DB code: M00103

CATH domain 3.30.457.10 : Copper Amine Oxidase; Chain A, domain 1
3.10.450.40 : Nuclear Transport Factor 2; Chain
2.70.98.20 : Beta-galactosidase; Chain A, domain 5 Catalytic domain
3.10.450.40 : Nuclear Transport Factor 2; Chain
E.C. 1.4.3.21
CSA 1oac
M-CSA 1oac
MACiE

CATH domain Related DB codes (homologues)
2.70.98.20 : Beta-galactosidase; Chain A, domain 5 M00202 T00206 T00250 T00251
3.10.450.40 : Nuclear Transport Factor 2; Chain M00202 T00206 T00250 T00251

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq Pfam
P46883 Primary amine oxidase
EC 1.4.3.21
Copper amine oxidase
Tyramine oxidase
2-phenylethylamine oxidase
NP_415904.3 (Protein)
NC_000913.2 (DNA/RNA sequence)
YP_489655.1 (Protein)
NC_007779.1 (DNA/RNA sequence)
PF01179 (Cu_amine_oxid)
PF07833 (Cu_amine_oxidN1)
PF02727 (Cu_amine_oxidN2)
PF02728 (Cu_amine_oxidN3)
[Graphical View]

KEGG enzyme name
primary-amine oxidase
amine oxidase (ambiguous)
amine oxidase (copper-containing)
amine oxidase (pyridoxal containing) (incorrect)
benzylamine oxidase (incorrect)
CAO (ambiguous)
copper amine oxidase (ambiguous)
Cu-amine oxidase (ambiguous)
Cu-containing amine oxidase (ambiguous)
diamine oxidase (incorrect)
diamino oxhydrase (incorrect)
histamine deaminase (ambiguous)
histamine oxidase (ambiguous)
monoamine oxidase (ambiguous)
plasma monoamine oxidase (ambiguous)
polyamine oxidase (ambiguous)
semicarbazide-sensitive amine oxidase (ambiguous)
SSAO (ambiguous)

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P46883 AMO_ECOLI RCH(2)NH(2) + H(2)O + O(2) = RCHO + NH(3) + H(2)O(2). 2-phenylethylamine + H(2)O + O(2) = phenylacetaldehyde + NH(3) + H(2)O(2). Homodimer. Periplasm. Binds 1 copper ion per subunit. Binds 2 calcium ions per subunit. Contains 1 topaquinone per subunit.

KEGG Pathways
Map code Pathways E.C.
MAP00260 Glycine, serine and threonine metabolism
MAP00350 Tyrosine metabolism
MAP00360 Phenylalanine metabolism
MAP00410 beta-Alanine metabolism
MAP00960 Alkaloid biosynthesis II

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C00070 C00076 L00003 C00375 C00001 C00007 C00071 C00014 C00027 I00021 I00022 I00023 I00024
E.C.
