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EC Number Cofactor Commentary Reference
Show all pathways known for 2.6.1.19Display the word mapDisplay the reaction diagram Show all sequences 2.6.1.19pyridoxal 5'-phosphate - 636963, 637032, 637033, 637046, 637049, 637050, 637051, 637052, 637054, 637056, 637057, 637058, 637062, 662255, 671175, 672536, 672609, 672615, 673052, 673585, 675313, 675667, 700887, 702606, 702914, 702961, 704874, 704882, 704969, 706140, 723611, 754623, 758692, 759240, 759852, 760153
Show all pathways known for 2.6.1.19Display the word mapDisplay the reaction diagram Show all sequences 2.6.1.19pyridoxal 5'-phosphate requirement, bound to lysine-residue 330 637048, 637076
Show all pathways known for 2.6.1.19Display the word mapDisplay the reaction diagram Show all sequences 2.6.1.19pyridoxal 5'-phosphate no activation by addition of pyridoxal phosphate, but sensitive to carbonyl reagents 637055
Show all pathways known for 2.6.1.19Display the word mapDisplay the reaction diagram Show all sequences 2.6.1.19pyridoxal 5'-phosphate 2 mol per mol enzyme 637059
Show all pathways known for 2.6.1.19Display the word mapDisplay the reaction diagram Show all sequences 2.6.1.19pyridoxal 5'-phosphate K357 is involved in binding 662869
Show all pathways known for 2.6.1.19Display the word mapDisplay the reaction diagram Show all sequences 2.6.1.19pyridoxal 5'-phosphate 0.1 mM 671915
Show all pathways known for 2.6.1.19Display the word mapDisplay the reaction diagram Show all sequences 2.6.1.19pyridoxal 5'-phosphate dependent 661332, 672598
Show all pathways known for 2.6.1.19Display the word mapDisplay the reaction diagram Show all sequences 2.6.1.19pyridoxal 5'-phosphate 0.01 mM 672849
Show all pathways known for 2.6.1.19Display the word mapDisplay the reaction diagram Show all sequences 2.6.1.19pyridoxal 5'-phosphate cofactor remains bound during purification 698627
Show all pathways known for 2.6.1.19Display the word mapDisplay the reaction diagram Show all sequences 2.6.1.19pyridoxal 5'-phosphate PLP, the PLP-GABA-binding pocket is located at the interface of the dimer formation and is composed of one alpha-helix (alpha4) with four loops (beta5-alpha5, beta7-alpha9, beta8-alpha10, and alpha12-alpha13). The positively charged pyridine nitrogen of PLP makes a salt bridge with the carboxylate group of Asp259. The hydroxyl group of the pyridine ring is hydrogen bonded with Gln262 and Lys288. Moreover, the pyridine ring is stabilized by being sandwiched between Tyr157 and Ile261, contributing to generation of van der Waals interactions. The phosphate group of PLP is stabilized by hydrogen bonds with the main chain nitrogen atoms of Gly130 and Ala131. The main chain of Thr317 from the neighboring monomer is also involved in hydrogen bonding with the phosphate group. The carboxylate group of GABA interacts with the N-terminus and the NE atom of Arg160, and Ile69 and Tyr157 form a substrate binding pocket. Ligand binding and binding site structure, overview 758736
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