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EC Number Crystallization (Commentary)
Show all pathways known for 4.1.2.8Display the word mapDisplay the reaction diagram Show all sequences 4.1.2.8-
Show all pathways known for 4.1.2.8Display the word mapDisplay the reaction diagram Show all sequences 4.1.2.8the crystal structure of BX1 suggusts that the faster catalytic rate of BX1 compared to the homologous alpha-subuni8t of tryptophan synthase EC 4.2.1.20, may due to a stabilzation of the active conformation, loop alphaL6 is closed and the catalytic glutamate, Glu134 is in the active conformation. There are two crystallographically independent molecules in the asymmetric unit of the rhombohedral BX1 crystal form
Show all pathways known for 4.1.2.8Display the word mapDisplay the reaction diagram Show all sequences 4.1.2.8the crystal structure of tryptophan synthase is determined at 2.1 A resolution
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