Compound Copper Calcium Topaquinone RCH2NH2 H2O Oxygen Aldehyde NH3 H2O2 Substrate Schiff-base (Iminoquinone=substrate) Carbanionic intermediate Product Schiff-base (Aminoquinol=product) Aminoquinol/Semiquinone Iminoquinone
Type heavy metal divalent metal (Ca2+, Mg2+) amino acids,aromatic ring (only carbon atom) amine group H2O others carbohydrate amine group,organic ion others
ChEBI 28694
30052
28694
30052
29108
29108
36077
68431
36077
68431
15377
15377
15379
26689
27140
15379
26689
27140
16134
16134
16240
16240
PubChem 23978
23978
271
271
22247451
962
22247451
962
977
977
222
222
22326046
784
22326046
784
1d6uA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1d6uB01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1d6yA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1d6yB01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1d6zA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1d6zB01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1jrqA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1jrqB01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1lvnA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1lvnB01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1oacA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1oacB01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1spuA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1spuB01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1dyuA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1dyuB01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1qafA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1qafB01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1qakA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1qakB01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1qalA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1qalB01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1d6uA02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1d6uB02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1d6yA02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1d6yB02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1d6zA02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1d6zB02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1jrqA02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1jrqB02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1lvnA02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1lvnB02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1oacA02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1oacB02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1spuA02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1spuB02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1dyuA02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1dyuB02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1qafA02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1qafB02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1qakA02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1qakB02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1qalA02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1qalB02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1d6uA03 Bound:_CU Bound:2x_CA Analogue:TYQ_466 Unbound Unbound Bound:HY1 Unbound Unbound Unbound Unbound Unbound Intermediate-bound:TYQ_466 Unbound
1d6uB03 Bound:_CU Bound:2x_CA Analogue:TYQ_466 Unbound Unbound Bound:HY1 Unbound Unbound Unbound Unbound Unbound Intermediate-bound:TYQ_466 Unbound
1d6yA03 Bound:_CU Bound:2x_CA Analogue:TYQ_466 Unbound Analogue:_NO Bound:HY1 Unbound Unbound Unbound Unbound Unbound Intermediate-bound:TYQ_466 Unbound
