EzCatDB: M00004

DB codeM00004
CATH domainDomain 13.30.43.10Catalytic domain
Domain 23.30.465.20Catalytic domain
Domain 33.40.462.10Catalytic domain
Domain 41.10.45.10
E.C.1.1.3.38
CSA1vao
MACiEM0103

CATH domainRelated DB codes (homologues)
1.10.45.10M00179
3.30.43.10M00001,M00039,M00179,T00003
3.30.465.20M00001,M00179
3.40.462.10M00179

Enzyme Name
Swiss-protKEGG

P56216
Protein nameVanillyl-alcohol oxidasevanillyl-alcohol oxidase
4-hydroxy-2-methoxybenzyl alcohol oxidase
SynonymsEC 1.1.3.38
Aryl-alcohol oxidase
4-allylphenol oxidase

KEGG pathways
MAP codePathways
MAP006232,4-Dichlorobenzoate degradation

Swiss-prot:Accession NumberP56216
Entry nameVAOX_PENSI
ActivityVanillyl alcohol + O(2) = vanillin + H(2)O(2).
SubunitHomooctamer (tetramer of tightly interacting dimers).
Subcellular locationPeroxisome. Cytoplasm.
CofactorBinds 1 FAD covalently per subunit.


CofactorsSubstratesProductsintermediates
KEGG-idC00016C06317C00007C00755C00027
CompoundFADVanillyl alcoholO2VanillinH2O2p-quinone methide intermediate
Typeamide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carbohydrate,nucleotidearomatic ring (only carbon atom),carbohydrateothersaromatic ring (only carbon atom),carbohydrateothers
1ahuA01Analogue:FAAUnboundUnboundUnboundUnboundUnbound
1ahuB01Analogue:FAAUnboundUnboundUnboundUnboundUnbound
1ahvA01Bound:FADUnboundUnboundUnboundUnboundUnbound
1ahvB01Bound:FADUnboundUnboundUnboundUnboundUnbound
1ahzA01Bound:FADUnboundUnboundUnboundUnboundUnbound
1ahzB01Bound:FADUnboundUnboundUnboundUnboundUnbound
1dznA01Bound:FADUnboundUnboundUnboundUnboundUnbound
1dznB01Bound:FADUnboundUnboundUnboundUnboundUnbound
1e0yA01Bound:FADUnboundUnboundUnboundUnboundUnbound
1e0yB01Bound:FADUnboundUnboundUnboundUnboundUnbound
1e8fA01UnboundUnboundUnboundUnboundUnboundUnbound
1e8fB01UnboundUnboundUnboundUnboundUnboundUnbound
1e8gA01Bound:FADUnboundUnboundUnboundUnboundUnbound
1e8gB01Bound:FADUnboundUnboundUnboundUnboundUnbound
1e8hA01Analogue:ADPUnboundUnboundUnboundUnboundUnbound
1e8hB01Analogue:ADPUnboundUnboundUnboundUnboundUnbound
1qltA01Bound:FADUnboundUnboundUnboundUnboundUnbound
1qltB01Bound:FADUnboundUnboundUnboundUnboundUnbound
1qluA01Bound:FADUnboundUnboundUnboundUnboundUnbound
1qluB01Bound:FADUnboundUnboundUnboundUnboundUnbound
1vaoA01Bound:FADUnboundUnboundUnboundUnboundUnbound
1vaoB01Bound:FADUnboundUnboundUnboundUnboundUnbound
1w1jA01Bound:FADUnboundUnboundUnboundUnboundUnbound
1w1jB01Bound:FADUnboundUnboundUnboundUnboundUnbound
1w1kA01Bound:FADUnboundUnboundUnboundUnboundUnbound
1w1kB01Bound:FADUnboundUnboundUnboundUnboundUnbound
1w1lA01Analogue:EUG-FADUnboundUnboundUnboundUnboundUnbound
