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Crystal Structure and Mechanism of Tryptophan 2,3-Dioxygenase, a Heme Enzyme Involved in Tryptophan Catabolism and in Quinolinate Biosynthesis†,‡

✍ Scribed by Zhang, Yang; Kang, Seong A.; Mukherjee, Tathagata; Bale, Shridhar; Crane, Brian R.; Begley, Tadhg P.; Ealick, Steven E.


Book ID
115523120
Publisher
American Chemical Society
Year
2007
Tongue
English
Weight
721 KB
Volume
46
Category
Article
ISSN
0006-2960

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Tryptophan 2,3-dioxygenase: A review of
✍ Frank O. Brady 📂 Article 📅 1975 🏛 Elsevier Science ⚖ 958 KB

L-Tryptophan 2,3dioxygenase (EC 1.13.11.11) has been purified to homogenity from L-tryptophan induced Pseudomonas acidovorans(ATCC 11299b) and from L-tryptophan and cortisone induced rat liver. The enzyme from both sources is composed of four subunits and contains two g-atoms copper and two moles he