
Swiss-prot;P40394, P00325, P00327, P00326, P00328,P26325
pdbCatalytic residuesCofactor-binding residuescomment
           
1hsoA01THR 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
 
1hsoB01THR 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
 
1u3tA01THR 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
 
1u3tB01THR 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
 
1dehA01THR 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
 
1dehB01THR 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
 
1hdxA01THR 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
 
1hdxB01THR 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
 
1hdyA01THR 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
 
1hdyB01THR 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
 
1hdzA01THR 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
mutant R47G
1hdzB01THR 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
mutant R47G
1hszA01THR 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
 
1hszB01THR 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
 
1htbA01THR 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
 
1htbB01THR 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
 
3hudA01THR 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
 
3hudB01THR 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
 
1agnA01THR 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
 
1agnB01THR 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
 
1agnC01THR 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
 
1agnD01THR 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
 
1d1sA01THR 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
 
1d1sB01THR 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
 
1d1sC01THR 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
 
1d1sD01THR 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
 
1d1tA01THR 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
mutant M141L
1d1tB01THR 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
mutant M141L
1d1tC01THR 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
mutant M141L
1d1tD01THR 48;HIS 51
CYS 46;HIS 67;CYS 174(Catalytic zinc binding)
mutant M141L
1hsoA02 
 
 
1hsoB02 
 
 
1u3tA02 
 
 
1u3tB02 
 
 
1dehA02 
 
 
1dehB02 
 
 
1hdxA02 
 
 
1hdxB02 
 
 
1hdyA02 
 
 
1hdyB02 
 
 
1hdzA02 
 
 
1hdzB02 
 
 
1hszA02 
 
 
1hszB02 
 
 
1htbA02 
 
 
1htbB02 
 
 
3hudA02 
 
 
3hudB02 
 
 
1agnA02 
 
 
1agnB02 
 
 
1agnC02 
 
 
1agnD02 
 
 
1d1sA02 
 
 
1d1sB02 
 
 
1d1sC02 
 
 
1d1sD02 
 
 
1d1tA02 
 
 
1d1tB02 
 
 
1d1tC02 
 
 
1d1tD02 
 
 

