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B6db activities: 2.6.1.28

2.6.1.28
Description Tryptophan--phenylpyruvate aminotransferase
Alternative names TdiD.
Catalyzed reaction L-tryptophan + phenylpyruvate = indole-3-pyruvate + L-phenylalanine.
Cofactor Pyridoxal-phosphate.
Comments -!- Valine, leucine and isoleucine can replace tryptophan as amino donor.
Activity originally reported in bacteria, but an enzyme with this specificity has been cloned from Aspergillus nidulans, where it catalyzes the first step in the synthesis of bioactive alkaloids belonging to the bis-indolylquinone family.
Organisms -Eubacteria -Fungi
 

Family 

2.6.1.28 (7)
 
Links Enzyme (activities) 2.6.1.28
BRENDA (activities) 2.6.1.28
KEGG (pathways) 2.6.1.28
PLPMDB (PLP mutants) 2.6.1.28
 
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 2019/06/21 13:04

B6db activities