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Literature summary 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

Cloned(Commentary)

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

Protein Variants

EC Number Protein Variants Comment Organism
1.4.3.4 Y402A decrease in activity not significant, decrease in the FAD incorporation Rattus norvegicus
1.4.3.4 Y402F decrease in activity not significant Rattus norvegicus
1.4.3.4 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
1.4.3.4 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
1.4.3.4 Y407A no activity with serotonin, phenylethylamine, tyramine, low activity with tryptamine, decrease in the FAD incorporation Rattus norvegicus
1.4.3.4 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
1.4.3.4 Y407F little changes in Km for all substrates Rattus norvegicus
1.4.3.4 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
1.4.3.4 Y410A decrease in activity not significant Rattus norvegicus
1.4.3.4 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

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

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.4.3.4 additional information
-
 additional information comparison of Km of mutant enzymes using serotonin, phenylethylamine, tyramine, tryptamine as substrates Rattus norvegicus
1.4.3.4 0.028
-
 tryptamine 30°C, mutant enzyme Y407F Rattus norvegicus
1.4.3.4 0.033
-
 tryptamine 30°C, wild-type enzyme Rattus norvegicus
1.4.3.4 0.035
-
 tryptamine 30°C, mutant enzyme Y402F Rattus norvegicus
1.4.3.4 0.038
-
 tryptamine 30°C, mutant enzyme Y410A Rattus norvegicus
1.4.3.4 0.055
-
 tryptamine 30°C, mutant enzyme Y402A Rattus norvegicus
1.4.3.4 0.44
-
 serotonin 30°C, wild-type enzyme Rattus norvegicus
1.4.3.4 0.51
-
 serotonin 30°C, mutant enzyme Y410A Rattus norvegicus
1.4.3.4 0.55
-
 serotonin 30°C, mutant enzyme Y402A Rattus norvegicus
1.4.3.4 0.57
-
 2-Phenylethylamine 30°C, wild-type enzyme Rattus norvegicus
1.4.3.4 0.59
-
 serotonin 30°C, mutant enzyme Y402F Rattus norvegicus
1.4.3.4 0.6
-
 tyramine 30°C, wild-type enzyme Rattus norvegicus
1.4.3.4 0.63
-
 tyramine 30°C, mutant enzyme Y402F Rattus norvegicus
1.4.3.4 0.78
-
 2-Phenylethylamine 30°C, mutant enzyme Y402F Rattus norvegicus
1.4.3.4 0.95
-
 serotonin 30°C, mutant enzyme Y407F Rattus norvegicus
1.4.3.4 1.13
-
 tyramine 30°C, mutant enzyme Y410A Rattus norvegicus
1.4.3.4 1.13
-
 2-Phenylethylamine 30°C, mutant enzyme Y410A Rattus norvegicus
1.4.3.4 1.42
-
 tyramine 30°C, mutant enzyme Y407F Rattus norvegicus
1.4.3.4 1.42
-
 2-Phenylethylamine 30°C, mutant enzyme Y407F Rattus norvegicus
1.4.3.4 1.98
-
 2-Phenylethylamine 30°C, mutant enzyme Y402A Rattus norvegicus
1.4.3.4 3.1
-
 tryptamine 30°C, mutant enzyme Y407A Rattus norvegicus
1.4.3.4 4.6
-
 tyramine 30°C, mutant enzyme Y402A Rattus norvegicus

Localization

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

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
1.4.3.4 Rattus norvegicus
-
-
-
1.4.3.4 Rattus norvegicus
-
 MAO-A
-
1.4.3.4 Rattus norvegicus MAO-A
-
 MAO-A
-

Purification (Commentary)

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.4.3.4 2-phenylethylamine + H2O + O2
-
 Rattus norvegicus 2-phenylethanal + NH3 + H2O2
-
 ?
1.4.3.4 2-phenylethylamine + H2O + O2
-
 Rattus norvegicus MAO-A 2-phenylethanal + NH3 + H2O2
-
 ?
1.4.3.4 RCH2NH2 + H2O + O2
-
 Rattus norvegicus RCHO + NH3 + H2O2
-
 ?
1.4.3.4 RCH2NH2 + H2O + O2
-
 Rattus norvegicus MAO-A RCHO + NH3 + H2O2
-
 ?
1.4.3.4 serotonin + H2O + O2
-
 Rattus norvegicus (5-hydroxy-1H-indol-3-yl)acetaldehyde + NH3 + H2O2
-
 ?
1.4.3.4 tryptamine + H2O + O2
-
 Rattus norvegicus 1-H-indol-3-yl-acetaldehyde + NH3 + H2O2
-
 ?
1.4.3.4 tyramine + H2O + O2
-
 Rattus norvegicus (4-hydroxyphenyl)acetaldehyde + NH3 + H2O2
-
 ?
1.4.3.4 tyramine + H2O + O2
-
 Rattus norvegicus MAO-A (4-hydroxyphenyl)acetaldehyde + NH3 + H2O2
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.4.3.4 MAOA
-
 Rattus norvegicus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.4.3.4 0.033
-
 2-Phenylethylamine 30°C, mutant enzyme Y402A Rattus norvegicus
1.4.3.4 0.066
-
 tryptamine 30°C, mutant enzyme Y402A Rattus norvegicus
1.4.3.4 0.17
-
 serotonin 30°C, mutant enzyme Y402A Rattus norvegicus
1.4.3.4 0.183
-
 tryptamine 30°C, mutant enzyme Y407A Rattus norvegicus
1.4.3.4 0.33
-
 tyramine 30°C, mutant enzyme Y402A Rattus norvegicus
1.4.3.4 0.5
-
 serotonin 30°C, mutant enzyme Y402F Rattus norvegicus
1.4.3.4 0.67
-
 2-Phenylethylamine 30°C, mutant enzyme Y410A Rattus norvegicus
1.4.3.4 0.833
-
 2-Phenylethylamine 30°C, mutant enzyme Y402F Rattus norvegicus
1.4.3.4 1.17
-
 2-Phenylethylamine 30°C, mutant enzyme Y407F Rattus norvegicus
1.4.3.4 1.2
-
 tryptamine 30°C, mutant enzyme Y410A Rattus norvegicus
1.4.3.4 1.267
-
 serotonin 30°C, wild-type enzyme Rattus norvegicus
1.4.3.4 1.8
-
 tryptamine 30°C, mutant enzyme Y402F Rattus norvegicus
1.4.3.4 1.83
-
 serotonin 30°C, mutant enzyme Y410A Rattus norvegicus
1.4.3.4 2
-
 2-Phenylethylamine 30°C, wild-type enzyme Rattus norvegicus
1.4.3.4 2
-
 tyramine 30°C, mutant enzyme Y410A Rattus norvegicus
1.4.3.4 2.4
-
 tryptamine 30°C, mutant enzyme Y407F Rattus norvegicus
1.4.3.4 3.33
-
 tyramine 30°C, mutant enzyme Y402F Rattus norvegicus
1.4.3.4 3.5
-
 tryptamine 30°C, wild-type enzyme Rattus norvegicus
1.4.3.4 4.83
-
 tyramine 30°C, mutant enzyme Y407F Rattus norvegicus
1.4.3.4 6.83
-
 tyramine 30°C, wild-type enzyme Rattus norvegicus
1.4.3.4 10.67
-
 serotonin 30°C, mutant enzyme Y407F Rattus norvegicus

Cofactor

EC Number Cofactor Comment Organism Structure
1.4.3.4 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
1.4.3.4 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