1w1lB01Analogue:EUG-FADUnboundUnboundUnboundUnboundUnbound
1w1mA01Bound:FADUnboundUnboundUnboundUnboundUnbound
1w1mB01Bound:FADUnboundUnboundUnboundUnboundUnbound
2vaoA01Bound:FADUnboundUnboundUnboundUnboundUnbound
2vaoB01Bound:FADUnboundUnboundUnboundUnboundUnbound
1ahuA02UnboundUnboundUnboundUnboundUnboundUnbound
1ahuB02UnboundUnboundUnboundUnboundUnboundUnbound
1ahvA02UnboundUnboundUnboundUnboundUnboundUnbound
1ahvB02UnboundUnboundUnboundUnboundUnboundUnbound
1ahzA02UnboundUnboundUnboundUnboundUnboundUnbound
1ahzB02UnboundUnboundUnboundUnboundUnboundUnbound
1dznA02UnboundUnboundUnboundUnboundUnboundUnbound
1dznB02UnboundUnboundUnboundUnboundUnboundUnbound
1e0yA02UnboundUnboundUnboundUnboundUnboundUnbound
1e0yB02UnboundUnboundUnboundUnboundUnboundUnbound
1e8fA02UnboundUnboundUnboundUnboundUnboundUnbound
1e8fB02UnboundUnboundUnboundUnboundUnboundUnbound
1e8gA02UnboundUnboundUnboundUnboundUnboundUnbound
1e8gB02UnboundUnboundUnboundUnboundUnboundUnbound
1e8hA02UnboundUnboundUnboundUnboundUnboundUnbound
1e8hB02UnboundUnboundUnboundUnboundUnboundUnbound
1qltA02UnboundUnboundUnboundUnboundUnboundUnbound
1qltB02UnboundUnboundUnboundUnboundUnboundUnbound
1qluA02UnboundUnboundUnboundUnboundUnboundUnbound
1qluB02UnboundUnboundUnboundUnboundUnboundUnbound
1vaoA02UnboundUnboundUnboundUnboundUnboundUnbound
1vaoB02UnboundUnboundUnboundUnboundUnboundUnbound
1w1jA02UnboundUnboundUnboundUnboundUnboundUnbound
1w1jB02UnboundUnboundUnboundUnboundUnboundUnbound
1w1kA02UnboundUnboundUnboundUnboundUnboundUnbound
1w1kB02UnboundUnboundUnboundUnboundUnboundUnbound
1w1lA02UnboundUnboundUnboundUnboundUnboundUnbound
1w1lB02UnboundUnboundUnboundUnboundUnboundUnbound
1w1mA02UnboundUnboundUnboundUnboundUnboundUnbound
1w1mB02UnboundUnboundUnboundUnboundUnboundUnbound
2vaoA02UnboundUnboundUnboundUnboundUnboundUnbound
2vaoB02UnboundUnboundUnboundUnboundUnboundUnbound
1ahuA03UnboundAnalogue:FAAUnboundUnboundUnboundUnbound
1ahuB03UnboundAnalogue:FAAUnboundUnboundUnboundUnbound
1ahvA03UnboundAnalogue:NCRUnboundUnboundUnboundUnbound
1ahvB03UnboundAnalogue:NCRUnboundUnboundUnboundUnbound
1ahzA03UnboundAnalogue:EPTUnboundUnboundUnboundUnbound
1ahzB03UnboundUnboundUnboundUnboundUnboundUnbound
1dznA03UnboundUnboundUnboundAnalogue:EUGUnboundUnbound
1dznB03UnboundUnboundUnboundAnalogue:EUGUnboundUnbound
1e0yA03UnboundUnboundUnboundUnboundUnboundUnbound
1e0yB03UnboundAnalogue:FCRUnboundUnboundUnboundUnbound
1e8fA03UnboundUnboundUnboundUnboundUnboundUnbound
1e8fB03UnboundUnboundUnboundUnboundUnboundUnbound
1e8gA03UnboundAnalogue:FCRUnboundUnboundUnboundUnbound
