EC Number   |
Metals/Ions |
Reference |
|---|
   4.1.99.5 | Co2+ |
enzyme contains Co2+ that might be part of a Co2+-porphyrin |
648394 |
| 4.1.99.5 | Co2+ |
noncorrin-cobalt-containing enzyme, 1 Co-porphyrin per alphabeta pair of subunits |
648396 |
| 4.1.99.5 | Cu2+ |
probably a copper enzyme |
648395 |
| 4.1.99.5 | Fe2+ |
a ferritin-like protein with a dinuclear metal cofactor |
715293 |
| 4.1.99.5 | Fe2+ |
a nonheme di-iron enzyme |
746597 |
| 4.1.99.5 | Fe2+ |
dependent on |
726552 |
| 4.1.99.5 | Fe2+ |
di-iron center |
747409 |
| 4.1.99.5 | Fe2+ |
di-iron center, Glu144 is one of the iron-coordinating residues and plays a vital role in the catalytic reaction of cADO. The helix, in which Glu144 resides, exhibits two distinct conformations that correlate with the different binding states of the di-iron center in cADO structures. The highly labile feature of cADO di-iron center seems to be responsible for the low enzymatic activity. Six conservative amino acids, loctaed in two EX28-29EX2H motifs, from four helices (Glu32 from helix H1, Glu115 from helix H4, Glu60 and His63 from helix H2, and Glu144 and His147 from helix H5) act as metal ligands. The WT0 structure is characterized by losing the di-iron cluster and by exhibiting a distorted conformation of helix H5. This structure is likely to represent the inactive state of SeADO, as it has lost its cofactor iron |
749212 |
| 4.1.99.5 | Fe2+ |
di-iron center, the amount of hydrocarbons produced in recombinant Escherichia coli is decreased when the iron concentration in the M9 medium is decreased. The Cys-to-Ala/Ser mutations do not affect the iron binding to the enzyme |
749051 |
| 4.1.99.5 | Fe2+ |
di-iron centre, coordinated by two histidine residues and four carboxylates from glutamate side chains |
727312 |
