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Literature summary for 1.4.3.4 extracted from

  • Edmondson, D.E.; Mattevi, A.; Binda, C.; Li, M.; Hubalek, F.
    Structure and mechanism of monoamine oxidase (2004), Curr. Med. Chem., 11, 1983-1993.
    View publication on PubMed
Search for more literature for 1.4.3.4

Cloned(Commentary)

Cloned (Comment) Organism
high level expression in Pichia pastoris Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
three-dimensional structure of the enzyme in complex with different reversible (isatin, 1,4-diphenyl-2-butene) and irreversible inhibitors (pargyline, N-(2,aminoethyl)-p-chlorobenzamide, and trans-2-phenylcyclopropylamine), up to 1.7 A resolution Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrial outer membrane
-
 Homo sapiens 5741
-
mitochondrion outer membrane Homo sapiens 5739
-

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
acetylated protein the amino-terminal Met is cleaved from the protein on processing the nascent polypeptide chain and the resulting N-terminal serine is acetylated both in the recombinant human and in the bovine enzymes Homo sapiens
acetylated protein the amino-terminal Met residue remains with the protein and is N-acetylated Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
 Homo sapiens
-

Synonyms

Synonyms Comment Organism
MAO A
-
 Homo sapiens
MAO B
-
 Homo sapiens
monoamine oxidase A
-
 Homo sapiens
monoamine oxidase B
-
 Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
-
 Homo sapiens

Cofactor

Cofactor Comment Organism Structure
FAD covalently bound Homo sapiens