1e8gB03UnboundAnalogue:FCRUnboundUnboundUnboundUnbound
1e8hA03UnboundUnboundUnboundUnboundUnboundUnbound
1e8hB03UnboundUnboundUnboundUnboundUnboundUnbound
1qltA03UnboundUnboundUnboundUnboundUnboundUnbound
1qltB03UnboundUnboundUnboundUnboundUnboundUnbound
1qluA03UnboundAnalogue:EUGUnboundAnalogue:EUGUnboundUnbound
1qluB03UnboundAnalogue:EUGUnboundAnalogue:EUGUnboundUnbound
1vaoA03UnboundUnboundUnboundUnboundUnboundUnbound
1vaoB03UnboundUnboundUnboundUnboundUnboundUnbound
1w1jA03UnboundUnboundUnboundAnalogue:EUGUnboundUnbound
1w1jB03UnboundUnboundUnboundAnalogue:EUGUnboundUnbound
1w1kA03UnboundUnboundUnboundAnalogue:EUGUnboundUnbound
1w1kB03UnboundUnboundUnboundAnalogue:EUGUnboundUnbound
1w1lA03UnboundUnboundUnboundAnalogue:EUGUnboundUnbound
1w1lB03UnboundUnboundUnboundAnalogue:EUGUnboundUnbound
1w1mA03UnboundUnboundUnboundAnalogue:EUGUnboundUnbound
1w1mB03UnboundUnboundUnboundAnalogue:EUGUnboundUnbound
2vaoA03UnboundUnboundUnboundAnalogue:EUGUnboundUnbound
2vaoB03UnboundUnboundUnboundAnalogue:EUGUnboundUnbound
1ahuA04UnboundUnboundUnboundUnboundUnboundUnbound
1ahuB04UnboundUnboundUnboundUnboundUnboundUnbound
1ahvA04UnboundUnboundUnboundUnboundUnboundUnbound
1ahvB04UnboundUnboundUnboundUnboundUnboundUnbound
1ahzA04UnboundUnboundUnboundUnboundUnboundUnbound
1ahzB04UnboundUnboundUnboundUnboundUnboundUnbound
1dznA04UnboundUnboundUnboundUnboundUnboundUnbound
1dznB04UnboundUnboundUnboundUnboundUnboundUnbound
1e0yA04UnboundUnboundUnboundUnboundUnboundUnbound
1e0yB04UnboundUnboundUnboundUnboundUnboundUnbound
1e8fA04UnboundUnboundUnboundUnboundUnboundUnbound
1e8fB04UnboundUnboundUnboundUnboundUnboundUnbound
1e8gA04UnboundUnboundUnboundUnboundUnboundUnbound
1e8gB04UnboundUnboundUnboundUnboundUnboundUnbound
1e8hA04UnboundUnboundUnboundUnboundUnboundUnbound
1e8hB04UnboundUnboundUnboundUnboundUnboundUnbound
1qltA04UnboundUnboundUnboundUnboundUnboundUnbound
1qltB04UnboundUnboundUnboundUnboundUnboundUnbound
1qluA04UnboundUnboundUnboundUnboundUnboundUnbound
1qluB04UnboundUnboundUnboundUnboundUnboundUnbound
1vaoA04UnboundUnboundUnboundUnboundUnboundUnbound
1vaoB04UnboundUnboundUnboundUnboundUnboundUnbound
1w1jA04UnboundUnboundUnboundUnboundUnboundUnbound
1w1jB04UnboundUnboundUnboundUnboundUnboundUnbound
1w1kA04UnboundUnboundUnboundUnboundUnboundUnbound
1w1kB04UnboundUnboundUnboundUnboundUnboundUnbound
1w1lA04UnboundUnboundUnboundUnboundUnboundUnbound
1w1lB04UnboundUnboundUnboundUnboundUnboundUnbound
1w1mA04UnboundUnboundUnboundUnboundUnboundUnbound
1w1mB04UnboundUnboundUnboundUnboundUnboundUnbound
2vaoA04UnboundUnboundUnboundUnboundUnboundUnbound
2vaoB04UnboundUnboundUnboundUnboundUnboundUnbound