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[2]Fig.4, p.1065-1067

references
[1]
PubMed ID1772423
JournalBiochem Int
Year1991
Volume24
Pages451-60
AuthorsFong WP, Keung WM
TitleExamination of subunit interaction in human ADH: carboxymethylation of the heterodimer beta 2 gamma 1.
[2]
PubMed ID1989677
JournalBiochemistry
Year1991
Volume30
Pages1062-8
AuthorsEhrig T, Hurley TD, Edenberg HJ, Bosron WF
TitleGeneral base catalysis in a glutamine for histidine mutant at position 51 of human liver alcohol dehydrogenase.
[3]
CommentsX-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
Medline ID91376103
PubMed ID1896463
JournalProc Natl Acad Sci U S A
Year1991
Volume88
Pages8149-53
AuthorsHurley TD, Bosron WF, Hamilton JA, Amzel LM
TitleStructure of human beta 1 beta 1 alcohol dehydrogenase: catalytic effects of non-active-site substitutions.
Related PDB3hud
Related UniProtKBP00325
[4]
PubMed ID1572355
JournalEur J Biochem
Year1992
Volume205
Pages519-26
AuthorsHoog JO, Eklund H, Jornvall H
TitleA single-residue exchange gives human recombinant beta beta alcohol dehydrogenase gamma gamma isozyme properties.
[5]
PubMed ID8493917
JournalAdv Exp Med Biol
Year1993
Volume328
Pages391-400
AuthorsPlapp BV, Green DW, Sun HW, Park DH, Kim K
TitleSubstrate specificity of alcohol dehydrogenases.
[6]
PubMed ID8127901
JournalProc Natl Acad Sci U S A
Year1994
Volume91
Pages1893-7
AuthorsPares X, Cederlund E, Moreno A, Hjelmqvist L, Farres J, Jornvall H
TitleMammalian class IV alcohol dehydrogenase (stomach alcohol dehydrogenase): structure, origin, and correlation with enzymology.
[7]
PubMed ID7957193
JournalEur J Biochem
Year1994
Volume225
Pages1015-9
AuthorsJelokova J, Karlsson C, Estonius M, Jornvall H, Hoog JO
TitleFeatures of structural zinc in mammalian alcohol dehydrogenase. Site-directed mutagenesis of the zinc ligands.
[8]
CommentsX-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS).
Medline ID94260547
PubMed ID8201622
JournalJ Mol Biol
Year1994
Volume239
Pages415-29
AuthorsHurley TD, Bosron WF, Stone CL, Amzel LM
TitleStructures of three human beta alcohol dehydrogenase variants. Correlations with their functional differences.
Related PDB1hdx,1hdy,1hdz
Related UniProtKBP00325
[9]
PubMed ID7484389
JournalAdv Exp Med Biol
Year1995
Volume372
Pages281-94
AuthorsJornvall H, Danielsson O, Hjelmqvist L, Persson B, Shafqat J
TitleThe alcohol dehydrogenase system.
[10]
PubMed ID7479907
JournalProc Natl Acad Sci U S A
Year1995
Volume92
Pages10904-8
AuthorsHjelmqvist L, Estonius M, Jornvall H
TitleThe vertebrate alcohol dehydrogenase system: variable class II type form elucidates separate stages of enzymogenesis.
[11]
PubMed ID8898073
JournalFEBS Lett
Year1996
Volume395
Pages99-102
AuthorsMoreno A, Farres J, Pares X, Jornvall H, Persson B
TitleMolecular modelling of human gastric alcohol dehydrogenase (class IV) and substrate docking: differences towards the classical liver enzyme (class I).
[12]
CommentsX-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
Medline ID96291846
PubMed ID8663387
JournalJ Biol Chem
Year1996
Volume271
Pages17057-61
AuthorsDavis GJ, Bosron WF, Stone CL, Owusu-Dekyi K, Hurley TD
TitleX-ray structure of human beta3beta3 alcohol dehydrogenase. The contribution of ionic interactions to coenzyme binding.
Related PDB1deh,1htb
Related UniProtKBP00325
[13]
PubMed ID9059633
JournalAdv Exp Med Biol
Year1997
Volume414
Pages291-302
AuthorsHurley TD, Steinmetz CG, Xie P, Yang ZN
TitleThree-dimensional structures of human alcohol dehydrogenase isoenzymes reveal the molecular basis for their functional diversity.
[14]
PubMed ID9059632
JournalAdv Exp Med Biol
Year1997
Volume414
Pages281-9
AuthorsJornvall H, Shafqat J, el-Ahmad M, Hjelmqvist L, Persson B, Danielsson O
TitleAlcohol dehydrogenase variability. Evolutionary and functional conclusions from characterization of further variants.
[15]
CommentsX-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
Medline ID97373546
PubMed ID9228021
JournalJ Biol Chem
Year1997
Volume272
Pages18558-63
