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<< < Results 21 - 29 of 29
EC Number Subunits Commentary Reference
Show all pathways known for 3.5.4.5Display the word mapDisplay the reaction diagram Show all sequences 3.5.4.5tetramer 4 * 15000, SDS-PAGE, purified enzyme, homotetramer 209665
Show all pathways known for 3.5.4.5Display the word mapDisplay the reaction diagram Show all sequences 3.5.4.5tetramer 4 * 16000, amino acid sequence 209665
Show all pathways known for 3.5.4.5Display the word mapDisplay the reaction diagram Show all sequences 3.5.4.5homotetramer 4 * 16600, calculated from amino acid sequence 711824
Show all pathways known for 3.5.4.5Display the word mapDisplay the reaction diagram Show all sequences 3.5.4.5homotetramer 4 * 20000, SDS-PAGE 711824
Show all pathways known for 3.5.4.5Display the word mapDisplay the reaction diagram Show all sequences 3.5.4.5dimer crystallization data, in the dimeric interface, residues Gly94, Ala95, Gln98, Thr100, Gly130, His131, Arg133, Gln134, Pro162, Asp163, Ala200, Asn234, Thr263 and Ile271 participate in hydrogen bonding or salt bridges -, 752690
Show all pathways known for 3.5.4.5Display the word mapDisplay the reaction diagram Show all sequences 3.5.4.5tetramer homotetramer 667736
Show all pathways known for 3.5.4.5Display the word mapDisplay the reaction diagram Show all sequences 3.5.4.5tetramer homotetramer, residue Y33 is involved in enzyme folding, enzyme structure analysis using circular dichroism, molecular modeling, overview 689935
Show all pathways known for 3.5.4.5Display the word mapDisplay the reaction diagram Show all sequences 3.5.4.5More wild-type tetramer dissociates into enzymatically inactive monomers, without intermediate forms via a non-cooperative transition. Extensive dialysis or dilution of the inativated mponomers restores completely the activity 657227
Show all pathways known for 3.5.4.5Display the word mapDisplay the reaction diagram Show all sequences 3.5.4.5? x * 20800, SDS-PAGE 734018
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