B6db families : 2_6_1

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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

PLP-dependent Domain

Domain alignment
Domain hmm

Fold type I

Number of sequences

Sequences in seed alignment

Fungi

XP_001523024 (Magnaporthe grisea 70-15); ABU51605 (Emericella nidulans); XP_017990264 (Malassezia pachydermatis); EAU86022 (Coprinopsis cinerea); XP_011387757 (Ustilago maydis 521); AGI59488 (Malassezia furfur); OAJ19145 (Tilletia walkeri);

DISPLAY: Fasta format, alignment, hmm, hmm_local

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