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Literature summary for 1.4.3.4 extracted from

  • Ma, J.; Ito, A.
    Tyrosine residues near the FAD binding site are critical for FAD binding and for the maintenance of the stable and active conformation of rat monoamine oxidase A (2002), J. Biochem., 131, 107-111.
    View publication on PubMed
Search for more literature for 1.4.3.4

Cloned(Commentary)

Cloned (Comment) Organism
expression in Saccharomyces cerevisiae BJ 2168 Rattus norvegicus
expression in yeast Rattus norvegicus

Protein Variants

Protein Variants Comment Organism
Y402A decrease in activity not significant, decrease in the FAD incorporation Rattus norvegicus
Y402F decrease in activity not significant Rattus norvegicus
Y402F the ratio of turnover number to Km-value for serotonin is 3.4fold lower than that of the mutant enzyme, the ratio of turnover number to Km-value for phenylethylamine is 3.3fold lower than that of the wild-type enzyme, the ratio of turnover number to Km-value for tyramine is 2.1fold lower than that of the wild-type enzyme, the ratio of turnover number to KM-value for tryptamine is 2.1fold lower than that of the wild-type enzyme Rattus norvegicus
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 Rattus norvegicus
Y407A no activity with serotonin, phenylethylamine, tyramine, low activity with tryptamine, decrease in the FAD incorporation Rattus norvegicus
Y407A mutation leads to almost complete loss of catalytic activity for serotonin, phenylethylamine, tyramine and tryptamine. Mutant enzyme is sensitive to trypsin treatment, while the wild-type enzyme is resistant Rattus norvegicus
Y407F little changes in Km for all substrates Rattus norvegicus
Y407F the ratio of turnover number to Km-value for serotonin is 2.6fold lower than that of the mutant enzyme, the ratio of turnover number to Km-value for phenylethylamine is 4.3fold lower than that of the wild-type enzyme, the ratio of turnover number to Km-value for tyramine is 2.7fold lower than that of the wild-type enzyme, the ratio of turnover number to KM-value for tryptamine is 1.3fold lower than that of the wild-type enzyme Rattus norvegicus
Y410A decrease in activity not significant Rattus norvegicus
Y410A the ratio of turnover number to Km-value for serotonin is 7.8fold lower than that of the mutant enzyme, the ratio of turnover number to Km-value for phenylethylamine is 6fold lower than that of the wild-type enzyme, the ratio of turnover number to Km-value for tyramine is 3.4fold lower than that of the wild-type enzyme, the ratio of turnover number to KM-value for tryptamine is 3.4fold lower than that of the wild-type enzyme. Mutant enzyme is sensitive to trypsin treatment, while the wild-type enzyme is resistant Rattus norvegicus

General Stability

General Stability Organism
wild-type enzyme is resistant to trypsin treatment, mutant enzyms Y403A, Y407A and Y410A are sensitive Rattus norvegicus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information comparison of Km of mutant enzymes using serotonin, phenylethylamine, tyramine, tryptamine as substrates Rattus norvegicus
0.028
-
 tryptamine 30°C, mutant enzyme Y407F Rattus norvegicus
0.033
-
 tryptamine 30°C, wild-type enzyme Rattus norvegicus
0.035
-
 tryptamine 30°C, mutant enzyme Y402F Rattus norvegicus
0.038
-
 tryptamine 30°C, mutant enzyme Y410A Rattus norvegicus
0.055
-
 tryptamine 30°C, mutant enzyme Y402A Rattus norvegicus
0.44
-
 serotonin 30°C, wild-type enzyme Rattus norvegicus
0.51
-
 serotonin 30°C, mutant enzyme Y410A Rattus norvegicus
0.55
-
 serotonin 30°C, mutant enzyme Y402A Rattus norvegicus
0.57
-
 2-Phenylethylamine 30°C, wild-type enzyme Rattus norvegicus
0.59
-
 serotonin 30°C, mutant enzyme Y402F Rattus norvegicus
0.6
-
 tyramine 30°C, wild-type enzyme Rattus norvegicus
0.63
-
 tyramine 30°C, mutant enzyme Y402F Rattus norvegicus
0.78
-
 2-Phenylethylamine 30°C, mutant enzyme Y402F Rattus norvegicus
0.95
-
 serotonin 30°C, mutant enzyme Y407F Rattus norvegicus
1.13
-
 tyramine 30°C, mutant enzyme Y410A Rattus norvegicus
1.13
-
 2-Phenylethylamine 30°C, mutant enzyme Y410A Rattus norvegicus
1.42
-
 tyramine 30°C, mutant enzyme Y407F Rattus norvegicus
1.42
-
 2-Phenylethylamine 30°C, mutant enzyme Y407F Rattus norvegicus
1.98
-
 2-Phenylethylamine 30°C, mutant enzyme Y402A Rattus norvegicus
3.1
-
 tryptamine 30°C, mutant enzyme Y407A Rattus norvegicus
4.6
-
 tyramine 30°C, mutant enzyme Y402A Rattus norvegicus

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrial outer membrane
-
 Rattus norvegicus 5741
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
RCH2NH2 + H2O + O2 Rattus norvegicus
-
 RCHO + NH3 + H2O2
-
 ?
RCH2NH2 + H2O + O2 Rattus norvegicus MAO-A
-
 RCHO + NH3 + H2O2
-
 ?