1d6yB03 Bound:_CU Bound:2x_CA Analogue:TYQ_466 Unbound Analogue:_NO Bound:HY1 Unbound Unbound Unbound Unbound Unbound Intermediate-bound:TYQ_466 Unbound
1d6zA03 Bound:_CU Bound:2x_CA Analogue:TYY_466 Unbound Unbound Bound:HY1 Unbound Bound:PEO Unbound Unbound Unbound Unbound Intermediate-bound:TYY_466
1d6zB03 Bound:_CU Bound:2x_CA Analogue:TYY_466 Unbound Unbound Bound:HY1 Unbound Bound:PEO Unbound Unbound Unbound Unbound Intermediate-bound:TYY_466
1jrqA03 Bound:_CU Bound:2x_CA Bound:TPQ_466 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1jrqB03 Bound:_CU Bound:2x_CA Bound:TPQ_466 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1lvnA03 Bound:_CU Bound:2x_CA Analogue:TYT_466 Unbound Unbound Unbound Unbound Unbound Intermediate-analogue:TYT_466 Unbound Unbound Unbound Unbound
1lvnB03 Bound:_CU Bound:2x_CA Analogue:TYT_466 Unbound Unbound Unbound Unbound Unbound Intermediate-analogue:TYT_466 Unbound Unbound Unbound Unbound
1oacA03 Bound:_CU Bound:2x_CA Bound:TPQ_466 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1oacB03 Bound:_CU Bound:2x_CA Bound:TPQ_466 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1spuA03 Bound:_CU Bound:2x_CA Analogue:PAQ_466 Unbound Unbound Unbound Unbound Unbound Intermediate-analogue:PAQ_466 Unbound Unbound Unbound Unbound
1spuB03 Bound:_CU Bound:2x_CA Analogue:PAQ_466 Unbound Unbound Unbound Unbound Unbound Intermediate-analogue:PAQ_466 Unbound Unbound Unbound Unbound
1dyuA03 Bound:_CU Bound:2x_CA Bound:TPQ_466 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1dyuB03 Bound:_CU Bound:2x_CA Bound:TPQ_466 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1qafA03 Bound:_CU Bound:2x_CA Bound:TPQ_466 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1qafB03 Bound:_CU Bound:2x_CA Bound:TPQ_466 Analogue:GOL Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1qakA03 Bound:_CU Bound:2x_CA Bound:TPQ_466 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1qakB03 Bound:_CU Bound:2x_CA Bound:TPQ_466 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1qalA03 Bound:_CU Bound:2x_CA Bound:TPQ_466 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1qalB03 Bound:_CU Bound:2x_CA Bound:TPQ_466 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1d6uA04 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1d6uB04 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1d6yA04 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1d6yB04 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1d6zA04 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1d6zB04 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1jrqA04 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1jrqB04 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1lvnA04 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1lvnB04 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1oacA04 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1oacB04 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1spuA04 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1spuB04 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1dyuA04 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1dyuB04 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1qafA04 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1qafB04 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1qakA04 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1qakB04 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1qalA04 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1qalB04 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1d6uA01
1d6uB01
1d6yA01
1d6yB01
1d6zA01
1d6zB01
1jrqA01
1jrqB01
1lvnA01
1lvnB01
1oacA01
1oacB01
1spuA01
1spuB01
1dyuA01
1dyuB01
1qafA01
1qafB01
1qakA01
1qakB01
1qalA01
1qalB01
1d6uA02
1d6uB02
1d6yA02
