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Results 1 - 8 of 8
EC Number Metals/Ions Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 1.14.11.29Ca2+ the crystal structure reveals an EF domain with two Ca2+-binding motifs inserted within the catalytic domain. The proximity of the EF domain to the active site suggests that Ca2+ binding is relevant to the catalytic activity. Functional analysis demonstrates that Ca2+-binding affinity of P4H-TM is within the range of physiological Ca2+ concentration in the endoplasmic reticulum. P4H-TM is found both as a monomer and a dimer in the solution, but the monomer-dimer equilibrium is not regulated by Ca2+ 765073
Display the word mapDisplay the reaction diagram Show all sequences 1.14.11.29Fe2+ dependent on 724225, 724523, 724847, 726084
Display the word mapDisplay the reaction diagram Show all sequences 1.14.11.29Fe2+ dependent on, non-heme iron 725647, 725653
Display the word mapDisplay the reaction diagram Show all sequences 1.14.11.29Fe2+ required 701217, 725596, 741852
Display the word mapDisplay the reaction diagram Show all sequences 1.14.11.29Fe2+ required. the enzyme activity is inhibited by substitution of Fe2+ with Co2+ or Ni2+ 701218
Display the word mapDisplay the reaction diagram Show all sequences 1.14.11.29Fe2+ the catalytic site contained bound Fe2+ and N-oxalylglycine 765073
Display the word mapDisplay the reaction diagram Show all sequences 1.14.11.29Fe2+ the enzyme contains Fe2+ 701219
Display the word mapDisplay the reaction diagram Show all sequences 1.14.11.29Zn2+ the enzyme contains a zinc finger motif 743285
Results 1 - 8 of 8