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Results 1 - 10 of 29 > >>
EC Number Subunits Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 1.1.2.7? x * 62000, alpha-subunit, + x * 7500, beta-subunit, SDS-PAGE -, 670785
Display the word mapDisplay the reaction diagram Show all sequences 1.1.2.7dimer 2 * 70000, SDS-PAGE -, 687432
Display the word mapDisplay the reaction diagram Show all sequences 1.1.2.7heterotetramer alpha2beta2, the MEDH heterotetramer is composed of two large subunits and two small subunits -, 723854, 724176
Display the word mapDisplay the reaction diagram Show all sequences 1.1.2.7monomer 1 * 18000, cytochrome cL, SDS-PAGE -, 763357
Display the word mapDisplay the reaction diagram Show all sequences 1.1.2.7monomer in contrast to other two-subunit pyrroloquinoline quinone-dependent quinoprotein methanol dehydrogenases, wide-spread in Burkholderiales, the enzyme from Methyloversatilis universalis strain FAM5 is a monosubunit protein -, 687417
Display the word mapDisplay the reaction diagram Show all sequences 1.1.2.7More in contrast to other two-subunit pyrroloquinoline quinone-dependent quinoprotein methanol dehydrogenases, wide-spread in Burkholderiales, the enzyme from Methylibium petroleiphilum strain PM1 is a monosubunit protein 687417
Display the word mapDisplay the reaction diagram Show all sequences 1.1.2.7More the alpha-subunit is known to function as the active site for the oxidoreduction reaction, which includes the PQQ group as a redox cofactor and a calcium ion coordinated to vicinal charged and hydrophobic amino-acid residues -, 723854
Display the word mapDisplay the reaction diagram Show all sequences 1.1.2.7More the enzyme shows a propeller structure, QMDH contains a disulfide structure that is similar to the analogous structure in QEDH, EC 1.1.5.5 -, 724402
Display the word mapDisplay the reaction diagram Show all sequences 1.1.2.7More the large alpha-subunit has a propeller fold making up a superbarrel of eight radially arranged beta-sheets, i.e. the propeller blades, containing the tryptophan-docking motifs that link together the eight beta-sheets, and the presence in the active site of a unique eight-membered disulfide ring structure formed from adjacent cysteine residues 103 and 104, joined by an atypical non-planar peptide bond 684666
Display the word mapDisplay the reaction diagram Show all sequences 1.1.2.7More the MxaJ molecule consists of nine alpha-helices (alpha1-alpha9) and six beta-strands (beta1-beta6), which are partitioned to form two globular domains (domain-1 and 2). The two domains are connected by a long and rigid beta-strand (beta3) at the center, and each domain has a different arrangement of alpha/beta secondary structural element. Detailed MxaJ structure analysis, overview -, 763672
Results 1 - 10 of 29 > >>