DB code: T00211
CATH domain | 3.90.660.10 : Polyamine Oxidase; Chain A, domain 2 | Catalytic domain |
---|---|---|
3.50.50.60 : FAD/NAD(P)-binding domain | ||
1.10.405.10 : Guanine Nucleotide Dissociation Inhibitor; domain 1 | Catalytic domain | |
E.C. | 1.4.3.2 | |
CSA | 1f8r | |
M-CSA | 1f8r | |
MACiE |
CATH domain | Related DB codes (homologues) |
---|---|
3.50.50.60 : FAD/NAD(P)-binding domain | M00163 D00015 D00041 D00042 D00045 D00064 D00071 T00004 T00015 T00017 T00025 T00213 T00233 T00242 |
3.90.660.10 : Polyamine Oxidase; Chain A, domain 2 | D00042 |
Uniprot Enzyme Name | UniprotKB | Protein name | Synonyms | Pfam |
---|---|---|---|
P81382 |
L-amino-acid oxidase
|
LAAO
LAO EC 1.4.3.2 |
PF01593
(Amino_oxidase)
[Graphical View] |
KEGG enzyme name |
---|
L-amino-acid oxidase
ophio-amino-acid oxidase |
UniprotKB: Accession Number | Entry name | Activity | Subunit | Subcellular location | Cofactor |
---|---|---|---|---|---|
P81382 | OXLA_AGKRH | An L-amino acid + H(2)O + O(2) = a 2-oxo acid + NH(3) + H(2)O(2). | Homodimer. | Secreted. | FAD. |
KEGG Pathways | Map code | Pathways | E.C. |
---|---|---|
MAP00252 | Alanine and aspartate metabolism | |
MAP00271 | Methionine metabolism | |
MAP00280 | Valine, leucine and isoleucine degradation | |
MAP00350 | Tyrosine metabolism | |
MAP00360 | Phenylalanine metabolism | |
MAP00380 | Tryptophan metabolism | |
MAP00400 | Phenylalanine, tyrosine and tryptophan biosynthesis | |
MAP00950 | Alkaloid biosynthesis I |
Compound table | |||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Cofactors | Substrates | Products | Intermediates | ||||||||||
KEGG-id | C00016 | C00001 | C00007 | C00151 | C00014 | C00027 | C00161 | ||||||
E.C. | |||||||||||||
Compound | FAD | H2O | O2 | L-Amino acid | NH3 | H2O2 | 2-Oxo acid | ||||||
Type | amide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carbohydrate,nucleotide | H2O | others | amino acids | amine group,organic ion | others | carbohydrate,carboxyl group | ||||||
ChEBI |
16238 16238 |
15377 15377 |
15379 26689 27140 15379 26689 27140 |
16134 16134 |
16240 16240 |
||||||||
PubChem |
643975 643975 |
22247451 962 22247451 962 |
977 977 |
222 222 |
22326046 784 22326046 784 |
||||||||
1f8rA01 | Unbound | Unbound | Unbound | Unbound | Unbound | Analogue:CIT | |||||||
1f8rB01 | Unbound | Unbound | Unbound | Unbound | Unbound | Analogue:CIT | |||||||
1f8rC01 | Unbound | Unbound | Unbound | Unbound | Unbound | Analogue:CIT | |||||||
1f8rD01 | Unbound | Unbound | Unbound | Unbound | Unbound | Analogue:CIT | |||||||
1f8sA01 | Unbound | Unbound | Analogue:BE2_1 | Unbound | Unbound | Unbound | |||||||
1f8sB01 | Unbound | Unbound | Analogue:BE2_4 | Unbound | Unbound | Unbound | |||||||
1f8sC01 | Unbound | Unbound | Analogue:BE2_7 | Unbound | Unbound | Unbound | |||||||
1f8sD01 | Unbound | Unbound | Analogue:BE2_10 | Unbound | Unbound | Unbound | |||||||
1f8sE01 | Unbound | Unbound | Analogue:BE2_13 | Unbound | Unbound | Unbound | |||||||
1f8sF01 | Unbound | Unbound | Analogue:BE2_16 | Unbound | Unbound | Unbound | |||||||
1f8sG01 | Unbound | Unbound | Analogue:BE2_19 | Unbound | Unbound | Unbound | |||||||
1f8sH01 | Unbound | Unbound | Analogue:BE2_22 | Unbound | Unbound | Unbound | |||||||
1tdkA01 | Unbound | Unbound | Bound:LVG_491 | Unbound | Unbound | Unbound | |||||||
1tdnA01 | Unbound | Unbound | Bound:LEU | Unbound | Unbound | Unbound | |||||||
1tdoA01 | Unbound | Unbound | Bound:PHE | Unbound | Unbound | Unbound | |||||||
1reoA01 | Unbound | Unbound | Unbound | Unbound | Unbound | Analogue:CIT | |||||||
1f8rA02 | Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | |||||||
1f8rB02 | Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | |||||||
1f8rC02 | Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | |||||||
1f8rD02 | Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | |||||||
1f8sA02 | Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | |||||||
1f8sB02 | Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | |||||||
1f8sC02 | Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | |||||||
1f8sD02 | Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | |||||||
1f8sE02 | Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | |||||||
1f8sF02 | Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | |||||||
