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Literature summary extracted from

  • Takai, K.; Sasai, Y.; Morimoto, H.; Yamazaki, H.; Yoshii, H.; Inoue, S.
    Enzymatic dehydrogenation of tryptophan residues of human globins by tryptophan side chain oxidase II (1984), J. Biol. Chem., 259, 4452-4457.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.3.3.10 Sodium dodecyl sulfate no modification with 0.4% SDS Pseudomonas sp.
1.3.3.10 Urea no modification with 8 M urea Pseudomonas sp.

Organism

EC Number Organism UniProt Comment Textmining
1.3.3.10 Pseudomonas sp.
-
-
-
1.13.99.3 Pseudomonas sp.
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.13.99.3 L-tryptophan + O2 = (indol-3-yl)glycolaldehyde + CO2 + NH3 model of mechanism Pseudomonas sp.

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.3.10 tryptophan No.14 of alpha-globin + O2
-
Pseudomonas sp. alpha,beta-dehydrotryptophan + H2O2
-
?
1.3.3.10 tryptophan No.15 of beta-globin + O2
-
Pseudomonas sp. alpha,beta-dehydrotryptophan + H2O2
-
?
1.13.99.3 additional information substrates: tryptophan residues in human alpha- and beta-globins Pseudomonas sp. additional information
-
?

Synonyms

EC Number Synonyms Comment Organism
1.3.3.10 tryptophan side chain oxidase II
-
Pseudomonas sp.

Cofactor

EC Number Cofactor Comment Organism Structure
1.13.99.3 heme hemoprotein Pseudomonas sp.