EzCatDB: M00103

DB codeM00103
CATH domainDomain 13.30.457.10
Domain 23.10.450.40
Domain 32.70.98.20Catalytic domain
Domain 43.10.450.40
E.C.1.4.3.21
CSA1oac

CATH domainRelated DB codes (homologues)
2.70.98.20M00202,T00206,T00250,T00251
3.10.450.40M00202,T00206,T00250,T00251

Enzyme Name
Swiss-protKEGG

P46883
Protein namePrimary amine oxidaseprimary-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)
SynonymsEC 1.4.3.21
Copper amine oxidase
Tyramine oxidase
2-phenylethylamine oxidase

KEGG pathways
MAP codePathways
MAP00260Glycine, serine and threonine metabolism
MAP00350Tyrosine metabolism
MAP00360Phenylalanine metabolism
MAP00410beta-Alanine metabolism
MAP00960Alkaloid biosynthesis II

Swiss-prot:Accession NumberP46883
Entry nameAMO_ECOLI
ActivityRCH(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).
SubunitHomodimer.
Subcellular locationPeriplasm.
CofactorBinds 1 copper ion per subunit.,Binds 2 calcium ions per subunit.,Contains 1 topaquinone per subunit.


CofactorsSubstratesProductsintermediates
KEGG-idC00070C00076L00003C00375C00001C00007C00071C00014C00027I00021
I00022I00023I00024
CompoundCopperCalciumTopaquinoneRCH2NH2H2OOxygenAldehydeNH3H2O2Substrate Schiff-base (Iminoquinone=substrate)Carbanionic intermediateProduct Schiff-base (Aminoquinol=product)Aminoquinol/SemiquinoneIminoquinone
Typeheavy metaldivalent metal (Ca2+, Mg2+)amino acids,aromatic ring (only carbon atom)amine groupH2Ootherscarbohydrateamine group,organic ionothers




1d6uA01UnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1d6uB01UnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1d6yA01UnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1d6yB01UnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1d6zA01UnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1d6zB01UnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1jrqA01UnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1jrqB01UnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1lvnA01UnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1lvnB01UnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1oacA01UnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1oacB01UnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1spuA01UnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1spuB01UnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1dyuA01UnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1dyuB01UnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1qafA01UnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1qafB01UnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1qakA01UnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1qakB01UnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1qalA01UnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1qalB01UnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1d6uA02UnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1d6uB02UnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1d6yA02UnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1d6yB02UnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1d6zA02UnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1d6zB02UnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1jrqA02UnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1jrqB02UnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1lvnA02UnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1lvnB02UnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1oacA02UnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1oacB02UnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1spuA02UnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1spuB02UnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1dyuA02UnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1dyuB02UnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1qafA02UnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1qafB02UnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1qakA02UnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1qakB02UnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1qalA02UnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1qalB02UnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1d6uA03Bound:_CUBound:2x_CAAnalogue:TYQ 466Unbound
UnboundBound:HY1UnboundUnboundUnboundUnboundUnboundIntermediate-bound:TYQ 466Unbound
1d6uB03Bound:_CUBound:2x_CAAnalogue:TYQ 466Unbound
UnboundBound:HY1UnboundUnboundUnboundUnboundUnboundIntermediate-bound:TYQ 466Unbound
1d6yA03Bound:_CUBound:2x_CAAnalogue:TYQ 466Unbound
Analogue:_NOBound:HY1UnboundUnboundUnboundUnboundUnboundIntermediate-bound:TYQ 466Unbound
1d6yB03Bound:_CUBound:2x_CAAnalogue:TYQ 466Unbound
Analogue:_NOBound:HY1UnboundUnboundUnboundUnboundUnboundIntermediate-bound:TYQ 466Unbound
1d6zA03Bound:_CUBound:2x_CAAnalogue:TYY 466Unbound
UnboundBound:HY1UnboundBound:PEOUnboundUnboundUnboundUnboundIntermediate-bound:TYY 466
1d6zB03Bound:_CUBound:2x_CAAnalogue:TYY 466Unbound
UnboundBound:HY1UnboundBound:PEOUnboundUnboundUnboundUnboundIntermediate-bound:TYY 466
1jrqA03Bound:_CUBound:2x_CABound:TPQ 466Unbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1jrqB03Bound:_CUBound:2x_CABound:TPQ 466Unbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1lvnA03Bound:_CUBound:2x_CAAnalogue:TYT 466Unbound
UnboundUnboundUnboundUnboundIntermediate-analogue:TYT 466UnboundUnboundUnboundUnbound
1lvnB03Bound:_CUBound:2x_CAAnalogue:TYT 466Unbound
UnboundUnboundUnboundUnboundIntermediate-analogue:TYT 466UnboundUnboundUnboundUnbound
1oacA03Bound:_CUBound:2x_CABound:TPQ 466Unbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1oacB03Bound:_CUBound:2x_CABound:TPQ 466Unbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1spuA03Bound:_CUBound:2x_CAAnalogue:PAQ 466Unbound
UnboundUnboundUnboundUnboundIntermediate-analogue:PAQ 466UnboundUnboundUnboundUnbound
1spuB03Bound:_CUBound:2x_CAAnalogue:PAQ 466Unbound
UnboundUnboundUnboundUnboundIntermediate-analogue:PAQ 466UnboundUnboundUnboundUnbound
1dyuA03Bound:_CUBound:2x_CABound:TPQ 466Unbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1dyuB03Bound:_CUBound:2x_CABound:TPQ 466Unbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1qafA03Bound:_CUBound:2x_CABound:TPQ 466Unbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1qafB03Bound:_CUBound:2x_CABound:TPQ 466Analogue:GOL
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1qakA03Bound:_CUBound:2x_CABound:TPQ 466Unbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1qakB03Bound:_CUBound:2x_CABound:TPQ 466Unbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1qalA03Bound:_CUBound:2x_CABound:TPQ 466Unbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1qalB03Bound:_CUBound:2x_CABound:TPQ 466Unbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1d6uA04UnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1d6uB04UnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1d6yA04UnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1d6yB04UnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1d6zA04UnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1d6zB04UnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1jrqA04UnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1jrqB04UnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1lvnA04UnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1lvnB04UnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1oacA04UnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1oacB04UnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1spuA04UnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1spuB04UnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1dyuA04UnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1dyuB04UnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1qafA04UnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1qafB04UnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1qakA04UnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1qakB04UnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1qalA04UnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1qalB04UnboundUnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound

