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Literature summary for 1.4.3.4 extracted from

  • Pohl, B.; Schmidt, W.
    Comparative studies of purified and reconstituted monoamine oxidase from bovine liver mitochondria (1983), Biochim. Biophys. Acta, 731, 338-345.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
deoxycholate
-
Bos taurus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information effect of phospholipids on Km Bos taurus

Localization

Localization Comment Organism GeneOntology No. Textmining

Organic Solvent Stability

Organic Solvent Comment Organism
deoxycholate
-
Bos taurus
Triton X-100 disintegrates the lipid-enzyme cluster to the smallest active units Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
additional information the lipid enviroment appears to be an indispensable prerequisite for proper enzyme activity Bos taurus

Purification (Commentary)

Purification (Comment) Organism
-
Bos taurus

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Bos taurus
-

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
additional information
-
temperature-dependencies of enzyme activity of purified and lipid-treated enzyme Bos taurus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
purified enzyme Bos taurus
8 10 phosphatidylcholine-treated enzyme Bos taurus

Cofactor

Cofactor Comment Organism Structure
flavin flavoprotein Bos taurus