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Results 1 - 5 of 5
EC Number Crystallization (Commentary)
Show all pathways known for 2.6.1.39Display the word mapDisplay the reaction diagram Show all sequences 2.6.1.39-
Show all pathways known for 2.6.1.39Display the word mapDisplay the reaction diagram Show all sequences 2.6.1.39complexed with N-(5'-phosphopyridoxyl)-L-glutamate, vapor diffusion method, using 16% (w/v) PEG3350, 100 mM HEPES, pH 7.0, and 200 mM calcium acetate, at 20°C
Show all pathways known for 2.6.1.39Display the word mapDisplay the reaction diagram Show all sequences 2.6.1.39crystal structures of AAA-AT in four forms: with pyridoxal 5'-phosphate (PLP) (PLP complex), with PLP and leucine (PLP/Leu complex), with N-phosphopyridoxyl-leucine (PPL) (PPL complex), and with N-phosphopyridoxyl-alpha-aminoadipate (PPA) at 2.67, 2.26, 1.75, and 1.67 A resolution, respectively
Show all pathways known for 2.6.1.39Display the word mapDisplay the reaction diagram Show all sequences 2.6.1.39in complex with pyridoxal 5'-phosphate, with pyridoxal 5'-phosphate and leucine, with N-phosphopyridoxyl-leucine, and with N-phosphopyridoxyl-alpha-aminoadipate, at 2.67, 2.26, 1.75 and 1.67 A resolution, respectively. Enzyme contains a mobile alpha2-helix involved in substrate recognition
Show all pathways known for 2.6.1.39Display the word mapDisplay the reaction diagram Show all sequences 2.6.1.39to 1.91 A resolution, and comparison to alpha-aminoadipate aminotransferase LysN from Thermus thermophilus and human kynurenine aminotransferase II. The active site reveals asymmetric cofactor binding with lysine-pyridoxal-5-phosphate bound within the active site of one subunit in the Aro8 homodimer and pyridoxamine phosphate and a HEPES molecule bound to the other subunit. The HEPES buffer molecule binds within the substrate-binding site of Aro8
Results 1 - 5 of 5