1f8sG02 | Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | |||||||
1f8sH02 | Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | |||||||
1tdkA02 | Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | |||||||
1tdnA02 | Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | |||||||
1tdoA02 | Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | |||||||
1reoA02 | Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | |||||||
1f8rA03 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||||||
1f8rB03 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||||||
1f8rC03 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||||||
1f8rD03 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||||||
1f8sA03 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||||||
1f8sB03 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||||||
1f8sC03 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||||||
1f8sD03 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||||||
1f8sE03 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||||||
1f8sF03 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||||||
1f8sG03 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||||||
1f8sH03 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||||||
1tdkA03 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||||||
1tdnA03 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||||||
1tdoA03 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||||||
1reoA03 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
Reference for Active-site residues | ||
---|---|---|
resource | references | E.C. |
literature [5] |
Active-site residues | ||||||||||
---|---|---|---|---|---|---|---|---|---|---|
PDB | Catalytic residues | Cofactor-binding residues | Modified residues | Main-chain involved in catalysis | Comment | |||||
1f8rA01 | LYS 326 | |||||||||
1f8rB01 | LYS 326 | |||||||||
1f8rC01 | LYS 326 | |||||||||
1f8rD01 | LYS 326 | |||||||||
1f8sA01 | LYS 326 | |||||||||
1f8sB01 | LYS 326 | |||||||||
1f8sC01 | LYS 326 | |||||||||
1f8sD01 | LYS 326 | |||||||||
1f8sE01 | LYS 326 | |||||||||
1f8sF01 | LYS 326 | |||||||||
1f8sG01 | LYS 326 | |||||||||
1f8sH01 | LYS 326 | |||||||||
1tdkA01 | LYS 326 | |||||||||
1tdnA01 | LYS 326 | |||||||||
1tdoA01 | LYS 326 | |||||||||
1reoA01 | LYS 326 | |||||||||
1f8rA02 | ||||||||||
1f8rB02 | ||||||||||
1f8rC02 | ||||||||||
1f8rD02 | ||||||||||
1f8sA02 | ||||||||||
1f8sB02 | ||||||||||
1f8sC02 | ||||||||||
1f8sD02 | ||||||||||
1f8sE02 | ||||||||||
1f8sF02 | ||||||||||
1f8sG02 | ||||||||||
1f8sH02 | ||||||||||
1tdkA02 | ||||||||||
1tdnA02 | ||||||||||
1tdoA02 | ||||||||||
1reoA02 | ||||||||||
1f8rA03 | HIS 223 | |||||||||
1f8rB03 | HIS 223 | |||||||||
1f8rC03 | HIS 223 | |||||||||
1f8rD03 | HIS 223 | |||||||||
1f8sA03 | HIS 223 | |||||||||
1f8sB03 | HIS 223 | |||||||||
1f8sC03 | HIS 223 | |||||||||
1f8sD03 | HIS 223 | |||||||||
1f8sE03 | HIS 223 | |||||||||
1f8sF03 | HIS 223 | |||||||||
1f8sG03 | HIS 223 | |||||||||
1f8sH03 | HIS 223 | |||||||||
1tdkA03 | HIS 223 | |||||||||
1tdnA03 | HIS 223 | |||||||||
1tdoA03 | HIS 223 | |||||||||
1reoA03 | HIS 223 |
References for Catalytic Mechanism | ||
---|---|---|
References | Sections | No. of steps in catalysis |
[5]
|
Scheme 1, p.4212-4213 | 2 |
[7]
|
Scheme 1 | |
[8]
|
Scheme 1 | |
[11]
|
Fig.1, Fig.4, p.23975-23976 |
References | |
---|---|
[1] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 2044840 |
Journal | Int J Biochem |
Year | 1991 |
Volume | 23 |
Pages | 323-7 |
Authors | Tan NH, Saifuddin MN |
Title | Substrate specificity of king cobra (Ophiophagus hannah) venom L-amino acid oxidase. |
Related PDB | |
Related UniProtKB | |
[2] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 8755511 |
Journal | Proc Natl Acad Sci U S A |
Year | 1996 |
Volume | 93 |
Pages | 7546-51 |
Authors | Raibekas AA, Massey V |
Title | Glycerol-induced development of catalytically active conformation of Crotalus adamanteus L-amino acid oxidase in vitro. |
Related PDB | |
Related UniProtKB | |
[3] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 10441379 |
Journal | Arch Biochem Biophys |
Year | 1999 |
Volume | 368 |
Pages | 285-90 |
Authors | Souza DH, Eugenio LM, Fletcher JE, Jiang MS, Garratt RC, Oliva G, Selistre-de-Araujo HS |
