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Results 1 - 4 of 4
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EC Number Cofactor Commentary Reference
Show all pathways known for 2.6.1.79Display the reaction diagram Show all sequences 2.6.1.79pyridoxal 5'-phosphate - 659858, 660563, 759178
Show all pathways known for 2.6.1.79Display the reaction diagram Show all sequences 2.6.1.79pyridoxal 5'-phosphate PLP, dependent on, PLP is bound in the active site of each chain in the wild-type structure. In the AtPAT crystal structure, PLP is covalently linked to the epsilon-nitrogen of Lys306 to form the internal aldimine (i.e. Schiff base). Trp193 and Ile274 position the ring of PLP through pi-pi stacking and van der Waals interactions, respectively. The pyridine ring nitrogen of PLP forms a charge-charge interaction with the side chain of Asp272 759965
Show all pathways known for 2.6.1.79Display the reaction diagram Show all sequences 2.6.1.79pyridoxal 5'-phosphate required, stabilizes the enzyme 657635
Show all pathways known for 2.6.1.79Display the reaction diagram Show all sequences 2.6.1.79pyridoxal 5'-phosphate tightly bound to the enzyme 659858
Results 1 - 4 of 4
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