EzCatDB: T00211
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DB codeT00211
CATH domainDomain 13.90.660.10 : Polyamine Oxidase; Chain A, domain 2Catalytic domain
Domain 23.50.50.60 : FAD/NAD(P)-binding domain
Domain 31.10.405.10 : Guanine Nucleotide Dissociation Inhibitor; domain 1Catalytic domain
E.C.1.4.3.2
CSA1f8r

CATH domainRelated DB codes (homologues)
3.50.50.60 : FAD/NAD(P)-binding domainM00163,D00015,D00041,D00042,D00045,D00064,D00071,T00004,T00015,T00017,T00025,T00213,T00233,T00242
3.90.660.10 : Polyamine Oxidase; Chain A, domain 2D00042

Enzyme Name
UniProtKBKEGG

P81382
Protein nameL-amino-acid oxidaseL-amino-acid oxidase
ophio-amino-acid oxidase
SynonymsLAAO
LAO
EC 1.4.3.2
PfamPF01593 (Amino_oxidase)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00252Alanine and aspartate metabolism
MAP00271Methionine metabolism
MAP00280Valine, leucine and isoleucine degradation
MAP00350Tyrosine metabolism
MAP00360Phenylalanine metabolism
MAP00380Tryptophan metabolism
MAP00400Phenylalanine, tyrosine and tryptophan biosynthesis
MAP00950Alkaloid biosynthesis I

UniProtKB:Accession NumberP81382
Entry nameOXLA_AGKRH
ActivityAn L-amino acid + H(2)O + O(2) = a 2-oxo acid + NH(3) + H(2)O(2).
SubunitHomodimer.
Subcellular locationSecreted.
CofactorFAD.

Compound table: links to PDB-related databases & PoSSuM

CofactorsSubstratesProducts
KEGG-idC00016C00001C00007C00151C00014C00027C00161
CompoundFADH2OO2L-Amino acidNH3H2O22-Oxo acid
Typeamide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carbohydrate,nucleotideH2Oothersamino acidsamine group,organic ionotherscarbohydrate,carboxyl group
ChEBI16238
15377
27140
26689
15379

16134
16240

PubChem643975
962
22247451
977

222
784
22326046

               
1f8rA01Unbound UnboundUnboundUnboundUnboundAnalogue:CIT
1f8rB01Unbound UnboundUnboundUnboundUnboundAnalogue:CIT
1f8rC01Unbound UnboundUnboundUnboundUnboundAnalogue:CIT
1f8rD01Unbound UnboundUnboundUnboundUnboundAnalogue:CIT
1f8sA01Unbound UnboundAnalogue:BE2 1UnboundUnboundUnbound
1f8sB01Unbound UnboundAnalogue:BE2 4UnboundUnboundUnbound
1f8sC01Unbound UnboundAnalogue:BE2 7UnboundUnboundUnbound
1f8sD01Unbound UnboundAnalogue:BE2 10UnboundUnboundUnbound
1f8sE01Unbound UnboundAnalogue:BE2 13UnboundUnboundUnbound
1f8sF01Unbound UnboundAnalogue:BE2 16UnboundUnboundUnbound
1f8sG01Unbound UnboundAnalogue:BE2 19UnboundUnboundUnbound
1f8sH01Unbound UnboundAnalogue:BE2 22UnboundUnboundUnbound
1tdkA01Unbound UnboundBound:LVG 491UnboundUnboundUnbound
1tdnA01Unbound UnboundBound:LEUUnboundUnboundUnbound
1tdoA01Unbound UnboundBound:PHEUnboundUnboundUnbound
1reoA01Unbound UnboundUnboundUnboundUnboundAnalogue:CIT
1f8rA02Bound:FAD UnboundUnboundUnboundUnboundUnbound
1f8rB02Bound:FAD UnboundUnboundUnboundUnboundUnbound
1f8rC02Bound:FAD UnboundUnboundUnboundUnboundUnbound
1f8rD02Bound:FAD UnboundUnboundUnboundUnboundUnbound
1f8sA02Bound:FAD UnboundUnboundUnboundUnboundUnbound
1f8sB02Bound:FAD UnboundUnboundUnboundUnboundUnbound
1f8sC02Bound:FAD UnboundUnboundUnboundUnboundUnbound
1f8sD02Bound:FAD UnboundUnboundUnboundUnboundUnbound
1f8sE02Bound:FAD UnboundUnboundUnboundUnboundUnbound
1f8sF02Bound:FAD UnboundUnboundUnboundUnboundUnbound
1f8sG02Bound:FAD UnboundUnboundUnboundUnboundUnbound
1f8sH02Bound:FAD UnboundUnboundUnboundUnboundUnbound
1tdkA02Bound:FAD UnboundUnboundUnboundUnboundUnbound
1tdnA02Bound:FAD UnboundUnboundUnboundUnboundUnbound
1tdoA02Bound:FAD UnboundUnboundUnboundUnboundUnbound
1reoA02Bound:FAD UnboundUnboundUnboundUnboundUnbound
1f8rA03Unbound UnboundUnboundUnboundUnboundUnbound
1f8rB03Unbound UnboundUnboundUnboundUnboundUnbound
1f8rC03Unbound UnboundUnboundUnboundUnboundUnbound
1f8rD03Unbound UnboundUnboundUnboundUnboundUnbound
1f8sA03Unbound UnboundUnboundUnboundUnboundUnbound
1f8sB03Unbound UnboundUnboundUnboundUnboundUnbound
1f8sC03Unbound UnboundUnboundUnboundUnboundUnbound
1f8sD03Unbound UnboundUnboundUnboundUnboundUnbound
1f8sE03Unbound UnboundUnboundUnboundUnboundUnbound
1f8sF03Unbound UnboundUnboundUnboundUnboundUnbound
1f8sG03Unbound UnboundUnboundUnboundUnboundUnbound
1f8sH03Unbound UnboundUnboundUnboundUnboundUnbound
1tdkA03Unbound UnboundUnboundUnboundUnboundUnbound
1tdnA03Unbound UnboundUnboundUnboundUnboundUnbound
1tdoA03Unbound UnboundUnboundUnboundUnboundUnbound
1reoA03Unbound UnboundUnboundUnboundUnboundUnbound