Active-site residues
resource
Swiss-prot;P56216 & literature [10]
pdbCatalytic residuesCofactor-binding residuescomment
1ahuA01TYR 108


1ahuB01TYR 108


1ahvA01TYR 108


1ahvB01TYR 108


1ahzA01TYR 108


1ahzB01TYR 108


1dznA01TYR 108


1dznB01TYR 108


1e0yA01TYR 108


1e0yB01TYR 108


1e8fA01TYR 108

mutant H61T
1e8fB01TYR 108

mutant H61T
1e8gA01TYR 108

mutant H61T
1e8gB01TYR 108

mutant H61T
1e8hA01TYR 108

mutant H61T
1e8hB01TYR 108

mutant H61T
1qltA01TYR 108


1qltB01TYR 108


1qluA01TYR 108


1qluB01TYR 108


1vaoA01TYR 108


1vaoB01TYR 108


1w1jA01TYR 108


1w1jB01TYR 108


1w1kA01TYR 108


1w1kB01TYR 108


1w1lA01TYR 108


1w1lB01TYR 108


1w1mA01TYR 108


1w1mB01TYR 108


2vaoA01TYR 108


2vaoB01TYR 108


1ahuA02ASP 170


1ahuB02ASP 170


1ahvA02ASP 170


1ahvB02ASP 170


1ahzA02ASP 170


1ahzB02ASP 170


1dznA02       

mutant D170S
1dznB02       

mutant D170S
1e0yA02       

mutant D170S
1e0yB02       

mutant D170S
1e8fA02ASP 170


1e8fB02ASP 170


1e8gA02ASP 170


1e8gB02ASP 170


1e8hA02ASP 170


1e8hB02ASP 170


1qltA02ASP 170


1qltB02ASP 170


1qluA02ASP 170


1qluB02ASP 170


1vaoA02ASP 170


1vaoB02ASP 170


1w1jA02ASP 170


1w1jB02ASP 170


1w1kA02ASP 170

mutant I238T
1w1kB02ASP 170

mutant I238T
1w1lA02ASP 170


1w1lB02ASP 170


1w1mA02ASP 170


1w1mB02ASP 170


2vaoA02ASP 170


2vaoB02ASP 170


1ahuA03TYR 503;ARG 504
HIS 422(FAD binding)

1ahuB03TYR 503;ARG 504
HIS 422(FAD binding)

1ahvA03TYR 503;ARG 504
HIS 422(FAD binding)

1ahvB03TYR 503;ARG 504
HIS 422(FAD binding)

1ahzA03TYR 503;ARG 504
HIS 422(FAD binding)

1ahzB03TYR 503;ARG 504
HIS 422(FAD binding)

1dznA03TYR 503;ARG 504
HIS 422(FAD binding)

1dznB03TYR 503;ARG 504
HIS 422(FAD binding)

1e0yA03TYR 503;ARG 504
HIS 422(FAD binding)
mutant T457E
1e0yB03TYR 503;ARG 504
HIS 422(FAD binding)
mutant T457E
1e8fA03TYR 503;ARG 504
HIS 422(FAD binding)

1e8fB03TYR 503;ARG 504
HIS 422(FAD binding)

1e8gA03TYR 503;ARG 504
HIS 422(FAD binding)

1e8gB03TYR 503;ARG 504
HIS 422(FAD binding)

1e8hA03TYR 503;ARG 504
HIS 422(FAD binding)

1e8hB03TYR 503;ARG 504
HIS 422(FAD binding)

1qltA03TYR 503;ARG 504
                    
mutant H422A
1qltB03TYR 503;ARG 504
                    
mutant H422A
1qluA03TYR 503;ARG 504
                    
mutant H422A
1qluB03TYR 503;ARG 504
                    
mutant H422A
1vaoA03TYR 503;ARG 504
HIS 422(FAD binding)

1vaoB03TYR 503;ARG 504
HIS 422(FAD binding)

1w1jA03TYR 503;ARG 504
HIS 422(FAD binding)
mutant T505S
1w1jB03TYR 503;ARG 504
HIS 422(FAD binding)
mutant T505S
1w1kA03TYR 503;ARG 504
HIS 422(FAD binding)

1w1kB03TYR 503;ARG 504
HIS 422(FAD binding)

1w1lA03TYR 503;ARG 504
HIS 422(FAD binding)
mutant F454Y
1w1lB03TYR 503;ARG 504
HIS 422(FAD binding)
mutant F454Y
1w1mA03TYR 503;ARG 504
HIS 422(FAD binding)
mutant E502G
1w1mB03TYR 503;ARG 504
HIS 422(FAD binding)
mutant E502G
2vaoA03TYR 503;ARG 504
HIS 422(FAD binding)

2vaoB03TYR 503;ARG 504
HIS 422(FAD binding)