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-
Rattus norvegicus
-
 MAO-A
-
Rattus norvegicus MAO-A
-
 MAO-A
-

Purification (Commentary)

Purification (Comment) Organism
His-tagged rat enzyme and its mutants Y403A, Y402F, Y407A, Y407F, Y410A Rattus norvegicus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-phenylethylamine + H2O + O2
-
 Rattus norvegicus 2-phenylethanal + NH3 + H2O2
-
 ?
2-phenylethylamine + H2O + O2
-
 Rattus norvegicus MAO-A 2-phenylethanal + NH3 + H2O2
-
 ?
RCH2NH2 + H2O + O2
-
 Rattus norvegicus RCHO + NH3 + H2O2
-
 ?
RCH2NH2 + H2O + O2
-
 Rattus norvegicus MAO-A RCHO + NH3 + H2O2
-
 ?
serotonin + H2O + O2
-
 Rattus norvegicus (5-hydroxy-1H-indol-3-yl)acetaldehyde + NH3 + H2O2
-
 ?
tryptamine + H2O + O2
-
 Rattus norvegicus 1-H-indol-3-yl-acetaldehyde + NH3 + H2O2
-
 ?
tyramine + H2O + O2
-
 Rattus norvegicus (4-hydroxyphenyl)acetaldehyde + NH3 + H2O2
-
 ?
tyramine + H2O + O2
-
 Rattus norvegicus MAO-A (4-hydroxyphenyl)acetaldehyde + NH3 + H2O2
-
 ?

Synonyms

Synonyms Comment Organism
MAOA
-
 Rattus norvegicus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.033
-
 2-Phenylethylamine 30°C, mutant enzyme Y402A Rattus norvegicus
0.066
-
 tryptamine 30°C, mutant enzyme Y402A Rattus norvegicus
0.17
-
 serotonin 30°C, mutant enzyme Y402A Rattus norvegicus
0.183
-
 tryptamine 30°C, mutant enzyme Y407A Rattus norvegicus
0.33
-
 tyramine 30°C, mutant enzyme Y402A Rattus norvegicus
0.5
-
 serotonin 30°C, mutant enzyme Y402F Rattus norvegicus
0.67
-
 2-Phenylethylamine 30°C, mutant enzyme Y410A Rattus norvegicus
0.833
-
 2-Phenylethylamine 30°C, mutant enzyme Y402F Rattus norvegicus
1.17
-
 2-Phenylethylamine 30°C, mutant enzyme Y407F Rattus norvegicus
1.2
-
 tryptamine 30°C, mutant enzyme Y410A Rattus norvegicus
1.267
-
 serotonin 30°C, wild-type enzyme Rattus norvegicus
1.8
-
 tryptamine 30°C, mutant enzyme Y402F Rattus norvegicus
1.83
-
 serotonin 30°C, mutant enzyme Y410A Rattus norvegicus
2
-
 2-Phenylethylamine 30°C, wild-type enzyme Rattus norvegicus
2
-
 tyramine 30°C, mutant enzyme Y410A Rattus norvegicus
2.4
-
 tryptamine 30°C, mutant enzyme Y407F Rattus norvegicus
3.33
-
 tyramine 30°C, mutant enzyme Y402F Rattus norvegicus
3.5
-
 tryptamine 30°C, wild-type enzyme Rattus norvegicus
4.83
-
 tyramine 30°C, mutant enzyme Y407F Rattus norvegicus
6.83
-
 tyramine 30°C, wild-type enzyme Rattus norvegicus
10.67
-
 serotonin 30°C, mutant enzyme Y407F Rattus norvegicus

Cofactor

Cofactor Comment Organism Structure
FAD the attachment to the enzyme may require a pocket constructed partially of tyrosine residues. Through the interactions among the aromatic rings of the tyrosine residues and that of FAD via pi-pi cloud, the enzyme forms a catalytic center and adopts a stable conformation Rattus norvegicus
flavin tyrosine residues near Cys406 may form a pocket to facilitate FAD incorporation and a stable conformation, probably through interactions among the aromatic rings of the tyrosine residues and FAD Rattus norvegicus