Active-site residues
resource
literature [5]
pdbCatalytic residues
         
1f8rA01LYS 326
1f8rB01LYS 326
1f8rC01LYS 326
1f8rD01LYS 326
1f8sA01LYS 326
1f8sB01LYS 326
1f8sC01LYS 326
1f8sD01LYS 326
1f8sE01LYS 326
1f8sF01LYS 326
1f8sG01LYS 326
1f8sH01LYS 326
1tdkA01LYS 326
1tdnA01LYS 326
1tdoA01LYS 326
1reoA01LYS 326
1f8rA02 
1f8rB02 
1f8rC02 
1f8rD02 
1f8sA02 
1f8sB02 
1f8sC02 
1f8sD02 
1f8sE02 
1f8sF02 
1f8sG02 
1f8sH02 
1tdkA02 
1tdnA02 
1tdoA02 
1reoA02 
1f8rA03HIS 223
1f8rB03HIS 223
1f8rC03HIS 223
1f8rD03HIS 223
1f8sA03HIS 223
1f8sB03HIS 223
1f8sC03HIS 223
1f8sD03HIS 223
1f8sE03HIS 223
1f8sF03HIS 223
1f8sG03HIS 223
1f8sH03HIS 223
1tdkA03HIS 223
1tdnA03HIS 223
1tdoA03HIS 223
1reoA03HIS 223

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[5]Scheme 1, p.4212-42132
[7]Scheme 1
[8]Scheme 1
[11]Fig.1, Fig.4, p.23975-23976

