LIS - Legume Information System
Information about legume traits for crop improvement
CicerMine
v5.1.0.3
Cicer data from the Legume Information System
v5.1.0.3
Cicer data from the Legume Information System
| Type | Family |
| Description | Synonym(s): Protohaem ferro-lyase, Iron chelatase, etc. Ferrochelatase is the terminal enzyme of the heme biosynthetic pathway. It catalyzes the insertion of ferrous iron into the protoporphyrin IX ring yielding protoheme. This enzyme is ubiquitous in nature and widely distributed in bacteria and eukaryotes. Recently, some archaeal members have been identified. The oligomeric state of these enzymes varies depending on the presence of a dimerization motif at the C terminus [ , , , , , , , , , , , ]. In eukaryotic cells, it binds to the mitochondrial inner membrane with its active site on the matrix side of the membrane.The X-ray structure of Bacillus subtilisand human ferrochelatase have been solved [ , ].The human enzyme exists as a homodimer. Each subunit contains one [2Fe-2S]cluster. The monomer is folded into two similar domains, each with a four-stranded parallelβ-sheet flanked by an α-helix in a beta-α-β motif that is reminiscent of the fold found in the periplasmic bindingproteins. The topological similarity between the domains suggests that they have arisen from a gene duplication event. However,significant differences exist between the two domains, including an N-terminal section (residues 80-130) that forms part of theactive site pocket, and a C-terminal extension (residues 390-423) that is involved in coordination of the [2Fe-2S]cluster and in stabilisation of the homodimer. Ferrochelatase seems to have a structurally conserved core region that is common to the enzyme from bacteria, plants and mammals. Porphyrin binds in the identified cleft; this cleft also includes the metal-binding site of the enzyme. It is likely that the structure of the cleft region will have different conformations upon substrate binding and release [ ]. |
| Short Name | Ferrochelatase |
