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Results 1 - 10 of 14 > >>
EC Number Subunits Commentary Reference
Show all pathways known for 1.14.15.1Display the word mapDisplay the reaction diagram Show all sequences 1.14.15.1? x * 47000, SDS-PAGE/Coomassie staining 702820
Show all pathways known for 1.14.15.1Display the word mapDisplay the reaction diagram Show all sequences 1.14.15.1? x * 47561.6, recombinant mutant R365L/E366Q, mass spectrometry, x * 47607.4, recombinant mutant C357U, mass spectrometry -, 746282
Show all pathways known for 1.14.15.1Display the word mapDisplay the reaction diagram Show all sequences 1.14.15.1monomer 1 * 46000 711268
Show all pathways known for 1.14.15.1Display the word mapDisplay the reaction diagram Show all sequences 1.14.15.1More cytochrome P450cam dimerizes via the formation of an intermolecular disulfide bond 347706
Show all pathways known for 1.14.15.1Display the word mapDisplay the reaction diagram Show all sequences 1.14.15.1More multi-component mixed function monooxygenase consisting of putidaredoxin reductase, MW 47000, putidaredoxin, MW 11700, cytochrome m, MW 50500, Pseudomonas putida PpG786, SDS-PAGE 347692
Show all pathways known for 1.14.15.1Display the word mapDisplay the reaction diagram Show all sequences 1.14.15.1More release of the substrate is caused both due to increased solubility of the substrate in solution in presence of alcohol and due to change in the tertiary structure of the active site of the enzyme, addition of alcohols to cytochrome P450cam causes a small change in the secondary structural elements but a significant change in the tertiary structural organization of the enzyme 671612
Show all pathways known for 1.14.15.1Display the word mapDisplay the reaction diagram Show all sequences 1.14.15.1More secondary structure analysis of wild-type and mutant C357M enzymes, overview 673071
Show all pathways known for 1.14.15.1Display the word mapDisplay the reaction diagram Show all sequences 1.14.15.1More secondary structure and localization of perturbation sites of cytochrome b5 and putidaredoxin, overview 672144
Show all pathways known for 1.14.15.1Display the word mapDisplay the reaction diagram Show all sequences 1.14.15.1More structural changes upon complex formation between enzyme and cofactor cause an increase in beta-sheets and alpha-helix content, a decrease in population of random coil/3 10-helix structure, a redistribution of turn structures within the interacting proteins and changes in the protonation states or hydrogen-bondonh of amino acid carboxylic side chains 672413
Show all pathways known for 1.14.15.1Display the word mapDisplay the reaction diagram Show all sequences 1.14.15.1More tertiary and secondary structure of the heme active site, overview 672083
Results 1 - 10 of 14 > >>