1d6yB02
1d6zA02
1d6zB02
1jrqA02
1jrqB02
1lvnA02
1lvnB02
1oacA02
1oacB02
1spuA02
1spuB02
1dyuA02
1dyuB02
1qafA02
1qafB02
1qakA02
1qakB02
1qalA02
1qalB02
1d6uA03 TYR 369;ASP 383 HIS 524;HIS 526;HIS 689(Copper);ASP 533;LEU 534;ASP 535;ASP 678;ALA 679(Calcium-1);GLU 573;TYR 667;ASP 670;GLU 672(Calcium-2) TYQ 466(aminoquinol)
1d6uB03 TYR 369;ASP 383 HIS 524;HIS 526;HIS 689(Copper);ASP 533;LEU 534;ASP 535;ASP 678;ALA 679(Calcium-1);GLU 573;TYR 667;ASP 670;GLU 672(Calcium-2) TYQ 466(aminoquinol)
1d6yA03 TYR 369;ASP 383 HIS 524;HIS 526;HIS 689(Copper);ASP 533;LEU 534;ASP 535;ASP 678;ALA 679(Calcium-1);GLU 573;TYR 667;ASP 670;GLU 672(Calcium-2) TYQ 466(aminoquinol)
1d6yB03 TYR 369;ASP 383 HIS 524;HIS 526;HIS 689(Copper);ASP 533;LEU 534;ASP 535;ASP 678;ALA 679(Calcium-1);GLU 573;TYR 667;ASP 670;GLU 672(Calcium-2) TYQ 466(aminoquinol)
1d6zA03 TYR 369;ASP 383 HIS 524;HIS 526;HIS 689(Copper);ASP 533;LEU 534;ASP 535;ASP 678;ALA 679(Calcium-1);GLU 573;TYR 667;ASP 670;GLU 672(Calcium-2) TYY 466(iminoquinone)
1d6zB03 TYR 369;ASP 383 HIS 524;HIS 526;HIS 689(Copper);ASP 533;LEU 534;ASP 535;ASP 678;ALA 679(Calcium-1);GLU 573;TYR 667;ASP 670;GLU 672(Calcium-2) TYY 466(iminoquinone)
1jrqA03 ;ASP 383 HIS 524;HIS 526;HIS 689(Copper);ASP 533;LEU 534;ASP 535;ASP 678;ALA 679(Calcium-1);GLU 573;TYR 667;ASP 670;GLU 672(Calcium-2) TPQ 466(topaquinone) mutant Y369F
1jrqB03 ;ASP 383 HIS 524;HIS 526;HIS 689(Copper);ASP 533;LEU 534;ASP 535;ASP 678;ALA 679(Calcium-1);GLU 573;TYR 667;ASP 670;GLU 672(Calcium-2) TPQ 466(topaquinone) mutant Y369F
1lvnA03 TYR 369;ASP 383 HIS 524;HIS 526;HIS 689(Copper);ASP 533;LEU 534;ASP 535;ASP 678;ALA 679(Calcium-1);GLU 573;TYR 667;ASP 670;GLU 672(Calcium-2) TYT 466(iminoquinone-substrate analogue)
1lvnB03 TYR 369;ASP 383 HIS 524;HIS 526;HIS 689(Copper);ASP 533;LEU 534;ASP 535;ASP 678;ALA 679(Calcium-1);GLU 573;TYR 667;ASP 670;GLU 672(Calcium-2) TYT 466(iminoquinone-substrate analogue)
1oacA03 TYR 369;ASP 383 HIS 524;HIS 526;HIS 689(Copper);ASP 533;LEU 534;ASP 535;ASP 678;ALA 679(Calcium-1);GLU 573;TYR 667;ASP 670;GLU 672(Calcium-2) TPQ 466(topaquinone)
1oacB03 TYR 369;ASP 383 HIS 524;HIS 526;HIS 689(Copper);ASP 533;LEU 534;ASP 535;ASP 678;ALA 679(Calcium-1);GLU 573;TYR 667;ASP 670;GLU 672(Calcium-2) TPQ 466(topaquinone)
1spuA03 TYR 369;ASP 383 HIS 524;HIS 526;HIS 689(Copper);ASP 533;LEU 534;ASP 535;ASP 678;ALA 679(Calcium-1);GLU 573;TYR 667;ASP 670;GLU 672(Calcium-2) PAQ 466(2-oxy-4-hydroxy-5-(2-hydrazinopyridine)phenylalanine)
1spuB03 TYR 369;ASP 383 HIS 524;HIS 526;HIS 689(Copper);ASP 533;LEU 534;ASP 535;ASP 678;ALA 679(Calcium-1);GLU 573;TYR 667;ASP 670;GLU 672(Calcium-2) PAQ 466(2-oxy-4-hydroxy-5-(2-hydrazinopyridine)phenylalanine)
1dyuA03 TYR 369;ASP 383 HIS 524;HIS 526;HIS 689(Copper);ASP 533;LEU 534;ASP 535;ASP 678;ALA 679(Calcium-1);GLU 573;TYR 667;ASP 670;GLU 672(Calcium-2) TYR 466(topaquinone)
1dyuB03 TYR 369;ASP 383 HIS 524;HIS 526;HIS 689(Copper);ASP 533;LEU 534;ASP 535;ASP 678;ALA 679(Calcium-1);GLU 573;TYR 667;ASP 670;GLU 672(Calcium-2) TYR 466(topaquinone)
1qafA03 TYR 369; HIS 524;HIS 526;HIS 689(Copper);ASP 533;LEU 534;ASP 535;ASP 678;ALA 679(Calcium-1);GLU 573;TYR 667;ASP 670;GLU 672(Calcium-2) TPQ 466(topaquinone) mutant D383E
1qafB03 TYR 369; HIS 524;HIS 526;HIS 689(Copper);ASP 533;LEU 534;ASP 535;ASP 678;ALA 679(Calcium-1);GLU 573;TYR 667;ASP 670;GLU 672(Calcium-2) TPQ 466(topaquinone) mutant D383E
1qakA03 TYR 369; HIS 524;HIS 526;HIS 689(Copper);ASP 533;LEU 534;ASP 535;ASP 678;ALA 679(Calcium-1);GLU 573;TYR 667;ASP 670;GLU 672(Calcium-2) TPQ 466(topaquinone) mutant D383A
1qakB03 TYR 369; HIS 524;HIS 526;HIS 689(Copper);ASP 533;LEU 534;ASP 535;ASP 678;ALA 679(Calcium-1);GLU 573;TYR 667;ASP 670;GLU 672(Calcium-2) TPQ 466(topaquinone) mutant D383A
