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 |
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| PubChem |
643975 643975 |
22247451 962 22247451 962 |
977 977 |
222 222 |
22326046 784 22326046 784 |
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| 1f8rA01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Analogue:CIT | ||
| 1f8rB01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Analogue:CIT | ||
| 1f8rC01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Analogue:CIT | ||
| 1f8rD01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Analogue:CIT | ||
| 1f8sA01 |
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Unbound | Unbound | Analogue:BE2_1 | Unbound | Unbound | Unbound | ||
| 1f8sB01 |
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Unbound | Unbound | Analogue:BE2_4 | Unbound | Unbound | Unbound | ||
| 1f8sC01 |
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Unbound | Unbound | Analogue:BE2_7 | Unbound | Unbound | Unbound | ||
| 1f8sD01 |
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Unbound | Unbound | Analogue:BE2_10 | Unbound | Unbound | Unbound | ||
| 1f8sE01 |
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Unbound | Unbound | Analogue:BE2_13 | Unbound | Unbound | Unbound | ||
| 1f8sF01 |
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Unbound | Unbound | Analogue:BE2_16 | Unbound | Unbound | Unbound | ||
| 1f8sG01 |
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Unbound | Unbound | Analogue:BE2_19 | Unbound | Unbound | Unbound | ||
| 1f8sH01 |
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Unbound | Unbound | Analogue:BE2_22 | Unbound | Unbound | Unbound | ||
| 1tdkA01 |
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Unbound | Unbound | Bound:LVG_491 | Unbound | Unbound | Unbound | ||
| 1tdnA01 |
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Unbound | Unbound | Bound:LEU | Unbound | Unbound | Unbound | ||
| 1tdoA01 |
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Unbound | Unbound | Bound:PHE | Unbound | Unbound | Unbound | ||
| 1reoA01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Analogue:CIT | ||
| 1f8rA02 |
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Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1f8rB02 |
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Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1f8rC02 |
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Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1f8rD02 |
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Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1f8sA02 |
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Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1f8sB02 |
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Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1f8sC02 |
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Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1f8sD02 |
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Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1f8sE02 |
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Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1f8sF02 |
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Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1f8sG02 |
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Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1f8sH02 |
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Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1tdkA02 |
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Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1tdnA02 |
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Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1tdoA02 |
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Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1reoA02 |
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Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1f8rA03 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1f8rB03 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1f8rC03 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1f8rD03 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1f8sA03 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1f8sB03 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1f8sC03 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1f8sD03 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1f8sE03 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1f8sF03 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1f8sG03 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1f8sH03 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1tdkA03 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1tdnA03 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1tdoA03 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1reoA03 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| Reference for Active-site residues | ||
|---|---|---|
| resource | references | E.C. |
| literature [5] | ||
| Active-site residues | ||||||||||
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| PDB | Catalytic residues | Cofactor-binding residues | Modified residues | Main-chain involved in catalysis | Comment | |||||
| 1f8rA01 |
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LYS 326 | ||||
| 1f8rB01 |
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LYS 326 | ||||
| 1f8rC01 |
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LYS 326 | ||||
| 1f8rD01 |
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LYS 326 | ||||
| 1f8sA01 |
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LYS 326 | ||||
| 1f8sB01 |
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LYS 326 | ||||
| 1f8sC01 |
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LYS 326 | ||||
| 1f8sD01 |
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LYS 326 | ||||
| 1f8sE01 |
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LYS 326 | ||||
| 1f8sF01 |
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LYS 326 | ||||
| 1f8sG01 |
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LYS 326 | ||||
| 1f8sH01 |
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LYS 326 | ||||
| 1tdkA01 |
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LYS 326 | ||||
| 1tdnA01 |
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LYS 326 | ||||
| 1tdoA01 |
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LYS 326 | ||||
| 1reoA01 |
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LYS 326 | ||||
| 1f8rA02 |
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| 1f8rB02 |
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| 1f8rC02 |
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| 1f8rD02 |
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| 1f8sA02 |
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| 1f8sB02 |
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| 1f8sC02 |
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| 1f8sD02 |
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| 1f8sE02 |
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| 1f8sF02 |
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| 1f8sG02 |
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| 1f8sH02 |
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| 1tdkA02 |
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| 1tdnA02 |
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| 1tdoA02 |
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| 1reoA02 |
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| 1f8rA03 |
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HIS 223 | ||||
| 1f8rB03 |
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HIS 223 | ||||
| 1f8rC03 |
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HIS 223 | ||||
| 1f8rD03 |
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HIS 223 | ||||
| 1f8sA03 |
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HIS 223 | ||||
| 1f8sB03 |
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HIS 223 | ||||
| 1f8sC03 |
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HIS 223 | ||||
| 1f8sD03 |
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HIS 223 | ||||
| 1f8sE03 |
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HIS 223 | ||||
| 1f8sF03 |
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HIS 223 | ||||
| 1f8sG03 |
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HIS 223 | ||||
| 1f8sH03 |
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HIS 223 | ||||
| 1tdkA03 |
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HIS 223 | ||||
| 1tdnA03 |
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HIS 223 | ||||
| 1tdoA03 |
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HIS 223 | ||||
| 1reoA03 |
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HIS 223 | ||||
| References for Catalytic Mechanism | ||
|---|---|---|
| References | Sections | No. of steps in catalysis |
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[5]
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Scheme 1, p.4212-4213 | 2 |
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[7]
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Scheme 1 | |
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[8]
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Scheme 1 | |
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[11]
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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 |
|---|---|
| 2004-06-18 | 2009-02-26 |