Related Experiment Videos
Properties and function of indoleamine 2,3-dioxygenase
Journal of Biochemistry
|April 1, 1976
Summary
Indoleamine 2,3-dioxygenase (IDO) catalyzes indoleamine breakdown in vivo, potentially using superoxide anion. This enzyme produces novel anthraniloylamines with unknown biological activities.
Area of Science:
- Biochemistry
- Enzymology
- Pharmacology
Background:
- Indoleamine 2,3-dioxygenase (IDO) is abundant in the lung, colon, and intestine.
- IDO catalyzes the oxidative ring cleavage of various indoleamines, including tryptophan and serotonin.
Purpose of the Study:
- To investigate the in vivo occurrence and substrate utilization of indoleamine 2,3-dioxygenase (IDO).
- To characterize the novel biogenic amines produced by IDO activity.
Main Methods:
- Experiments using intestinal slices, organ culture of pineal glands, and perfusion of heart and lung preparations.
- In vivo studies with intact animals.
Main Results:
- Oxygenative ring cleavages of indoleamines occur significantly in vivo.
- IDO appears to utilize superoxide anion as a substrate, rather than molecular oxygen.
- A new class of biogenic amines, termed 'anthraniloylamines,' was produced by the enzyme.
Conclusions:
- IDO may represent a novel class of enzymes utilizing superoxide anion.
- The newly identified anthraniloylamines may possess significant biological or pharmacological activities requiring further investigation.