Active-site residues
pdbCatalytic residuesCofactor-binding residuesModified residuescomment
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       



1d6uA03TYR 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)

1d6uB03TYR 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)

1d6yA03TYR 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)

1d6yB03TYR 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)

1d6zA03TYR 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)

1d6zB03TYR 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
1lvnA03TYR 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)

1lvnB03TYR 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)

1oacA03TYR 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)

1oacB03TYR 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)

1spuA03TYR 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)

1spuB03TYR 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)

1dyuA03TYR 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)

1dyuB03TYR 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)

1qafA03TYR 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
1qafB03TYR 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
1qakA03TYR 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
1qakB03TYR 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
1qalA03TYR 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
1qalB03TYR 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
ReferencesSectionsNo. 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]
PubMed ID8155661
JournalBiochemistry
Year1994
Volume33
Pages4425-31
AuthorsBossa M, Morpurgo GO, Morpurgo L
TitleModels and molecular orbital semiempirical calculations in the study of the spectroscopic properties of bovine serum amine oxidase quinone cofactor.
[2]
PubMed ID8176752
JournalJ Mol Biol
Year1994
Volume238
Pages635-7
AuthorsRoh JH, Suzuki H, Kumagai H, Yamashita M, Azakami H, Murooka Y, Mikami B
TitleCrystallization and preliminary X-ray analysis of copper amine oxidase from Escherichia coli K-12.
[3]
PubMed ID8585612
JournalAnal Biochem
Year1995
Volume230
Pages159-66
AuthorsSteinebach V, Groen BW, Wijmenga SS, Niessen WM, Jongejan JA, Duine JA
TitleIdentification of topaquinone, as illustrated for pig kidney diamine oxidase and Escherichia coli amine oxidase.
[4]
PubMed ID7766611
JournalBiochemistry
Year1995
Volume34
Pages7020-6
AuthorsMoenne-Loccoz P, Nakamura N, Steinebach V, Duine JA, Mure M, Klinman JP, Sanders-Loehr J
TitleCharacterization of the topa quinone cofactor in amine oxidase from Escherichia coli by resonance Raman spectroscopy.
[5]
PubMed ID8524164
JournalMethods Enzymol
Year1995
Volume258
Pages53-69
AuthorsSayre LM, Lee Y
TitleCatalytic aerobic deamination of activated primary amines by a model for the quinone cofactor of mammalian copper amine oxidases.
[6]
PubMed ID8591022
JournalStructure
Year1995
Volume3
Pages1127-9
AuthorsFontecave M, Eklund H
TitleCopper amine oxidase: a novel use for a tyrosine.
[7]
CommentsX-ray crystallography
PubMed ID8591028
JournalStructure
Year1995
Volume3
Pages1171-84
AuthorsParsons MR, Convery MA, Wilmot CM, Yadav KD, Blakeley V, Corner AS, Phillips SE, McPherson MJ, Knowles PF
TitleCrystal structure of a quinoenzyme: copper amine oxidase of Escherichia coli at 2 A resolution.
Related PDB1oac
[8]
PubMed ID8706668
JournalEur J Biochem
Year1996
Volume238
Pages683-9
AuthorsSteinebach V, De Jong GA, Wijmenga SS, De Vries S, Duine JA
TitleThe copper-topaquinone-phenylhydrazine-adduct geometry in Escherichia coli amine oxidase derivatized with phenylhydrazines substituted with 19F-NMR relaxation measurements.
