Tryptophan decarboxylase from Catharanthus roseus is a pyridoxoquinoprotein

FEBS Letters

Groen, Barend W.¹  Pennings, Ed J.M.²  Duine, Johannis A.¹  Verpoorte, Robert² 

[1] Department of Microbiology and Enzymology, Delft University of Technology, Julianalaan 67, 2628 BC Delft, The Netherlands;Biotechnology Delft Leiden, Project Group Plant Cell Biotechnology, Center for Bio-Pharmaceutical Sciences, Division of Pharmacognosy, Leiden University, PO Box 9502, 2300 RA Leiden The Netherlands

关键词: Tryptophan decarboxylase;    Hydrophobic interaction chromatography;    Pyrroloquinoline quinone;    Pyridoxal Phosphate;    Pyridoxo-quinoprotein;    (Catharanthus roseus);    HIC;    hydrophobic interaction chromatography;    PLP;    pyridoxal-5′-phosphate;    PQQ;    pyrroloquinoline quinone;    PAGE;    polyacrylamide gel electrophoresis;    TDC;    tryptophan decarboxylase;   

DOI  :  10.1016/0014-5793(89)81068-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Tryptophan decarboxylase (EC 4.1.1.28) from Catharanthus roseus was purified to homogeneity. The native enzyme has an M _r of about 96000 as estimated from native PAGE. After SDS-PAGE, three protein bands were visible corresponding with M _r 49000, 33000 and 17000. The N-termini of the 49 kDa protein and the 33 kDa protein were identical. Antibodies against the 49 kDA protein also reacted strongly with the two smaller proteins. It is concluded that the native enzyme consists of two subunits of M _r 49000. Tryptophan decarboxylase appears to be a pyridoxo-quinoprotein, since two molecules of pyridoxal phosphate and two molecules of covalently-bound pyrroloquinoline quinone were found per enzyme molecule.

【 授权许可】

Unknown