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2.6.1.28 |
Activity |
2.6.1.28 |
Description |
Tryptophan--phenylpyruvate aminotransferase |
Notes |
The family has been built around the characterized enzyme from Aspergillus (Emericella) nidulans. This fungal enzyme catalyzes the first step in the synthesis of bioactive alkaloids of the bis-indolylquinone type.
Proteins most similar to those showing 2-aminoadipate aminotransferase activity (family 2.6.1.39_a). |
PLP Fold Type |
I |
PLP-dependent Domain |
|
Number of sequences |
7 |
Sequences in seed alignment |
|
Reference sequence |
ABU51605 |
Domain interval |
39-425 |
Catalytic site |
270 K |
| |
References |
Preuss J, Hort W, Lang S, Netsch A, Rahlfs S, Lochnit G, Jortzik E, Becker K, Mayser PA. (2013) Characterization of tryptophan aminotransferase 1 of Malassezia furfur, the key enzyme in the production of indolic compounds by M. furfur. Exp Dermatol. 22 736-41. Zuther K, Mayser P, Hettwer U, Wu W, Spiteller P, Kindler BL, Karlovsky P, Basse CW, Schirawski J (2008) The tryptophan aminotransferase Tam1 catalyses the single biosynthetic step for tryptophan-dependent pigment synthesis in Ustilago maydis Mol Microbiol 68 152-72. Schneider P, Weber M, Rosenberger K, Hoffmeister D. (2007) A one-pot chemoenzymatic synthesis for the universal precursor of antidiabetes and antiviral bis-indolylquinones Chem Biol 14 635-44. Articles on 2.6.1.28 |
last changed |
2017/07/17 14:33 |
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