AuthorsXie P, Parsons SH, Speckhard DC, Bosron WF, Hurley TD
TitleX-ray structure of human class IV sigmasigma alcohol dehydrogenase. Structural basis for substrate specificity.
Related PDB1agn
Related UniProtKBP40394
[16]
PubMed ID9572895
JournalJ Med Chem
Year1998
Volume41
Pages1696-701
AuthorsSchindler JF, Berst KB, Plapp BV
TitleInhibition of human alcohol dehydrogenases by formamides.
[17]
PubMed ID10352708
JournalAdv Exp Med Biol
Year1999
Volume463
Pages373-7
AuthorsPersson B, Nordling E, Kallberg Y, Lundh D, Oppermann UC, Marschall HU, Jornvall H
TitleBioinformatics in studies of SDR and MDR enzymes.
[18]
PubMed ID10407146
JournalBiochim Biophys Acta
Year1999
Volume1432
Pages239-50
AuthorsFoglio MH, Duester G
TitleMolecular docking studies on interaction of diverse retinol structures with human alcohol dehydrogenases predict a broad role in retinoid ligand synthesis.
[19]
CommentsX-ray crystallography
PubMed ID10631979
JournalProtein Sci
Year1999
Volume8
Pages2639-44
AuthorsXie PT, Hurley TD
TitleMethionine-141 directly influences the binding of 4-methylpyrazole in human sigma sigma alcohol dehydrogenase.
Related PDB1d1s,1d1t
[20]
PubMed ID10829036
JournalJ Biol Chem
Year2000
Volume275
Pages25180-7
AuthorsCrosas B, Allali-Hassani A, Martinez SE, Martras S, Persson B, Jornvall H, Pares X, Farres J
TitleMolecular basis for differential substrate specificity in class IV alcohol dehydrogenases: a conserved function in retinoid metabolism but not in ethanol oxidation.
[21]
PubMed ID11306065
JournalChem Biol Interact
Year2001
Volume130-132
Pages435-44
AuthorsAllali-Hassani A, Crosas B, Pares X, Farres J
TitleKinetic effects of a single-amino acid mutation in a highly variable loop (residues 114-120) of class IV ADH.
[22]
PubMed ID11173978
JournalJ Biomed Sci
Year2001
Volume8
Pages71-6
AuthorsHoog JO, Hedberg JJ, Stromberg P, Svensson S
TitleMammalian alcohol dehydrogenase - functional and structural implications.
[23]
CommentsX-ray crystallography
PubMed ID11274460
JournalProtein Sci
Year2001
Volume10
Pages697-706
AuthorsNiederhut MS, Gibbons BJ, Perez-Miller S, Hurley TD
TitleThree-dimensional structures of the three human class I alcohol dehydrogenases.
Related PDB1hso,1hsz,1ht0
[24]
PubMed ID11942822
JournalJ Am Chem Soc
Year2002
Volume124
Pages3858-64
AuthorsKohen A, Jensen JH
TitleBoundary conditions for the Swain-Schaad relationship as a criterion for hydrogen tunneling.
[25]
PubMed ID12604207
JournalChem Biol Interact
Year2003
Volume143-144
Pages219-27
AuthorsYin SJ, Chou CF, Lai CL, Lee SL, Han CL
TitleHuman class IV alcohol dehydrogenase: kinetic mechanism, functional roles and medical relevance.
[26]
PubMed ID14523561
JournalCell Mol Life Sci
Year2003
Volume60
Pages2009-16
AuthorsHjelmqvist L, Norin A, El-Ahmad M, Griffiths W, Jornvall H
TitleDistinct but parallel evolutionary patterns between alcohol and aldehyde dehydrogenases: addition of fish/human betaine aldehyde dehydrogenase divergence.

comments
This enzyme belongs to the human zinc-containing alcohol dehydrogenase class.
Although this enzyme binds two zinc ions, only one zinc is involved in catalysis. This enzyme catalyzes the similar reaction to that of its homologous enzyme (D00001 in EzCatDB). The hydride transfer reaction proceeds as follows:
(0) Catalytic zinc ion, which is bound to Cys46, His67 and Cys174 and the hydroxyl group of the substrate alcohol, may lower the pKa of the hydroxyl oxygen of the alcohol, facilitating its deprotonation.
(1) His51 may act as a general base to deprotonate the hydroxyl oxygen, through 2'-hydroxyl group of NAD+ ribose and Thr48 by a proton relay system, leading to an alkoxide transition-state.
(2) The hydrogen is transferred from the carbon atom of alcohol to the nicotinamide group in the NAD+. Thus, hydride transfer occurs.

createdupdated
2005-01-112010-09-09


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 - )
© Biotechnology Research Institute for Drug Discovery, AIST, 2015-2016 All Rights Reserved.
© Computational Biology Research Center, AIST, 2004-2016 All Rights Reserved.