1qalA03 TYR 369; HIS 524;HIS 526;HIS 689(Copper);ASP 533;LEU 534;ASP 535;ASP 678;ALA 679(Calcium-1);GLU 573;TYR 667;ASP 670;GLU 672(Calcium-2) TPQ 466(topaquinone) mutant D383N
1qalB03 TYR 369; HIS 524;HIS 526;HIS 689(Copper);ASP 533;LEU 534;ASP 535;ASP 678;ALA 679(Calcium-1);GLU 573;TYR 667;ASP 670;GLU 672(Calcium-2) TPQ 466(topaquinone) mutant D383N
1d6uA04
1d6uB04
1d6yA04
1d6yB04
1d6zA04
1d6zB04
1jrqA04
1jrqB04
1lvnA04
1lvnB04
1oacA04
1oacB04
1spuA04
1spuB04
1dyuA04
1dyuB04
1qafA04
1qafB04
1qakA04
1qakB04
1qalA04
1qalB04

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[5]
Scheme II, p.60-62
[6]
Fig. 1, p.1128-1129
[7]
Fig.1, p.1178-1179
[9]
Scheme 1, p.5586-5588
[10]
Fig.2, Fig.10, p.1617-1619
[11]
Scheme 23, Scheme 24, p.746-747
[12]
Fig.1, p.8224-8226
[13]
Fig.2, p.1725-1728
[15]
Fig.2, p.12814-12817
[17]
Scheme 1, Fig.1, p.4694-4605
[18]
Scheme 1, p.814-815
[21]
Fig.4, Fig.6, p.313-315
[22]
Scheme 1, Fig.1, p.494-496
[23]
Scheme 2

References
[1]
Resource
Comments
Medline ID
PubMed ID 8155661
Journal Biochemistry
Year 1994
Volume 33
Pages 4425-31
Authors Bossa M, Morpurgo GO, Morpurgo L
Title Models and molecular orbital semiempirical calculations in the study of the spectroscopic properties of bovine serum amine oxidase quinone cofactor.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 8176752
Journal J Mol Biol
Year 1994
Volume 238
Pages 635-7
Authors Roh JH, Suzuki H, Kumagai H, Yamashita M, Azakami H, Murooka Y, Mikami B
Title Crystallization and preliminary X-ray analysis of copper amine oxidase from Escherichia coli K-12.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 8585612
Journal Anal Biochem
Year 1995
Volume 230
Pages 159-66
Authors Steinebach V, Groen BW, Wijmenga SS, Niessen WM, Jongejan JA, Duine JA
Title Identification of topaquinone, as illustrated for pig kidney diamine oxidase and Escherichia coli amine oxidase.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 7766611
Journal Biochemistry
Year 1995
Volume 34
Pages 7020-6
Authors Moenne-Loccoz P, Nakamura N, Steinebach V, Duine JA, Mure M, Klinman JP, Sanders-Loehr J
Title Characterization of the topa quinone cofactor in amine oxidase from Escherichia coli by resonance Raman spectroscopy.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 8524164
Journal Methods Enzymol
Year 1995
Volume 258
Pages 53-69
Authors Sayre LM, Lee Y
Title Catalytic aerobic deamination of activated primary amines by a model for the quinone cofactor of mammalian copper amine oxidases.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 8591022
Journal Structure
Year 1995
Volume 3
Pages 1127-9
Authors Fontecave M, Eklund H
Title Copper amine oxidase: a novel use for a tyrosine.
Related PDB
Related UniProtKB
[7]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 8591028
Journal Structure
Year 1995
Volume 3
Pages 1171-84
Authors Parsons MR, Convery MA, Wilmot CM, Yadav KD, Blakeley V, Corner AS, Phillips SE, McPherson MJ, Knowles PF
Title Crystal structure of a quinoenzyme: copper amine oxidase of Escherichia coli at 2 A resolution.
Related PDB 1oac
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 8706668
Journal Eur J Biochem
Year 1996
Volume 238
Pages 683-9
Authors Steinebach V, De Jong GA, Wijmenga SS, De Vries S, Duine JA
Title The copper-topaquinone-phenylhydrazine-adduct geometry in Escherichia coli amine oxidase derivatized with phenylhydrazines substituted with 19F-NMR relaxation measurements.
Related PDB
Related UniProtKB
[9]
Resource
Comments
Medline ID
PubMed ID 8621418
Journal J Biol Chem
Year 1996
Volume 271
Pages 5580-8
Authors Steinebach V, de Vries S, Duine JA
Title Intermediates in the catalytic cycle of copper-quinoprotein amine oxidase from Escherichia coli.
