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Structure and Reaction Mechanism of Pyrrolysine Synthase (PylD)
Author(s) -
Quitterer Felix,
Beck Philipp,
Bacher Adelbert,
Groll Michael
Publication year - 2013
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201301164
Subject(s) - computer science , mechanism (biology) , substrate (aquarium) , product (mathematics) , computational biology , terminal (telecommunication) , chemistry , biochemistry , combinatorial chemistry , stereochemistry , biology , philosophy , computer network , mathematics , epistemology , geometry , ecology
The final step in the biosynthesis of the 22nd genetically encoded amino acid, pyrrolysine, is catalyzed by PylD, a structurally and mechanistically unique dehydrogenase. This catalyzed reaction includes an induced‐fit mechanism achieved by major structural rearrangements of the N‐terminal helix upon substrate binding. Different steps of the reaction trajectory are visualized by complex structures of PylD with substrate and product.