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1.4.3.21: primary-amine oxidase

This is an abbreviated version!
For detailed information about primary-amine oxidase, go to the full flat file.

Word Map on EC 1.4.3.21

Reaction

RCH2NH2
+
H2O
+
O2
=
RCHO
+
NH3
+
H2O2

Synonyms

AGAO, AMAO2, AMAO3, amine oxidase 1, amine oxidase, copper containing, AO1, AO2, AOC2, AOC3, BAO, benzylamine oxidase, bovine plasma amine oxidase, bovine serum amine oxidase, BPAO, BSAO, CAO, Copper amine oxidase, copper amine oxidase 1, copper amine oxidase 8, copper-containing amine oxidase, copper-containing AO, copper-containing monoamine oxidase, copper-dependent amine oxidase, copper/quinone containing amine oxidase, Cu/TPQ amine oxidase, CuAO, CuAO1, CuAO2, CuAO3, CuAO8, EC 1.4.3.6, ECAO, ELAO, GPAO, grass pea amine oxidase, Hansenula polymorpha amine oxidase, HPAO, hPAO-1, HPAO-2, lentil seedling amine oxidase, LSAO, MAO-N, More, OVAO, PAO, pea seedling amine oxidase, plasma amine oxidase, PrAO, primary amine oxidase, primary-amine:oxygen oxidoreductase, PSAO, quinone- and copper-containing amine oxidase, quinone-containing copper amine oxidase, quinone-dependent amine oxidase, quinoprotein copper-containing amine oxidase, RAO, sainfoin amine oxidase, semicarbazide-sensitive amine oxidase, semicarbazide-sensitive amine oxidase/vascular adhesion protein-1, SSAO, SSAO/VAP-1, TPQ-containing CuAO, tynA, tyramine oxidase, copper-requiring, VAP-1, vascular adhesion protein 1, vascular adhesion protein-1

ECTree

     1 Oxidoreductases
         1.4 Acting on the CH-NH2 group of donors
             1.4.3 With oxygen as acceptor
                1.4.3.21 primary-amine oxidase

Engineering

Engineering on EC 1.4.3.21 - primary-amine oxidase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D298A
Km-value for 2-phenylethylamine is 85% of the wild-type enzyme, kcat for 2-phenylethylamine is 360000fold lower than wild-type enzyme
D298K
in contrast to M602K and wild-type enzyme, the quinone in D298K does not react with any of the hydrazines. D298K shows no activity toward oxidative deamination of 2-phenylethylamine. The quinone formed in D298K is trapped in a conformation that can not react with amines. D298K contains a quinone other than topaquinone
M602K
the mutant enzyme shows 20% activity toward 2-phenylethylamine in comparison to wild-type enzyme
N336S/M348K/I246M
N336S/M348K/I246M/T384N/D385S
D383E
-
turnover-number of mutant enzyme is reduced up to 2000fold, depending on pH-value
D383N
-
catalytically inactive mutant enzyme
L469G
the mutant shows increased affinity for benzylamine and methylamine compared to the wild type enzyme
M211V
the mutant shows increased affinity for benzylamine and methylamine compared to the wild type enzyme
M211V/Y394N/L469G
T212A
the mutant shows increased affinity for benzylamine and reduced affinity for methylamine compared to the wild type enzyme
Y394N
the mutant shows reduced affinity for benzylamine and methylamine compared to the wild type enzyme
F190Y
the mutant loses the activity within the range of pH 6.8-8.5
F384G
the mutant loses the activity within the range of pH 6.8-8.5
I160F
the mutant loses the activity within the range of pH 6.8-8.5
S406T
the mutant loses the activity within the range of pH 6.8-8.5
Y320F
the mutant loses the activity within the range of pH 6.8-8.5
Y326F
the mutant loses the activity within the range of pH 6.8-8.5
Y305A
-
mutation has moderate effects on the kinetics of catalysis (2.7fold and 8fold decrease in kcat using ethylamine and benzylamine as substrates), the same mutation slows cofactor formation by about 45-fold relative to that of the wild-type enzyme. The Y305A mutant forms at least two species: primarily topaquinone at lower pH and a species with a blue-shifted absorbance at high pH
Y305F
-
the rate of topaquinone formation is reduced 3fold relative to that of wild-type enzyme, 125fold decrease in kcat using ethylamine as substrate
H456A
-
site-directed mutagenesis, the active site residue mutant shows reduced activity compared to the wild-type enzyme
H458A
-
site-directed mutagenesis, the active site residue mutant shows reduced activity compared to the wild-type enzyme
H460A
-
site-directed mutagenesis, the active site residue mutant shows reduced activity compared to the wild-type enzyme
H621A
-
site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-type enzyme
H627A
-
site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-type enzyme
H456A
Schizosaccharomyces pombe FY435 / ATCC 87284
-
site-directed mutagenesis, the active site residue mutant shows reduced activity compared to the wild-type enzyme
-
H458A
Schizosaccharomyces pombe FY435 / ATCC 87284
-
site-directed mutagenesis, the active site residue mutant shows reduced activity compared to the wild-type enzyme
-
H460A
Schizosaccharomyces pombe FY435 / ATCC 87284
-
site-directed mutagenesis, the active site residue mutant shows reduced activity compared to the wild-type enzyme
-
H621A
Schizosaccharomyces pombe FY435 / ATCC 87284
-
site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-type enzyme
-
H627A
Schizosaccharomyces pombe FY435 / ATCC 87284
-
site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-type enzyme
-
additional information