1ahuA04


1ahuB04


1ahvA04


1ahvB04


1ahzA04


1ahzB04


1dznA04


1dznB04


1e0yA04


1e0yB04


1e8fA04


1e8fB04


1e8gA04


1e8gB04


1e8hA04


1e8hB04


1qltA04


1qltB04


1qluA04


1qluB04


1vaoA04


1vaoB04


1w1jA04


1w1jB04


1w1kA04


1w1kB04


1w1lA04


1w1lB04


1w1mA04


1w1mB04


2vaoA04


2vaoB04



References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[2]p.276-277
[4]Equation 4, Scheme 1, p.18115-18116
[6]Fig.10, p.915-917
[7]Scheme 1, p.35518-35520
[8]Scheme 1, Fig.3, p.109
[10]Fig.1, Fig.8, p.14806-14807
[11]Scheme 1, Fig.5, p.9454-9456
[13]Fig.1
[16]Fig.2, p.182-186
[17]Fig.1, p.33498-33499

references
[1]
CommentsCHARACTERIZATION
Medline ID93011092
PubMed ID1396672
JournalEur J Biochem
Year1992
Volume208
Pages651-7
Authorsde Jong E, van Berkel WJ, van der Zwan RP, de Bont JA
TitlePurification and characterization of vanillyl-alcohol oxidase from Penicillium simplicissimum. A novel aromatic alcohol oxidase containing covalently bound FAD.
Related Swiss-protP56216
[2]
CommentsSUBSTRATE SPECIFICITY
Medline ID96096749
PubMed ID8529652
JournalEur J Biochem
Year1995
Volume234
Pages271-7
AuthorsFraaije MW, Veeger C, van Berkel WJ
TitleSubstrate specificity of flavin-dependent vanillyl-alcohol oxidase from Penicillium simplicissimum. Evidence for the production of 4-hydroxycinnamyl alcohols from 4-allylphenols.
Related Swiss-protP56216
[3]
PubMed ID9013853
JournalFEBS Lett
Year1997
Volume402
Pages33-5
AuthorsFraaije MW, Mattevi A, van Berkel WJ
TitleMercuration of vanillyl-alcohol oxidase from Penicillium simplicissimum generates inactive dimers.
[4]
PubMed ID9218444
JournalJ Biol Chem
Year1997
Volume272
Pages18111-6
AuthorsFraaije MW, van Berkel WJ
TitleCatalytic mechanism of the oxidative demethylation of 4-(methoxymethyl)phenol by vanillyl-alcohol oxidase. Evidence for formation of a p-quinone methide intermediate.
[5]
CommentsX-RAY CRYSTALLOGRAPHY (2.5 AND 3.2 ANGSTROMS)
Medline ID97285922
PubMed ID9141139
JournalProteins
Year1997
Volume27
Pages601-3
AuthorsMattevi A, Fraaije MW, Coda A, van Berkel WJ
TitleCrystallization and preliminary X-ray analysis of the flavoenzyme vanillyl-alcohol oxidase from Penicillium simplicissimum.
Related PDB1ahu,1ahv,1ahz,1vao,2vao
Related Swiss-protP56216
[6]
PubMed ID9261083
JournalStructure
Year1997
Volume5
Pages907-20
AuthorsMattevi A, Fraaije MW, Mozzarelli A, Olivi L, Coda A, van Berkel WJ
TitleCrystal structures and inhibitor binding in the octameric flavoenzyme vanillyl-alcohol oxidase: the shape of the active-site cavity controls substrate specificity.
[7]
CommentsX-RAY CRYSTALLOGRAPHY OF MUTANTS (2.2 ANGSTROMS)
Medline ID20054426
PubMed ID10585424
JournalJ Biol Chem
Year1999
Volume274
Pages35514-20
AuthorsFraaije MW, van den Heuvel RH, van Berkel WJ, Mattevi A
TitleCovalent flavinylation is essential for efficient redox catalysis in vanillyl-alcohol oxidase.
Related PDB1qlt,1qlu
Related Swiss-protP56216
[8]
PubMed ID10996306
JournalFEBS Lett
Year2000
Volume481
Pages109-12
Authorsvan den Heuvel RH, Fraaije MW, van Berkel WJ
TitleDirection of the reactivity of vanillyl-alcohol oxidase with 4-alkylphenols.
[9]
CommentsX-RAY CRYSTALLOGRAPHY OF MUTANTS (2.1 ANGSTROMS)
Medline ID20556311
