EC Number |
Metals/Ions |
Reference |
---|
1.14.11.29 | Ca2+ |
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 |
1.14.11.29 | Fe2+ |
dependent on |
724225, 724523, 724847, 726084 |
1.14.11.29 | Fe2+ |
dependent on, non-heme iron |
725647, 725653 |
1.14.11.29 | Fe2+ |
required |
701217, 725596, 741852 |
1.14.11.29 | Fe2+ |
required. the enzyme activity is inhibited by substitution of Fe2+ with Co2+ or Ni2+ |
701218 |
1.14.11.29 | Fe2+ |
the catalytic site contained bound Fe2+ and N-oxalylglycine |
765073 |
1.14.11.29 | Fe2+ |
the enzyme contains Fe2+ |
701219 |
1.14.11.29 | Zn2+ |
the enzyme contains a zinc finger motif |
743285 |