Title | Isolation and structural characterization of a cytotoxic L-amino acid oxidase from Agkistrodon contortrix laticinctus snake venom: preliminary crystallographic data. |
Related PDB | |
Related UniProtKB | |
[4] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 11368308 |
Journal | Arch Biochem Biophys |
Year | 2000 |
Volume | 384 |
Pages | 216-26 |
Authors | Ali SA, Stoeva S, Abbasi A, Alam JM, Kayed R, Faigle M, Neumeister B, Voelter W |
Title |
Isolation, |
Related PDB | |
Related UniProtKB | |
[5] | |
Resource | |
Comments |
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), |
Medline ID | 20402326 |
PubMed ID | 10944103 |
Journal | EMBO J |
Year | 2000 |
Volume | 19 |
Pages | 4204-15 |
Authors | Pawelek PD, Cheah J, Coulombe R, Macheroux P, Ghisla S, Vrielink A |
Title | The structure of L-amino acid oxidase reveals the substrate trajectory into an enantiomerically conserved active site. |
Related PDB | 1f8r 1f8s |
Related UniProtKB | P81382 |
[6] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 11341935 |
Journal | Biochim Biophys Acta |
Year | 2001 |
Volume | 1544 |
Pages | 267-77 |
Authors | Takatsuka H, Sakurai Y, Yoshioka A, Kokubo T, Usami Y, Suzuki M, Matsui T, Titani K, Yagi H, Matsumoto M, Fujimura Y |
Title | Molecular characterization of L-amino acid oxidase from Agkistrodon halys blomhoffii with special reference to platelet aggregation. |
Related PDB | |
Related UniProtKB | |
[7] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 11453999 |
Journal | Eur J Biochem |
Year | 2001 |
Volume | 268 |
Pages | 4044-53 |
Authors | Geyer A, Fitzpatrick TB, Pawelek PD, Kitzing K, Vrielink A, Ghisla S, Macheroux P |
Title | Structure and characterization of the glycan moiety of L-amino-acid oxidase from the Malayan pit viper Calloselasma rhodostoma. |
Related PDB | |
Related UniProtKB | |
[8] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 11248687 |
Journal | Eur J Biochem |
Year | 2001 |
Volume | 268 |
Pages | 1679-86 |
Authors | MacHeroux P, Seth O, Bollschweiler C, Schwarz M, Kurfurst M, Au LC, Ghisla S |
Title |
L-amino-acid oxidase from the Malayan pit viper Calloselasma rhodostoma. |
Related PDB | |
Related UniProtKB | |
[9] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 12031486 |
Journal | Biochim Biophys Acta |
Year | 2002 |
Volume | 1576 |
Pages | 70-80 |
Authors | Chavan SS, Tian W, Hsueh K, Jawaheer D, Gregersen PK, Chu CC |
Title | Characterization of the human homolog of the IL-4 induced gene-1 (Fig1). |
Related PDB | |
Related UniProtKB | |
[10] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | |
Journal | Enzyme Microb Technol |
Year | 2002 |
Volume | 31 |
Pages | 77-87 |
Authors | Geueke B, Hummel W |
Title | A new bacterial L-amino acid oxidase with a broad substrate specificity: purification and characterization. |
Related PDB | |
Related UniProtKB | |
[11] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 12015330 |
Journal | J Biol Chem |
Year | 2002 |
Volume | 277 |
Pages | 23973-6 |
Authors | Binda C, Mattevi A, Edmondson DE |
Title | Structure-function relationships in flavoenzyme-dependent amine oxidations: a comparison of polyamine oxidase and monoamine oxidase. |
Related PDB | |
Related UniProtKB | |
[12] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 12175601 |
Journal | Toxicon |
Year | 2002 |
Volume | 40 |
Pages | 659-65 |
Authors | Du XY, Clemetson KJ |
Title | Snake venom L-amino acid oxidases. |
Related PDB | |
Related UniProtKB | |
[13] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 14636049 |
Journal | Biochemistry |
Year | 2003 |
Volume | 42 |
Pages | 13826-32 |
Authors | Sobrado P, Fitzpatrick PF |
Title |
Analysis of the role of the active site residue Arg98 in the flavoprotein tryptophan 2-monooxygenase, |
Related PDB | |
Related UniProtKB | |
[14] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 15103157 |
Journal | Acta Crystallogr D Biol Crystallogr |
Year | 2004 |
Volume | 60 |
Pages | 974-7 |
Authors | Zhang H, Teng M, Niu L, Wang Y, Wang Y, Liu Q, Huang Q, Hao Q, Dong Y, Liu P |
Title |
Purification, |
Related PDB | 1tdk 1tdn 1tdo 1reo |
Related UniProtKB |
Comments |
---|
This enzyme catalyzes three distinct reactions (see [7], (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 |
Created | Updated |
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2004-06-18 | 2009-02-26 |