PubMed ID10984479
JournalJ Biol Chem
Year2000
Volume275
Pages38654-8
AuthorsFraaije MW, van Den Heuvel RH, van Berkel WJ, Mattevi A
TitleStructural analysis of flavinylation in vanillyl-alcohol oxidase.
Related PDB1e8f,1e8g,1e8h
Related Swiss-protP56216
[10]
CommentsX-RAY CRYSTALLOGRAPHY OF D170S MUTANT (2.8 ANGSTROMS)
Medline ID20270176
PubMed ID10809721
JournalJ Biol Chem
Year2000
Volume275
Pages14799-808
Authorsvan den Heuvel RH, Fraaije MW, Mattevi A, van Berkel WJ
TitleAsp-170 is crucial for the redox properties of vanillyl-alcohol oxidase.
Related PDB1dzn
Related Swiss-protP56216
[11]
CommentsX-RAY CRYSTALLOGRAPHY OF D170S/T457E MUTANT (2.75 ANGSTROMS)
Medline ID20402555
PubMed ID10920192
JournalProc Natl Acad Sci U S A
Year2000
Volume97
Pages9455-60
Authorsvan Den Heuvel RH, Fraaije MW, Ferrer M, Mattevi A, van Berkel WJ
TitleInversion of stereospecificity of vanillyl-alcohol oxidase.
Related PDB1e0y
Related Swiss-protP56216
[12]
PubMed ID10752605
JournalProtein Sci
Year2000
Volume9
Pages435-9
Authorsvan Berkel WJ, van den Heuvel RH, Versluis C, Heck AJ
TitleDetection of intact megaDalton protein assemblies of vanillyl-alcohol oxidase by mass spectrometry.
[13]
PubMed ID10694883
JournalTrends Biochem Sci
Year2000
Volume25
Pages126-32
AuthorsFraaije MW, Mattevi A
TitleFlavoenzymes: diverse catalysts with recurrent features.
[14]
PubMed ID11513884
JournalFEBS Lett
Year2001
Volume503
Pages213-6
Authorsvan den Heuvel RH, Partridge J, Laane C, Halling PJ, van Berkel WJ
TitleTuning of the product spectrum of vanillyl-alcohol oxidase by medium engineering.
[15]
PubMed ID12107187
JournalJ Biol Chem
Year2002
Volume277
Pages36425-32
AuthorsTahallah N, Van Den Heuvel RH, Van Den Berg WA, Maier CS, Van Berkel WJ, Heck AJ
TitleCofactor-dependent assembly of the flavoenzyme vanillyl-alcohol oxidase.
[16]
PubMed ID12078493
JournalMethods Enzymol
Year2002
Volume353
Pages177-86
Authorsvan den Heuvel RH, Fraaije MW, van Berkel WJ
TitleRedox properties of vanillyl-alcohol oxidase.
[17]
CommentsX-ray crystallography
PubMed ID15169773
JournalJ Biol Chem
Year2004
Volume279
Pages33492-500
Authorsvan den Heuvel RH, van den Berg WA, Rovida S, van Berkel WJ
TitleLaboratory-evolved vanillyl-alcohol oxidase produces natural vanillin.
Related PDB1w1j,1w1k,1w1l,1w1m

comments
Although vanillyl alcohol (C06317) is annotated as a substrate, 4-(methoxymethyl)phenol seems to be a major substrate, according to the literature. This enzyme seems to catalyze oxidative demethylation of 4-(methoxymethyl)phenol.
According to the literature [10], this enzyme catalyzes the following reactions:
(A) Hydride transfer from methyl group of substrate to FAD, forming p-quinone methide intermediate and FADH2:
(B) Hydride transfer from FADH2 to O2 (Re-oxidation of FAD by O2, releasing H2O2):
(C) Additive double-bond deformation; Addition of H2O to p-quinone methide intermediate (Hydroxylation):
(D) Eliminative double-bond formation; Elimination of H2O (or Elimination of methanol in the case of 4-(methoxymethyl)phenol as a substrate):

createdupdated
2005-06-012009-02-26
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)

© Computational Biology Research Center, AIST, 2004 All Rights Reserved.