[9]
PubMed ID8621418
JournalJ Biol Chem
Year1996
Volume271
Pages5580-8
AuthorsSteinebach V, de Vries S, Duine JA
TitleIntermediates in the catalytic cycle of copper-quinoprotein amine oxidase from Escherichia coli.
[10]
CommentsX-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS)
Medline ID97200715
PubMed ID9048544
JournalBiochemistry
Year1997
Volume36
Pages1608-20
AuthorsWilmot CM, Murray JM, Alton G, Parsons MR, Convery MA, Blakeley V, Corner AS, Palcic MM, Knowles PF, McPherson MJ, Phillips SE
TitleCatalytic mechanism of the quinoenzyme amine oxidase from Escherichia coli: exploring the reductive half-reaction.
Related PDB1spu
Related Swiss-protP46883
[11]
PubMed ID11848913
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Year1998
Volume98
Pages705-762
AuthorsStubbe J, van Der Donk WA
TitleProtein Radicals in Enzyme Catalysis.
[12]
CommentsX-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS)
Medline ID99315198
PubMed ID10387067
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Year1999
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Pages8217-27
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Related Swiss-protP46883
[13]
CommentsX-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS)
Medline ID20045000
PubMed ID10576737
JournalScience
Year1999
Volume286
Pages1724-8
AuthorsWilmot CM, Hajdu J, McPherson MJ, Knowles PF, Phillips SE
TitleVisualization of dioxygen bound to copper during enzyme catalysis.
Related PDB1d6u,1d6y,1d6z
Related Swiss-protP46883
[14]
PubMed ID11665487
JournalAdv Protein Chem
Year2001
Volume58
Pages141-74
AuthorsDove JE, Klinman JP
TitleTrihydroxyphenylalanine quinone (TPQ) from copper amine oxidases and lysyl tyrosylquinone (LTQ) from lysyl oxidase.
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Related PDB1jrq
[16]
PubMed ID11751046
JournalCurr Opin Struct Biol
Year2001
Volume11
Pages666-73
AuthorsDawkes HC, Phillips SE
TitleCopper amine oxidase: cunning cofactor and controversial copper.
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Pages4686-97
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TitleProbing the catalytic mechanism of Escherichia coli amine oxidase using mutational variants and a reversible inhibitor as a substrate analogue.
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Pages687-96
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PubMed ID12153561
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Pages3645-58
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Pages493-6
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Year2004
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Pages22-31
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JournalFEBS Lett
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Pages301-5
AuthorsWilmot CM, Saysell CG, Blessington A, Conn DA, Kurtis CR, McPherson MJ, Knowles PF, Phillips SE
TitleMedical implications from the crystal structure of a copper-containing amine oxidase complexed with the antidepressant drug tranylcypromine.
Related PDB1lvn
[25]
PubMed ID15369390
JournalJ Med Chem
Year2004
Volume47
Pages4865-74
AuthorsMarti L, Abella A, De La Cruz X, Garcia-Vicente S, Unzeta M, Carpene C, Palacin M, Testar X, Orozco M, Zorzano A
TitleExploring the binding mode of semicarbazide-sensitive amine oxidase/VAP-1: identification of novel substrates with insulin-like activity.

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):

createdupdated
2005-05-262009-02-26


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)

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