references
[1]
PubMed ID2044840
JournalInt J Biochem
Year1991
Volume23
Pages323-7
AuthorsTan NH, Saifuddin MN
TitleSubstrate specificity of king cobra (Ophiophagus hannah) venom L-amino acid oxidase.
[2]
PubMed ID8755511
JournalProc Natl Acad Sci U S A
Year1996
Volume93
Pages7546-51
AuthorsRaibekas AA, Massey V
TitleGlycerol-induced development of catalytically active conformation of Crotalus adamanteus L-amino acid oxidase in vitro.
[3]
PubMed ID10441379
JournalArch Biochem Biophys
Year1999
Volume368
Pages285-90
AuthorsSouza DH, Eugenio LM, Fletcher JE, Jiang MS, Garratt RC, Oliva G, Selistre-de-Araujo HS
TitleIsolation and structural characterization of a cytotoxic L-amino acid oxidase from Agkistrodon contortrix laticinctus snake venom: preliminary crystallographic data.
[4]
PubMed ID11368308
JournalArch Biochem Biophys
Year2000
Volume384
Pages216-26
AuthorsAli SA, Stoeva S, Abbasi A, Alam JM, Kayed R, Faigle M, Neumeister B, Voelter W
TitleIsolation, structural, and functional characterization of an apoptosis-inducing L-amino acid oxidase from leaf-nosed viper (Eristocophis macmahoni) snake venom.
[5]
CommentsX-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), AND CARBOHYDRATE-LINKAGE SITES
Medline ID20402326
PubMed ID10944103
JournalEMBO J
Year2000
Volume19
Pages4204-15
AuthorsPawelek PD, Cheah J, Coulombe R, Macheroux P, Ghisla S, Vrielink A
TitleThe structure of L-amino acid oxidase reveals the substrate trajectory into an enantiomerically conserved active site.
Related PDB1f8r,1f8s
Related UniProtKBP81382
[6]
PubMed ID11341935
JournalBiochim Biophys Acta
Year2001
Volume1544
Pages267-77
AuthorsTakatsuka H, Sakurai Y, Yoshioka A, Kokubo T, Usami Y, Suzuki M, Matsui T, Titani K, Yagi H, Matsumoto M, Fujimura Y
TitleMolecular characterization of L-amino acid oxidase from Agkistrodon halys blomhoffii with special reference to platelet aggregation.
[7]
PubMed ID11453999
JournalEur J Biochem
Year2001
Volume268
Pages4044-53
AuthorsGeyer A, Fitzpatrick TB, Pawelek PD, Kitzing K, Vrielink A, Ghisla S, Macheroux P
TitleStructure and characterization of the glycan moiety of L-amino-acid oxidase from the Malayan pit viper Calloselasma rhodostoma.
[8]
PubMed ID11248687
JournalEur J Biochem
Year2001
Volume268
Pages1679-86
AuthorsMacHeroux P, Seth O, Bollschweiler C, Schwarz M, Kurfurst M, Au LC, Ghisla S
TitleL-amino-acid oxidase from the Malayan pit viper Calloselasma rhodostoma. Comparative sequence analysis and characterization of active and inactive forms of the enzyme.
[9]
PubMed ID12031486
JournalBiochim Biophys Acta
Year2002
Volume1576
Pages70-80
AuthorsChavan SS, Tian W, Hsueh K, Jawaheer D, Gregersen PK, Chu CC
TitleCharacterization of the human homolog of the IL-4 induced gene-1 (Fig1).
[10]
JournalEnzyme Microb Technol
Year2002
Volume31
Pages77-87
AuthorsGeueke B, Hummel W
TitleA new bacterial L-amino acid oxidase with a broad substrate specificity: purification and characterization.
[11]
PubMed ID12015330
JournalJ Biol Chem
Year2002
Volume277
Pages23973-6
AuthorsBinda C, Mattevi A, Edmondson DE
TitleStructure-function relationships in flavoenzyme-dependent amine oxidations: a comparison of polyamine oxidase and monoamine oxidase.
[12]
PubMed ID12175601
JournalToxicon
Year2002
Volume40
Pages659-65
AuthorsDu XY, Clemetson KJ
TitleSnake venom L-amino acid oxidases.
[13]
PubMed ID14636049
JournalBiochemistry
Year2003
Volume42
Pages13826-32
AuthorsSobrado P, Fitzpatrick PF
TitleAnalysis of the role of the active site residue Arg98 in the flavoprotein tryptophan 2-monooxygenase, a member of the L-amino oxidase family.
[14]
PubMed ID15103157
JournalActa Crystallogr D Biol Crystallogr
Year2004
Volume60
Pages974-7
AuthorsZhang H, Teng M, Niu L, Wang Y, Wang Y, Liu Q, Huang Q, Hao Q, Dong Y, Liu P
TitlePurification, partial characterization, crystallization and structural determination of AHP-LAAO, a novel L-amino-acid oxidase with cell apoptosis-inducing activity from Agkistrodon halys pallas venom.
Related PDB1tdk,1tdn,1tdo,1reo

comments
This enzyme catalyzes three distinct reactions (see [7], [8] & [11]):
(A) Hydride transfer from amine group to FAD(ox)
(B) Exchange of double-bonded atoms (Schiff-base deformation)
(C) Hydride transfer from FADH2(red) to O2

createdupdated
2004-06-182009-02-26


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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