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1.4.3.4: monoamine oxidase

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

Word Map on EC 1.4.3.4

Reaction

RCH2NHR'
+
H2O
 +
O2
=
RCHO
 +
R'NH2
 +
H2O2

Synonyms

adrenaline oxidase, amine-oxygen oxidoreductase, C-MAO, EC 1.4.3.9, epinephrine oxidase, MAO, MAO A, MAO B, MAO type B, MAO-A, MAO-B, MAO-N, MAO-N-D5, MAOA, MAOB, monoamine oxidase, monoamine oxidase A, monoamine oxidase B, monoamine oxidase N, monoamine oxidase type B, monoamine oxidase-A, monoamine oxidase-B, monoamine oxidaseA, monoamine oxidases A, monoamine oxidases B, monoamine-oxidase-A, monoamine: O2-oxidoreductase, deaminated, monoamine: O2-oxidoreductase, deaminating, monoamine: O2-oxidoreductase: deaminating, monoamine:O2 oxidoreductase (deaminating), monoamine:O2 oxidoreductase, deaminating, monoamine:O2-oxidoreductase deaminating, monoaminoxidase B, More, semicarbazide-sensitive amine oxidase, serotonin deaminase, SSAO, tyraminase, tyramine oxidase, zMAO

ECTree

     1 Oxidoreductases
         1.4 Acting on the CH-NH2 group of donors
             1.4.3 With oxygen as acceptor
                1.4.3.4 monoamine oxidase

Engineering

Engineering on EC 1.4.3.4 - monoamine oxidase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
T354S
LG-F-B5, no activity with 1,2,3,4-tetrahydro-1-phenylisoquinoline
W230I/T354S/W430R
LG-F-B7, the mutant enzyme accepts the bulky substrate 1,2,3,4-tetrahydro-1-phenylisoquinoline with a specific activity of 0.3 U/mg
W230I/T354S/W430R/M242R/Y365V
LG-J-B4, specific activity towards 1,2,3,4-tetrahydro-1-phenylisoquinoline is improved more than 2fold as compared to mutant enzyme W230I/T354S/W430R
W230I/W430R
LG-F-B6, mutations change the size and thus shape of the active site pocket so that 1,2,3,4-tetrahydro-1-phenylisoquinoline is accepted with notable activity
W230R/W430C
LG-F-G6, specific activity towards 1,2,3,4-tetrahydro-1-methylisoquinoline is improved 6fold by mutant enzyme W230R/W430C/C214L as compared to mutant enzyme W230R/W430C
W230R/W430C/C214L
LG-I-D11, specific activity towards 1,2,3,4-tetrahydro-1-methylisoquinoline is improved 6fold as compared to mutant enzyme W230R/W430C, it is also active with 1,2,3,4-tetrahydro-1-phenylisoquinoline. When deracemizing 1,2,3,4-tetrahydro-1-methylisoquinoline on a preparative scale, the MAO-N variant allows access to the (S)-enantiomer. It also shows good activity in the preparation of (S)-1,2,3,4-tetrahydro-1-ethylisoquinoline and (S)-1,2,3,4-tetrahydro-1-isopropylisoquinoline on a preparative scale
C374A
mutation of surface cysteine 374 to alanine alters substrate turnover and inactivation by cyclopropylamines
C397A
-
expressed protein catalytically inactive
C397H
-
expressed protein catalytically inactive
D123A
-
2.4fold increase in Km-value for phenylethylamine, 3.3fold increase in IC50-value for clorgyline, 3.3fold increase in IC50-value for deprenyl
D132A
-
2.2fold increase in Km-value for serotonin,1.8fold increase in IC50-value for clorgyline, 3.9fold increase in IC50-value for deprenyl
E142K
a MAOB mutant
I199A
I199A/Y326A
-
the mutant exhibits catalytic properties with 75fold increased amine Km but unaltered kcat values. The mutant shows inhibitor binding properties more similar to those of isoform MAO A than to isoform MAO B. Benzylamine is a poor substrate for the double mutant
I199F
-
the bulky Phe side chain impedes such conformational flexibility, reduces the space of the entrance cavity and interferes with the binding of MAO B-specific inhibitors
K151E
a MAOA mutant
K296A
-
no activity with phenylethylamine
K305A
-
no detectable activity with serotonin
S209A
site-directed mutagenesis of the phosphorylation site. The MAO A S209A mutant exhibits similar catalytic properties to those of wild-type enzyme, its catalytic activity is reduced by 1.5-3.7fold compared to the wild-type MAO A
S209E
site-directed mutagenesis of the phosphorylation site. Compared with purified wild-type and S209A MAO A proteins, the S209G MAO A mutant shows 10fold reduced kcat values and 10fold increased Km values compared to the wild-type enzymesignificant differences in covalent flavin fluorescence yield, circular dichroism spectra and thermal stability
W388A
-
no activity with phenylethylamine
W397A
-
no detectable activity with serotonin
Y398F
-
3.5fold increase in Km-value for phenylethylamine, 7.9fold increase in IC50-value for clorgyline, 15.5fold increase in IC50-value for deprenyl
Y398S
-
no activity with phenylethylamine
Y407F
Y407S
-
no detectable activity with serotonin
Y435F
Y435H
kcat/KM for benzylamine is 120fold lower than wild-type value, kcat/KM for p-trifluoromethyl-benzylamine is 13fold lower than wild-type value, kcat/KM for p-nitrobenzylamine is 4.4fold lower than wild-type value, kcat/KM for phenylethylamine is 1037fold lower than wild-type value, kcat/KM for p-nitrophenylethylamine is 45.2 fold lower than wild-type value
Y435L
kcat/KM for benzylamine is 128fold lower than wild-type value, kcat/KM for p-trifluoromethyl-benzylamine is 58fold lower than wild-type value, kcat/KM for phenylethylamine is 15.2fold lower than wild-type value, kcat/KM for p-nitrophenylethylamine is 2.7fold lower than wild-type value
Y435S
-
no activity with phenylethylamine
Y435W
kcat/KM for benzylamine is 9524fold lower than wild-type value, kcat/KM for phenylethylamine is 13889fold lower than wild-type value, kcat/KM for p-nitrophenylethylamine is 23fold lower than wild-type value
Y444F
Y444S
-
no detectable activity with serotonin
C406A
-
MAO-A, Km for serotonin and tyramine not altered
Y402A
-
decrease in activity not significant, decrease in the FAD incorporation
Y402F
Y403A
-
the ratio of turnover number to Km-value for serotonin is 95.6fold lower than that of the mutant enzyme, the ratio of turnover number to Km-value for phenylethylamine is 210fold lower than that of the wild-type enzyme, the ratio of turnover number to Km-value for tyramine is 170fold lower than that of the wild-type enzyme, the ratio of turnover number to KM-value for tryptamine is 91fold lower than that of the wild-type enzyme. Mutant enzyme is sensitive to trypsin treatment, while the wild-type enzyme is resistant
Y407A
Y407F
Y410A
Y402A
-
decrease in activity not significant, decrease in the FAD incorporation
-
Y407A
Y407F
additional information