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Characterization of tryptophan aminotransferase 1 of M alassezia furfur , the key enzyme in the production of indolic compounds by M. furfur
Author(s) -
Preuss Janina,
Hort Wiebke,
Lang Sarah,
Netsch Anette,
Rahlfs Stefan,
Lochnit Günter,
Jortzik Esther,
Becker Katja,
Mayser Peter A.
Publication year - 2013
Publication title -
experimental dermatology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.108
H-Index - 96
eISSN - 1600-0625
pISSN - 0906-6705
DOI - 10.1111/exd.12260
Subject(s) - transamination , enzyme , tryptophan , biochemistry , chemistry , biosynthesis , pigment , pyridoxal phosphate , stereochemistry , cofactor , amino acid , organic chemistry
M alassezia yeasts are responsible for the widely distributed skin disease Pityriasis versicolor ( PV ), which is characterized by a hyper‐ or hypopigmentation of affected skin areas. For M alassezia furfur , it has been shown that pigment production relies on tryptophan metabolism. A tryptophan aminotransferase was found to catalyse the initial catalytic step in pigment formation in the model organism U stilago maydis . Here, we describe the sequence determination, recombinant production and biochemical characterization of tryptophan aminotransferase M f T am1 from M . furfur . The enzyme catalyses the transamination from l ‐tryptophan to keto acids such as α‐ketoglutarate with K m values for both substrates in the low millimolar range. Furthermore, M f T am1 presents a temperature optimum at 40°C and a p H optimum at 8.0. M f T am1 activity is highly dependent on pyridoxal phosphate ( PLP ), whereas compounds interfering with PLP , such as cycloserine ( CS ) and aminooxyacetate, inhibit the M f T am1 reaction. CS is known to reverse hyperpigmentation in PV . Thus, the results of the present study give a deeper insight into the role of M f T am1 in PV pathogenesis and as potential target for the development of novel PV therapeutics.