Related PDB
Related UniProtKB
[10]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS)
Medline ID 97200715
PubMed ID 9048544
Journal Biochemistry
Year 1997
Volume 36
Pages 1608-20
Authors Wilmot CM, Murray JM, Alton G, Parsons MR, Convery MA, Blakeley V, Corner AS, Palcic MM, Knowles PF, McPherson MJ, Phillips SE
Title Catalytic mechanism of the quinoenzyme amine oxidase from Escherichia coli: exploring the reductive half-reaction.
Related PDB 1spu
Related UniProtKB P46883
[11]
Resource
Comments
Medline ID
PubMed ID 11848913
Journal Chem Rev
Year 1998
Volume 98
Pages 705-762
Authors Stubbe J, van Der Donk WA
Title Protein Radicals in Enzyme Catalysis.
Related PDB
Related UniProtKB
[12]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS)
Medline ID 99315198
PubMed ID 10387067
Journal Biochemistry
Year 1999
Volume 38
Pages 8217-27
Authors Murray JM, Saysell CG, Wilmot CM, Tambyrajah WS, Jaeger J, Knowles PF, Phillips SE, McPherson MJ
Title The active site base controls cofactor reactivity in Escherichia coli amine oxidase: x-ray crystallographic studies with mutational variants.
Related PDB
Related UniProtKB P46883
[13]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS)
Medline ID 20045000
PubMed ID 10576737
Journal Science
Year 1999
Volume 286
Pages 1724-8
Authors Wilmot CM, Hajdu J, McPherson MJ, Knowles PF, Phillips SE
Title Visualization of dioxygen bound to copper during enzyme catalysis.
Related PDB 1d6u 1d6y 1d6z
Related UniProtKB P46883
[14]
Resource
Comments
Medline ID
PubMed ID 11665487
Journal Adv Protein Chem
Year 2001
Volume 58
Pages 141-74
Authors Dove JE, Klinman JP
Title Trihydroxyphenylalanine quinone (TPQ) from copper amine oxidases and lysyl tyrosylquinone (LTQ) from lysyl oxidase.
Related PDB
Related UniProtKB
[15]
Resource
Comments
Medline ID
PubMed ID 11669617
Journal Biochemistry
Year 2001
Volume 40
Pages 12808-18
Authors Murray JM, Kurtis CR, Tambyrajah W, Saysell CG, Wilmot CM, Parsons MR, Phillips SE, Knowles PF, McPherson MJ
Title Conserved tyrosine-369 in the active site of Escherichia coli copper amine oxidase is not essential.
Related PDB 1jrq
Related UniProtKB
[16]
Resource
Comments
Medline ID
PubMed ID 11751046
Journal Curr Opin Struct Biol
Year 2001
Volume 11
Pages 666-73
Authors Dawkes HC, Phillips SE
Title Copper amine oxidase: cunning cofactor and controversial copper.
Related PDB
Related UniProtKB
[17]
Resource
Comments
Medline ID
PubMed ID 11532005
Journal Eur J Biochem
Year 2001
Volume 268
Pages 4686-97
Authors Padiglia A, Medda R, Lorrai A, Paci M, Pedersen JZ, Boffi A, Bellelli A, Agro AF, Floris G
Title Irreversible inhibition of pig kidney copper-containing amine oxidase by sodium and lithium ions.
Related PDB
Related UniProtKB
[18]
Resource
Comments
Medline ID
PubMed ID 11985492
Journal Biochem J
Year 2002
Volume 365
Pages 809-16
Authors Saysell CG, Tambyrajah WS, Murray JM, Wilmot CM, Phillips SE, McPherson MJ, Knowles PF
Title Probing the catalytic mechanism of Escherichia coli amine oxidase using mutational variants and a reversible inhibitor as a substrate analogue.
Related PDB
Related UniProtKB
[19]
Resource
Comments
Medline ID
PubMed ID 11781110
Journal Biochemistry
Year 2002
Volume 41
Pages 687-96
Authors Green EL, Nakamura N, Dooley DM, Klinman JP, Sanders-Loehr J
Title Rates of oxygen and hydrogen exchange as indicators of TPQ cofactor orientation in amine oxidases.
