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Literature summary for 2.6.1.27 extracted from

  • Lesch, T.; Bode, R.; Birnbaum, D.
    Transamination of L- and D-tryptophan by a soluble and a particle-bound enzyme fraction of Rhodosporidium toruloides (1979), Biochem. Physiol. Pflanz., 174, 546-554.
No PubMed abstract available
Search for more literature for 2.6.1.27

Activating Compound

Activating Compound Comment Organism Structure
additional information
-
 Rhodotorula toruloides

Localization

Localization Comment Organism GeneOntology No. Textmining
particle-bound no sucess in solubilization of the enzyme from the particles Rhodotorula toruloides
-
-

Organism

Organism UniProt Comment Textmining
Rhodotorula toruloides
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-tryptophan + 2-oxoglutarate activity can be due to a different enzyme Rhodotorula toruloides L-glutamate + 3-indole-2-oxopropanoate
-
 ?
L-tryptophan + 2-oxoglutarate
-
 Rhodotorula toruloides L-glutamate + 3-indole-2-oxopropanoate
-
 ?