Related PDB
Related UniProtKB
[20]
Resource
Comments
Medline ID
PubMed ID 12153561
Journal Eur J Biochem
Year 2002
Volume 269
Pages 3645-58
Authors Shepard EM, Smith J, Elmore BO, Kuchar JA, Sayre LM, Dooley DM
Title Towards the development of selective amine oxidase inhibitors. Mechanism-based inhibition of six copper containing amine oxidases.
Related PDB
Related UniProtKB
[21]
Resource
Comments
Medline ID
PubMed ID 12078505
Journal Methods Enzymol
Year 2002
Volume 353
Pages 301-18
Authors Wilmot CM, Sjogren T, Carlsson GH, Berglund GI, Hajdu J
Title Defining redox state of X-ray crystal structures by single-crystal ultraviolet-visible microspectrophotometry.
Related PDB
Related UniProtKB
[22]
Resource
Comments
Medline ID
PubMed ID 12773142
Journal Biochem Soc Trans
Year 2003
Volume 31
Pages 493-6
Authors Wilmot CM
Title Oxygen activation in a copper-containing amine oxidase.
Related PDB
Related UniProtKB
[23]
Resource
Comments
Medline ID
PubMed ID 15234266
Journal Arch Biochem Biophys
Year 2004
Volume 428
Pages 22-31
Authors Brazeau BJ, Johnson BJ, Wilmot CM
Title Copper-containing amine oxidases. Biogenesis and catalysis; a structural perspective.
Related PDB
Related UniProtKB
[24]
Resource
Comments
Medline ID
PubMed ID 15498552
Journal FEBS Lett
Year 2004
Volume 576
Pages 301-5
Authors Wilmot CM, Saysell CG, Blessington A, Conn DA, Kurtis CR, McPherson MJ, Knowles PF, Phillips SE
Title Medical implications from the crystal structure of a copper-containing amine oxidase complexed with the antidepressant drug tranylcypromine.
Related PDB 1lvn
Related UniProtKB
[25]
Resource
Comments
Medline ID
PubMed ID 15369390
Journal J Med Chem
Year 2004
Volume 47
Pages 4865-74
Authors Marti L, Abella A, De La Cruz X, Garcia-Vicente S, Unzeta M, Carpene C, Palacin M, Testar X, Orozco M, Zorzano A
Title Exploring the binding mode of semicarbazide-sensitive amine oxidase/VAP-1: identification of novel substrates with insulin-like activity.
Related PDB
Related UniProtKB

Comments
Cofactor, topaquinone (2,4,5-trihydroxyphenylalanine), is a modified residue, generated from active site tyrosine residue (Tyr466) by self-catalysis (see [6]).
Although this enzyme binds a copper ion and two calcium ions as cofactors per subunit, the calcium ions are not involved in catalysis.
The following compounds can be inculded as substrate and product, respectively:
Phenethylamine;C05332
Phenylacetaldehyde;C00601
According to the literature [13], this enzyme catalyzes two half-reactions: (I) reductive half-reaction, and (II) oxidative half-reaction. These half-reactions can be subdivided into several basic reactions in terms of RLCP classification.
(I) Reductive half-reaction:
(A) Exchange of double-bonded atoms; Schiff-base formation; Substrate amine forms a Schiff-base with topaquinone, generating iminoquinone=substrate and H2O (dehydration):
(B) Isomerization from iminoquinone=substrate complex to aminoquinol=product complex:
(C) Exchange of double-bonded atoms; Schiff-base deformation; H2O reacts with the intermediate, generating aminoquinol and product aldehyde (hydration):
(II) Oxidative half-reaction:
(D) Reduction of dioxygen (O2) by aminoquinol, to produce hydrogen peroxide (H2O2) and iminoquinone (Hydride transfer):
(E) Exchange of double-bonded atoms; Schiff-base deformation; H2O reacts with the intermediate, generating topaquinone and product ammonia (hydration):

Created Updated
2005-05-26 2009-02-26